Proposed Changes to the Enzyme List

References:

Karki, S., Yoo, H.G., Kwon, S.Y., Suh, J.W. and Kwon, H.J. Cloning and in vitro characterization of dTDP-6-deoxy-L-talose biosynthetic genes from Kitasatospora kifunensis featuring the dTDP-6-deoxy-L-lyxo-4-hexulose reductase that synthesizes dTDP-6-deoxy-L-talose. Carbohydr. Res. 345 (2010) 1958–1962. [DOI] [PMID: 20667525]

[EC 1.1.1.344 created 2013]

1.1.1.345

Accepted name:

D-2-hydroxyacid dehydrogenase (NAD⁺)

Reaction:

an (R)-2-hydroxycarboxylate + NAD⁺ = a 2-oxocarboxylate + NADH + H⁺

Other name(s):

LdhA; HdhD; D-2-hydroxyisocaproate dehydrogenase; R-HicDH; D-HicDH; (R)-2-hydroxy-4-methylpentanoate:NAD⁺ oxidoreductase; (R)-2-hydroxyisocaproate dehydrogenase; D-mandelate dehydrogenase (ambiguous)

Systematic name:

(R)-2-hydroxycarboxylate:NAD⁺ oxidoreductase

Comments:

The enzymes, characterized from bacteria (Peptoclostridium difficile, Enterococcus faecalis and from lactic acid bacteria) prefer substrates with a main chain of 5 carbons (such as 4-methyl-2-oxopentanoate) to those with a shorter chain. It also utilizes phenylpyruvate. The enzyme from the halophilic archaeon Haloferax mediterranei prefers substrates with a main chain of 3-4 carbons (pyruvate and 2-oxobutanoate). cf. EC 1.1.1.272, (D)-2-hydroxyacid dehydrogenase (NADP⁺).

Links to other databases:

References:

1.	Dengler, U., Niefind, K., Kiess, M. and Schomburg, D. Crystal structure of a ternary complex of D-2-hydroxyisocaproate dehydrogenase from Lactobacillus casei, NAD⁺ and 2-oxoisocaproate at 1.9 Å resolution. J. Mol. Biol. 267 (1997) 640–660. [DOI] [PMID: 9126843]
2.	Bonete, M.J., Ferrer, J., Pire, C., Penades, M. and Ruiz, J.L. 2-Hydroxyacid dehydrogenase from Haloferax mediterranei, a D-isomer-specific member of the 2-hydroxyacid dehydrogenase family. Biochimie 82 (2000) 1143–1150. [DOI] [PMID: 11120357]
3.	Kim, J., Darley, D., Selmer, T. and Buckel, W. Characterization of (R)-2-hydroxyisocaproate dehydrogenase and a family III coenzyme A transferase involved in reduction of L-leucine to isocaproate by Clostridium difficile. Appl. Environ. Microbiol. 72 (2006) 6062–6069. [DOI] [PMID: 16957230]
4.	Wada, Y., Iwai, S., Tamura, Y., Ando, T., Shinoda, T., Arai, K. and Taguchi, H. A new family of D-2-hydroxyacid dehydrogenases that comprises D-mandelate dehydrogenases and 2-ketopantoate reductases. Biosci. Biotechnol. Biochem. 72 (2008) 1087–1094. [DOI] [PMID: 18391442]
5.	Chambellon, E., Rijnen, L., Lorquet, F., Gitton, C., van Hylckama Vlieg, J.E., Wouters, J.A. and Yvon, M. The D-2-hydroxyacid dehydrogenase incorrectly annotated PanE is the sole reduction system for branched-chain 2-keto acids in Lactococcus lactis. J. Bacteriol. 191 (2009) 873–881. [DOI] [PMID: 19047348]
6.	Miyanaga, A., Fujisawa, S., Furukawa, N., Arai, K., Nakajima, M. and Taguchi, H. The crystal structure of D-mandelate dehydrogenase reveals its distinct substrate and coenzyme recognition mechanisms from those of 2-ketopantoate reductase. Biochem. Biophys. Res. Commun. 439 (2013) 109–114. [DOI] [PMID: 23954635]

[EC 1.1.1.345 created 2013]

1.1.1.346

Accepted name:

2,5-didehydrogluconate reductase (2-dehydro-L-gulonate-forming)

Reaction:

2-dehydro-L-gulonate + NADP⁺ = 2,5-didehydro-D-gluconate + NADPH + H⁺

Glossary:

2-dehydro-L-gulonate = 2-dehydro-L-idonate = 2-keto-L-gulonate

Other name(s):

2,5-diketo-D-gluconate-reductase (ambiguous); YqhE reductase; dkgA (gene name); dkgB (gene name)

Systematic name:

2-dehydro-D-gluconate:NADP⁺ 2-oxidoreductase (2-dehydro-L-gulonate-forming)

Comments:

The enzyme is involved in ketogluconate metabolism, and catalyses the reaction in vivo in the reverse direction to that shown [1]. It is used in the commercial microbial production of ascorbate. cf. EC 1.1.1.274, 2,5-didehydrogluconate reductase (2-dehydro-D-gluconate-forming).

Links to other databases:

References:

1.	Sonoyama, T. and Kobayashi, K. Purification and properties of two 2,5-diketo-D-gluconate reductases from a mutant strain derived from Corynebacterium sp. J Ferment Technol. 65 (1987) 311–317.
2.	Miller, J.V., Estell, D.A. and Lazarus, R.A. Purification and characterization of 2,5-diketo-D-gluconate reductase from Corynebacterium sp. J. Biol. Chem. 262 (1987) 9016–9020. [PMID: 3597405]
3.	Yum, D.Y., Lee, B.Y. and Pan, J.G. Identification of the yqhE and yafB genes encoding two 2,5-diketo-D-gluconate reductases in Escherichia coli. Appl. Environ. Microbiol. 65 (1999) 3341–3346. [PMID: 10427017]
4.	Maremonti, M., Greco, G. and Wichmann, R. Characterisation of 2,5-diketo-D-gluconic acid reductase from Corynebacterium sp. Biotechnology Letters 18 (1996) 845–850.
5.	Khurana, S., Powers, D.B., Anderson, S. and Blaber, M. Crystal structure of 2,5-diketo-D-gluconic acid reductase A complexed with NADPH at 2.1-Å resolution. Proc. Natl. Acad. Sci. USA 95 (1998) 6768–6773. [DOI] [PMID: 9618487]

[EC 1.1.1.346 created 2013]

1.3.1.26

Transferred entry:

dihydrodipicolinate reductase. Now EC 1.17.1.8, 4-hydroxy-tetrahydrodipicolinate reductase.

[EC 1.3.1.26 created 1976, modified 2011, deleted 2013]

1.3.1.98

Accepted name:

UDP-N-acetylmuramate dehydrogenase

Reaction:

UDP-N-acetyl-α-D-muramate + NADP⁺ = UDP-N-acetyl-3-O-(1-carboxyvinyl)-α-D-glucosamine + NADPH + H⁺

Other name(s):

MurB reductase; UDP-N-acetylenolpyruvoylglucosamine reductase; UDP-N-acetylglucosamine-enoylpyruvate reductase; UDP-GlcNAc-enoylpyruvate reductase; uridine diphosphoacetylpyruvoylglucosamine reductase; uridine diphospho-N-acetylglucosamine-enolpyruvate reductase; uridine-5′-diphospho-N-acetyl-2-amino-2-deoxy-3-O-lactylglucose:NADP-oxidoreductase

Systematic name:

UDP-N-acetyl-α-D-muramate:NADP⁺ oxidoreductase

Comments:

A flavoprotein (FAD). NADH can to a lesser extent replace NADPH.

Links to other databases:

BRENDA, EXPASY, Gene, KEGG, PDB, CAS registry number: 39307-28-3

References:

1.	Taku, A. and Anwar, R.A. Biosynthesis of uridine diphospho-N-acetylmuramic acid. IV. Activation of uridine diphospho-N-acetylenolpyruvylglucosamine reductase by monovalent cations. J. Biol. Chem. 248 (1973) 4971. [PMID: 4717533]
2.	Taku, A., Gunetileke, K.G. and Anwar, R.A. Biosynthesis of uridine diphospho-N-acetylmuramic acid. 3. Purification and properties of uridine diphospho-N-acetylenolpyruvyl-glucosamine reductase. J. Biol. Chem. 245 (1970) 5012–5016. [PMID: 4394163]
3.	van Heijenoort, J. Recent advances in the formation of the bacterial peptidoglycan monomer unit. Nat. Prod. Rep. 18 (2001) 503–519. [PMID: 11699883]

[EC 1.3.1.98 created 1976 as EC 1.1.1.158, modified 1983, modified 2002, transferred 2013 to EC 1.3.1.98]

1.3.1.99

Transferred entry:

iridoid synthase. Now known to be catalyzed by two different enzymes, EC 1.3.1.122, (S)-8-oxocitronellyl enol synthase, and EC 5.5.1.34, (+)-cis,trans-nepetalactol synthase

[EC 1.3.1.99 created 2013, deleted 2019]

1.5.1.46

Accepted name:

agroclavine dehydrogenase

Reaction:

agroclavine + NADP⁺ = 6,8-dimethyl-6,7,8,9-tetradehydroergoline + NADPH + H⁺

For diagram of ergot alkaloid biosynthesis, click here

Glossary:

agroclavine = 6,8-dimethyl-8,9-didehydroergoline

Other name(s):

easG (gene name)

Systematic name:

agroclavine:NADP⁺ oxidoreductase

Comments:

The enzyme participates in the biosynthesis of ergotamine, an ergot alkaloid produced by some fungi of the Clavicipitaceae family. The reaction is catalysed in the opposite direction to that shown. The substrate for the enzyme is an iminium intermediate that is formed spontaneously from chanoclavine-I aldehyde in the presence of glutathione.

Links to other databases:

References:

Matuschek, M., Wallwey, C., Xie, X. and Li, S.M. New insights into ergot alkaloid biosynthesis in Claviceps purpurea: an agroclavine synthase EasG catalyses, via a non-enzymatic adduct with reduced glutathione, the conversion of chanoclavine-I aldehyde to agroclavine. Org. Biomol. Chem. 9 (2011) 4328–4335. [DOI] [PMID: 21494745]

[EC 1.5.1.46 created 2013]

1.7.3.4

Transferred entry:

hydroxylamine oxidase. Now covered by EC 1.7.2.6, hydroxylamine dehydrogenase, and EC 1.7.3.6, hydroxylamine oxidase (cytochrome)

[EC 1.7.3.4 created 1972, deleted 2013]

1.7.3.6

Accepted name:

hydroxylamine oxidase (cytochrome)

Reaction:

hydroxylamine + O₂ = nitrite + H₂O + H⁺ (overall reaction)
(1a) hydroxylamine + 2 ferricytochrome c = nitroxyl + 2 ferrocytochrome c + 2 H⁺
(1b) nitroxyl + 2 ferrocytochrome c + O₂ + H⁺ = nitrite + 2 ferricytochrome c + H₂O (spontaneous)

Other name(s):

HAO (ambiguous); hydroxylamine oxidoreductase (ambiguous); hydroxylamine oxidase (misleading)

Systematic name:

hydroxylamine:oxygen oxidoreductase

Comments:

The enzyme from the heterotrophic nitrifying bacterium Paracoccus denitrificans contains three to five non-heme, non-iron-sulfur iron atoms and interacts with cytochrome c₅₅₆ and pseudoazurin [2,3]. Under anaerobic conditions in vitro only nitrous oxide is formed [3]. Presumably nitroxyl is released and combines with a second nitroxyl to give nitrous oxide and water. When oxygen is present, nitrite is formed.

Links to other databases:

BRENDA, EXPASY, KEGG, PDB, CAS registry number: 9075-43-8

References:

1.	Kurokawa, M, Fukumori, Y and Yamanaka, T A hydroxylamine - cytochrome c reductase occurs in the heterotrophic nitrifier Arthrobacter globiformis. Plant Cell Physiol. 26 (1985) 1439–1442.
2.	Wehrfritz, J.M., Reilly, A., Spiro, S. and Richardson, D.J. Purification of hydroxylamine oxidase from Thiosphaera pantotropha. Identification of electron acceptors that couple heterotrophic nitrification to aerobic denitrification. FEBS Lett. 335 (1993) 246–250. [DOI] [PMID: 8253206]
3.	Moir, J.W., Wehrfritz, J.M., Spiro, S. and Richardson, D.J. The biochemical characterization of a novel non-haem-iron hydroxylamine oxidase from Paracoccus denitrificans GB17. Biochem. J. 319 (1996) 823–827. [PMID: 8920986]
4.	Wehrfritz, J., Carter, J.P., Spiro, S. and Richardson, D.J. Hydroxylamine oxidation in heterotrophic nitrate-reducing soil bacteria and purification of a hydroxylamine-cytochrome c oxidoreductase from a Pseudomonas species. Arch. Microbiol. 166 (1996) 421–424. [PMID: 9082922]

[EC 1.7.3.6 created 1972 as EC 1.7.3.4, part transferred 2013 to EC 1.7.3.6, modified 2015]

*EC

1.11.1.6

Accepted name:

catalase

Reaction:

2 H₂O₂ = O₂ + 2 H₂O

Other name(s):

equilase; caperase; optidase; catalase-peroxidase; CAT

Systematic name:

hydrogen-peroxide:hydrogen-peroxide oxidoreductase

Comments:

A hemoprotein. A manganese protein containing Mn^III in the resting state, which also belongs here, is often called pseudocatalase. The enzymes from some organisms, such as Penicillium simplicissimum, can also act as a peroxidase (EC 1.11.1.7) for which several organic substances, especially ethanol, can act as a hydrogen donor. Enzymes that exhibit both catalase and peroxidase activity belong under EC 1.11.1.21, catalase-peroxidase.

Links to other databases:

BRENDA, EAWAG-BBD, EXPASY, Gene, KEGG, PDB, CAS registry number: 9001-05-2

References:

1.	Herbert, D. and Pinsent, J. Crystalline bacterial catalase. Biochem. J. 43 (1948) 193–202. [PMID: 16748386]
2.	Herbert, D. and Pinsent, J. Crystalline human erythrocyte catalase. Biochem. J. 43 (1948) 203–205. [PMID: 16748387]
3.	Keilin, D. and Hartree, E.F. Coupled oxidation of alcohol. Proc. R. Soc. Lond. B Biol. Sci. 119 (1936) 141–159.
4.	Kono, Y. and Fridovich, I. Isolation and characterization of the pseudocatalase of Lactobacillus plantarum. J. Biol. Chem. 258 (1983) 6015–6019. [PMID: 6853475]
5.	Nicholls, P. and Schonbaum, G.R. Catalases. In: Boyer, P.D., Lardy, H. and Myrbäck, K. (Ed.), The Enzymes, 2nd edn, vol. 8, Academic Press, New York, 1963, pp. 147–225.

[EC 1.11.1.6 created 1961, modified 1986, modified 1999, modified 2013]

1.11.1.22

Accepted name:

hydroperoxy fatty acid reductase

Reaction:

a hydroperoxy fatty acid + NADPH + H⁺ = a hydroxy fatty acid + NADP⁺ + H₂O

Other name(s):

slr1171 (gene name); slr1992 (gene name); hydroperoxy fatty acid:NADPH oxidoreductase

Systematic name:

NADPH:hydroperoxy fatty acid oxidoreductase

Comments:

The enzyme, characterized from the cyanobacterium Synechocystis PCC 6803, can reduce unsaturated fatty acid hydroperoxides and alkyl hydroperoxides. The enzyme, which utilizes NADPH generated by the photosynthetic electron transfer system, protects the cells from lipid peroxidation.

Links to other databases:

References:

1.	Gaber, A., Tamoi, M., Takeda, T., Nakano, Y. and Shigeoka, S. NADPH-dependent glutathione peroxidase-like proteins (Gpx-1, Gpx-2) reduce unsaturated fatty acid hydroperoxides in Synechocystis PCC 6803. FEBS Lett. 499 (2001) 32–36. [DOI] [PMID: 11418106]
2.	Gaber, A., Yoshimura, K., Tamoi, M., Takeda, T., Nakano, Y. and Shigeoka, S. Induction and functional analysis of two reduced nicotinamide adenine dinucleotide phosphate-dependent glutathione peroxidase-like proteins in Synechocystis PCC 6803 during the progression of oxidative stress. Plant Physiol. 136 (2004) 2855–2861. [DOI] [PMID: 15347790]

[EC 1.11.1.22 created 2013]

*EC

1.12.1.3

Accepted name:

hydrogen dehydrogenase (NADP⁺)

Reaction:

H₂ + NADP⁺ = H⁺ + NADPH

Other name(s):

NADP⁺-linked hydrogenase; NADP⁺-reducing hydrogenase; hydrogenase (ambiguous); hydrogenase I (ambiguous)

Systematic name:

hydrogen:NADP⁺ oxidoreductase

Comments:

The protein from the bacterium Desulfovibrio fructosovorans is an iron-sulfur protein that exclusively functions as a hydrogen dehydrogenase [1], while the enzyme from the archaeon Pyrococcus furiosus is a nickel, iron, iron-sulfur protein, that is part of a heterotetrameric complex where the α and δ subunits function as a hydrogenase while the β and γ subunits function as sulfur reductase (EC 1.12.98.4, sulfhydrogenase). Different from EC 1.12.1.5, hydrogen dehydrogenase [NAD(P)⁺].

Links to other databases:

BRENDA, EXPASY, Gene, KEGG, PDB, CAS registry number: 9027-05-8

References:

1.	de Luca, G., de Philip, P., Rousset, M., Belaich, J.P. and Dermoun, Z. The NADP-reducing hydrogenase of Desulfovibrio fructosovorans: Evidence for a native complex with hydrogen-dependent methyl-viologen-reducing activity. Biochem. Biophys. Res. Commun. 248 (1998) 591–596. [DOI] [PMID: 9703971]
2.	Bryant, F.O. and Adams, M.W. Characterization of hydrogenase from the hyperthermophilic archaebacterium, Pyrococcus furiosus. J. Biol. Chem. 264 (1989) 5070–5079. [PMID: 2538471]
3.	Ma, K., Schicho, R.N., Kelly, R.M. and Adams, M.W. Hydrogenase of the hyperthermophile Pyrococcus furiosus is an elemental sulfur reductase or sulfhydrogenase: evidence for a sulfur-reducing hydrogenase ancestor. Proc. Natl. Acad. Sci. USA 90 (1993) 5341–5344. [DOI] [PMID: 8389482]
4.	Ma, K., Zhou, Z.H. and Adams, M.W. Hydrogen production from pyruvate by enzymes purified from the hyperthermophilic archaeon, Pyrococcus furiosus: A key role for NADPH. FEMS Microbiol. Lett. 122 (1994) 245–250.
5.	van Haaster, D.J., Silva, P.J., Hagedoorn, P.L., Jongejan, J.A. and Hagen, W.R. Reinvestigation of the steady-state kinetics and physiological function of the soluble NiFe-hydrogenase I of Pyrococcus furiosus. J. Bacteriol. 190 (2008) 1584–1587. [DOI] [PMID: 18156274]

[EC 1.12.1.3 created 2002, modified 2013]

1.12.1.5

Accepted name:

hydrogen dehydrogenase [NAD(P)⁺]

Reaction:

H₂ + NAD(P)⁺ = H⁺ + NAD(P)H

Other name(s):

hydrogenase II (ambiguous)

Systematic name:

hydrogen:NAD(P)⁺ oxidoreductase

Comments:

A nickel, iron, iron-sulfur protein. The enzyme from the archaeon Pyrococcus furiosus is part of a heterotetrameric complex where the α and δ subunits function as a hydrogenase while the β and γ subunits function as sulfur reductase (EC 1.12.98.4, sulfhydrogenase). Different from EC 1.12.1.3, hydrogen dehydrogenase (NADP⁺).

Links to other databases:

References:

1.	Ma, K., Weiss, R. and Adams, M.W. Characterization of hydrogenase II from the hyperthermophilic archaeon Pyrococcus furiosus and assessment of its role in sulfur reduction. J. Bacteriol. 182 (2000) 1864–1871. [DOI] [PMID: 10714990]

[EC 1.12.1.5 created 2013]

1.12.98.4

Accepted name:

sulfhydrogenase

Reaction:

H₂ + (sulfide)_n = hydrogen sulfide + (sulfide)_n-1

Other name(s):

sulfur reductase

Systematic name:

H₂:polysulfide oxidoreductase

Comments:

An iron-sulfur protein. The enzyme from the hyperthermophilic archaeon Pyrococcus furiosus is part of two heterotetrameric complexes where the β and γ subunits function as sulfur reductase and the α and δ subunits function as hydrogenases (EC 1.12.1.3, hydrogen dehydrogenase [NADP⁺] and EC 1.12.1.4, hydrogen dehydrogenase [NAD(P)⁺], respectively). Sulfur can also be used as substrate, but since it is insoluble in aqueous solution and polysulfide is generated abiotically by the reaction of hydrogen sulfide and sulfur, polysulfide is believed to be the true substrate [2].

Links to other databases:

References:

1.	Zöphel, A., Kennedy, M.C., Beinert, H. and Kroneck, P.M.H. Investigations on microbial sulfur respiration. 1. Activation and reduction of elemental sulfur in several strains of Eubacteria. Arch. Microbiol. 150 (1988) 72–77.
2.	Ma, K., Schicho, R.N., Kelly, R.M. and Adams, M.W. Hydrogenase of the hyperthermophile Pyrococcus furiosus is an elemental sulfur reductase or sulfhydrogenase: evidence for a sulfur-reducing hydrogenase ancestor. Proc. Natl. Acad. Sci. USA 90 (1993) 5341–5344. [DOI] [PMID: 8389482]
3.	Ma, K., Zhou, Z.H. and Adams, M.W. Hydrogen production from pyruvate by enzymes purified from the hyperthermophilic archaeon, Pyrococcus furiosus: A key role for NADPH. FEMS Microbiol. Lett. 122 (1994) 245–250.
4.	Ma, K., Weiss, R. and Adams, M.W. Characterization of hydrogenase II from the hyperthermophilic archaeon Pyrococcus furiosus and assessment of its role in sulfur reduction. J. Bacteriol. 182 (2000) 1864–1871. [DOI] [PMID: 10714990]

[EC 1.12.98.4 created 1992 as EC 1.97.1.3, transferred 2013 to EC 1.12.98.4]

*EC

1.13.11.37

Accepted name:

hydroxyquinol 1,2-dioxygenase

Reaction:

hydroxyquinol + O₂ = maleylacetate

For diagram of 4-nitrophenol metabolism, click here

Glossary:

hydroxyquinol = 1,2,4-trihydroxybenzene
maleylacetate = (2Z)-4-oxohex-2-enedioate

Other name(s):

hydroxyquinol dioxygenase; benzene-1,2,4-triol:oxygen 1,2-oxidoreductase (decyclizing); benzene-1,2,4-triol:oxygen 1,2-oxidoreductase (ring-opening)

Systematic name:

hydroxyquinol:oxygen 1,2-oxidoreductase (ring-opening)

Comments:

An iron protein. Highly specific; catechol and pyrogallol are acted on at less than 1% of the rate at which hydroxyquinol is oxidized.

Links to other databases:

BRENDA, EAWAG-BBD, EXPASY, Gene, KEGG, PDB, CAS registry number: 91847-14-2

References:

1.	Sze, I.S.-Y. and Dagley, S. Properties of salicylate hydroxylase and hydroxyquinol 1,2-dioxygenase purified from Trichosporon cutaneum. J. Bacteriol. 159 (1984) 353–359. [PMID: 6539772]
2.	Ferraroni, M., Seifert, J., Travkin, V.M., Thiel, M., Kaschabek, S., Scozzafava, A., Golovleva, L., Schlomann, M. and Briganti, F. Crystal structure of the hydroxyquinol 1,2-dioxygenase from Nocardioides simplex 3E, a key enzyme involved in polychlorinated aromatics biodegradation. J. Biol. Chem. 280 (2005) 21144–21154. [DOI] [PMID: 15772073]
3.	Hatta, T., Nakano, O., Imai, N., Takizawa, N. and Kiyohara, H. Cloning and sequence analysis of hydroxyquinol 1,2-dioxygenase gene in 2,4,6-trichlorophenol-degrading Ralstonia pickettii DTP0602 and characterization of its product. J. Biosci. Bioeng. 87 (1999) 267–272. [DOI] [PMID: 16232466]

[EC 1.13.11.37 created 1989, modified 2013]

1.13.12.20

Accepted name:

noranthrone monooxygenase

Reaction:

norsolorinic acid anthrone + O₂ = norsolorinic acid + H₂O

For diagram of aflatoxin biosynthesis (part 1), click here

Glossary:

norsolorinic acid anthrone = noranthrone = 2-hexanoyl-1,3,6,8-tetrahydroxyanthracen-9(10H)-one
norsolorinate = 2-hexanoyl-1,3,6,8-tetrahydroxy-9,10-anthraquinone

Other name(s):

norsolorinate anthrone oxidase

Systematic name:

norsolorinic acid anthrone:oxygen 9-oxidoreductase (norsolorinic acid-forming)

Comments:

Involved in the synthesis of aflatoxins in the fungus Aspergillus parasiticus.

Links to other databases:

References:

1.	Ehrlich, K.C., Li, P., Scharfenstein, L. and Chang, P.K. HypC, the anthrone oxidase involved in aflatoxin biosynthesis. Appl. Environ. Microbiol. 76 (2010) 3374–3377. [DOI] [PMID: 20348292]

[EC 1.13.12.20 created 2013]

*EC

1.14.13.70

Transferred entry:

sterol 14α-demethylase. Now EC 1.14.14.154, sterol 14α-demethylase

[EC 1.14.13.70 created 2001, modified 2013, deleted 2018]

*EC

1.14.15.6

Accepted name:

cholesterol monooxygenase (side-chain-cleaving)

Reaction:

cholesterol + 6 reduced adrenodoxin + 3 O₂ + 6 H⁺ = pregnenolone + 4-methylpentanal + 6 oxidized adrenodoxin + 4 H₂O (overall reaction)
(1a) cholesterol + 2 reduced adrenodoxin + O₂ + 2 H⁺ = (22R)-22-hydroxycholesterol + 2 oxidized adrenodoxin + H₂O
(1b) (22R)-22-hydroxycholesterol + 2 reduced adrenodoxin + O₂ + 2 H⁺ = (20R,22R)-20,22-dihydroxycholesterol + 2 oxidized adrenodoxin + H₂O
(1c) (20R,22R)-20,22-dihydroxy-cholesterol + 2 reduced adrenodoxin + O₂ + 2 H⁺ = pregnenolone + 4-methylpentanal + 2 oxidized adrenodoxin + 2 H₂O

Other name(s):

cholesterol desmolase; cytochrome P-450_scc; C₂₇-side chain cleavage enzyme; cholesterol 20-22-desmolase; cholesterol C_20-22 desmolase; cholesterol side-chain cleavage enzyme; cholesterol side-chain-cleaving enzyme; steroid 20-22 desmolase; steroid 20-22-lyase; CYP11A1 (gene name)

Systematic name:

cholesterol,reduced-adrenodoxin:oxygen oxidoreductase (side-chain-cleaving)

Comments:

A heme-thiolate protein (cytochrome P-450). The reaction proceeds in three stages, with two hydroxylations at C-22 and C-20 preceding scission of the side-chain between carbons 20 and 22. The initial source of the electrons is NADPH, which transfers the electrons to the adrenodoxin via EC 1.18.1.6, adrenodoxin-NADP⁺ reductase.

Links to other databases:

BRENDA, EXPASY, Gene, KEGG, PDB, CAS registry number: 37292-81-2, 440354-98-3

References:

1.	Burstein, S., Middleditch, B.S. and Gut, M. Mass spectrometric study of the enzymatic conversion of cholesterol to (22R)-22-hydroxycholesterol, (20R,22R)-20,22-dihydroxycholesterol, and pregnenolone, and of (22R)-22-hydroxycholesterol to the lgycol and pregnenolone in bovine adrenocortical preparations. Mode of oxygen incorporation. J. Biol. Chem. 250 (1975) 9028–9037. [PMID: 1238395]
2.	Hanukoglu, I., Spitsberg, V., Bumpus, J.A., Dus, K.M. and Jefcoate, C.R. Adrenal mitochondrial cytochrome P-450_scc. Cholesterol and adrenodoxin interactions at equilibrium and during turnover. J. Biol. Chem. 256 (1981) 4321–4328. [PMID: 7217084]
3.	Hanukoglu, I. and Hanukoglu, Z. Stoichiometry of mitochondrial cytochromes P-450, adrenodoxin and adrenodoxin reductase in adrenal cortex and corpus luteum. Implications for membrane organization and gene regulation. Eur. J. Biochem. 157 (1986) 27–31. [DOI] [PMID: 3011431]
4.	Strushkevich, N., MacKenzie, F., Cherkesova, T., Grabovec, I., Usanov, S. and Park, H.W. Structural basis for pregnenolone biosynthesis by the mitochondrial monooxygenase system. Proc. Natl. Acad. Sci. USA 108 (2011) 10139–10143. [DOI] [PMID: 21636783]
5.	Mast, N., Annalora, A.J., Lodowski, D.T., Palczewski, K., Stout, C.D. and Pikuleva, I.A. Structural basis for three-step sequential catalysis by the cholesterol side chain cleavage enzyme CYP11A1. J. Biol. Chem. 286 (2011) 5607–5613. [DOI] [PMID: 21159775]

[EC 1.14.15.6 created 1983, modified 2013, modified 2014]

1.14.15.12

Transferred entry:

pimeloyl-[acyl-carrier protein] synthase. Now EC 1.14.14.46, pimeloyl-[acyl-carrier protein] synthase

[EC 1.14.15.12 created 2013, deleted 2017]

*EC

1.14.99.9

Transferred entry:

steroid 17α-monooxygenase, now classified as EC 1.14.14.19, steroid 17α-monooxygenase

[EC 1.14.99.9 created 1961 as EC 1.99.1.9, transferred 1965 to EC 1.14.1.7, transferred 1972 to EC 1.14.99.9, modified 2013, deleted 2015]

*EC

1.14.99.10

Transferred entry:

steroid 21-monooxygenase. Now EC 1.14.14.16, steroid 21-monooxygenase

[EC 1.14.99.10 created 1961 as EC 1.99.1.11, transferred 1965 to EC 1.14.1.8, transferred 1972 to EC 1.14.99.10, modified 2013, deleted 2015]

1.17.1.8

Accepted name:

4-hydroxy-tetrahydrodipicolinate reductase

Reaction:

(S)-2,3,4,5-tetrahydropyridine-2,6-dicarboxylate + NAD(P)⁺ + H₂O = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + NAD(P)H + H⁺

For diagram of lysine biosynthesis (early stages), click here

Glossary:

(2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydropyridine-2,6-dicarboxylate
(S)-2,3,4,5-tetrahydropyridine-2,6-dicarboxylate = (2S)-2,3,4,5-tetrahydrodipicolinate

Other name(s):

dihydrodipicolinate reductase (incorrect); dihydrodipicolinic acid reductase (incorrect); 2,3,4,5-tetrahydrodipicolinate:NAD(P)⁺ oxidoreductase (incorrect); dapB (gene name)

Systematic name:

(S)-2,3,4,5-tetrahydropyridine-2,6-dicarboxylate:NAD(P)⁺ 4-oxidoreductase

Comments:

The substrate of the enzyme was initially thought to be (S)-2,3-dihydrodipicolinate [1], and the enzyme was classified accordingly as EC 1.3.1.26, dihydrodipicolinate reductase. Later studies of the enzyme from the bacterium Escherichia coli have suggested that the actual substrate of the enzyme is (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate, and that its activity includes a dehydration step [2], and thus the enzyme has been reclassified as 4-hydroxy-tetrahydrodipicolinate reductase. However, the identity of the substrate is still controversial, as more recently it has been suggested that it may be (S)-2,3-dihydrodipicolinate after all [3].

Links to other databases:

References:

1.	Farkas, W. and Gilvarg, C. The reduction step in diaminopimelic acid biosynthesis. J. Biol. Chem. 240 (1965) 4717–4722. [PMID: 4378965]
2.	Devenish, S.R., Blunt, J.W. and Gerrard, J.A. NMR studies uncover alternate substrates for dihydrodipicolinate synthase and suggest that dihydrodipicolinate reductase is also a dehydratase. J. Med. Chem. 53 (2010) 4808–4812. [DOI] [PMID: 20503968]
3.	Karsten, W.E., Nimmo, S.A., Liu, J. and Chooback, L. Identification of 2,3-dihydrodipicolinate as the product of the dihydrodipicolinate synthase reaction from Escherichia coli. Arch. Biochem. Biophys. 653 (2018) 50–62. [PMID: 29944868]

[EC 1.17.1.8 created 1976 as EC 1.3.1.26, transferred 2013 to EC 1.17.1.8, modified 2020]

1.23 Reducing C-O-C group as acceptor

1.23.1 With NADH or NADPH as donor (only sub-subclass identified to date)

1.23.1.1

Accepted name:

(+)-pinoresinol reductase

Reaction:

(+)-lariciresinol + NADP⁺ = (+)-pinoresinol + NADPH + H⁺

For diagram of matairesinol biosynthesis, click here

Glossary:

(+)-lariciresinol = 4-[(2S,3R,4R)-4-[(4-hydroxy-3-methoxyphenyl)methyl]-3-(hydroxymethyl)oxolan-2-yl]-2-methoxyphenol
(+)-pinoresinol = (1S,3aR,4S,6aR)-4,4-(tetrahydro-1H,3H-furo[3,4-c]furan-1,4-diyl)bis(2-methoxyphenol)

Other name(s):

pinoresinol/lariciresinol reductase; pinoresinol-lariciresinol reductases; (+)-pinoresinol/(+)-lariciresinol; (+)-pinoresinol-(+)-lariciresinol reductase; PLR

Systematic name:

(+)-lariciresinol:NADP⁺ oxidoreductase

Comments:

The reaction is catalysed in vivo in the opposite direction to that shown. A multifunctional enzyme that further reduces the product to the lignan (–)-secoisolariciresinol [EC 1.23.1.2, (+)-lariciresinol reductase]. Isolated from the plants Forsythia intermedia [1,2], Thuja plicata (western red cedar) [3], Linum perenne (perennial flax) [5] and Linum corymbulosum [6]. The 4-pro-R hydrogen of NADH is transferred to the 7-pro-R position of lariciresinol [1].

Links to other databases:

References:

1.	Chu, A., Dinkova, A., Davin, L.B., Bedgar, D.L. and Lewis, N.G. Stereospecificity of (+)-pinoresinol and (+)-lariciresinol reductases from Forsythia intermedia. J. Biol. Chem. 268 (1993) 27026–27033. [PMID: 8262939]
2.	Dinkova-Kostova, A.T., Gang, D.R., Davin, L.B., Bedgar, D.L., Chu, A. and Lewis, N.G. (+)-Pinoresinol/(+)-lariciresinol reductase from Forsythia intermedia. Protein purification, cDNA cloning, heterologous expression and comparison to isoflavone reductase. J. Biol. Chem. 271 (1996) 29473–29482. [DOI] [PMID: 8910615]
3.	Fujita, M., Gang, D.R., Davin, L.B. and Lewis, N.G. Recombinant pinoresinol-lariciresinol reductases from western red cedar (Thuja plicata) catalyze opposite enantiospecific conversions. J. Biol. Chem. 274 (1999) 618–627. [DOI] [PMID: 9872995]
4.	Min, T., Kasahara, H., Bedgar, D.L., Youn, B., Lawrence, P.K., Gang, D.R., Halls, S.C., Park, H., Hilsenbeck, J.L., Davin, L.B., Lewis, N.G. and Kang, C. Crystal structures of pinoresinol-lariciresinol and phenylcoumaran benzylic ether reductases and their relationship to isoflavone reductases. J. Biol. Chem. 278 (2003) 50714–50723. [DOI] [PMID: 13129921]
5.	Hemmati, S., Schmidt, T.J. and Fuss, E. (+)-Pinoresinol/(-)-lariciresinol reductase from Linum perenne Himmelszelt involved in the biosynthesis of justicidin B. FEBS Lett. 581 (2007) 603–610. [DOI] [PMID: 17257599]
6.	Bayindir, Ü., Alfermann, A.W. and Fuss, E. Hinokinin biosynthesis in Linum corymbulosum Reichenb. Plant J. 55 (2008) 810–820. [DOI] [PMID: 18489708]

[EC 1.23.1.1 created 2013]

1.23.1.2

Accepted name:

(+)-lariciresinol reductase

Reaction:

(–)-secoisolariciresinol + NADP⁺ = (+)-lariciresinol + NADPH + H⁺

For diagram of matairesinol biosynthesis, click here

Glossary:

(+)-lariciresinol = 4-[(2S,3R,4R)-4-[(4-hydroxy-3-methoxyphenyl)methyl]-3-(hydroxymethyl)oxolan-2-yl]-2-methoxyphenol
(–)-secoisolariciresinol = (2R,3R)-2,3-bis[(4-hydroxy-3-methoxyphenyl)methyl]butane-1,4-diol

Other name(s):

pinoresinol/lariciresinol reductase; pinoresinol-lariciresinol reductases; (+)-pinoresinol/(+)-lariciresinol; (+)-pinoresinol-(+)-lariciresinol reductase; PLR

Systematic name:

(–)-secoisolariciresinol:NADP⁺ oxidoreductase

Comments:

The reaction is catalysed in vivo in the opposite direction to that shown. A multifunctional enzyme that also reduces (+)-pinoresinol [EC 1.23.1.1, (+)-pinoresinol reductase]. Isolated from the plants Forsythia intermedia [1,2], Thuja plicata (western red cedar) [3], Linum perenne (perennial flax) [5] and Linum corymbulosum [6].

Links to other databases:

References:

1.	Chu, A., Dinkova, A., Davin, L.B., Bedgar, D.L. and Lewis, N.G. Stereospecificity of (+)-pinoresinol and (+)-lariciresinol reductases from Forsythia intermedia. J. Biol. Chem. 268 (1993) 27026–27033. [PMID: 8262939]
2.	Dinkova-Kostova, A.T., Gang, D.R., Davin, L.B., Bedgar, D.L., Chu, A. and Lewis, N.G. (+)-Pinoresinol/(+)-lariciresinol reductase from Forsythia intermedia. Protein purification, cDNA cloning, heterologous expression and comparison to isoflavone reductase. J. Biol. Chem. 271 (1996) 29473–29482. [DOI] [PMID: 8910615]
3.	Fujita, M., Gang, D.R., Davin, L.B. and Lewis, N.G. Recombinant pinoresinol-lariciresinol reductases from western red cedar (Thuja plicata) catalyze opposite enantiospecific conversions. J. Biol. Chem. 274 (1999) 618–627. [DOI] [PMID: 9872995]
4.	Min, T., Kasahara, H., Bedgar, D.L., Youn, B., Lawrence, P.K., Gang, D.R., Halls, S.C., Park, H., Hilsenbeck, J.L., Davin, L.B., Lewis, N.G. and Kang, C. Crystal structures of pinoresinol-lariciresinol and phenylcoumaran benzylic ether reductases and their relationship to isoflavone reductases. J. Biol. Chem. 278 (2003) 50714–50723. [DOI] [PMID: 13129921]
5.	Hemmati, S., Schmidt, T.J. and Fuss, E. (+)-Pinoresinol/(-)-lariciresinol reductase from Linum perenne Himmelszelt involved in the biosynthesis of justicidin B. FEBS Lett. 581 (2007) 603–610. [DOI] [PMID: 17257599]
6.	Bayindir, Ü., Alfermann, A.W. and Fuss, E. Hinokinin biosynthesis in Linum corymbulosum Reichenb. Plant J. 55 (2008) 810–820. [DOI] [PMID: 18489708]

[EC 1.23.1.2 created 2013]

1.23.1.3

Accepted name:

(–)-pinoresinol reductase

Reaction:

(–)-lariciresinol + NADP⁺ = (–)-pinoresinol + NADPH + H⁺

For diagram of (–)-lariciresinol biosynthesis, click here

Glossary:

(–)-lariciresinol = 4-[(2R,3S,4S)-4-[(4-hydroxy-3-methoxyphenyl)methyl]-3-(hydroxymethyl)oxolan-2-yl]-2-methoxyphenol
(–)-pinoresinol = (1R,3aS,4R,6aS)-4,4′-(tetrahydro-1H,3H-furo[3,4-c]furan-1,4-diyl)bis(2-methoxyphenol)

Other name(s):

pinoresinol/lariciresinol reductase; pinoresinol-lariciresinol reductases; (–)-pinoresinol-(–)-lariciresinol reductase; PLR

Systematic name:

(–)-lariciresinol:NADP⁺ oxidoreductase

Comments:

The reaction is catalysed in vivo in the opposite direction to that shown. A multifunctional enzyme that usually further reduces the product to (+)-secoisolariciresinol [EC 1.23.1.4, (–)-lariciresinol reductase]. Isolated from the plants Thuja plicata (western red cedar) [1], Linum perenne (perennial flax) [2] and Arabidopsis thaliana (thale cress) [3].

Links to other databases:

References:

1.	Fujita, M., Gang, D.R., Davin, L.B. and Lewis, N.G. Recombinant pinoresinol-lariciresinol reductases from western red cedar (Thuja plicata) catalyze opposite enantiospecific conversions. J. Biol. Chem. 274 (1999) 618–627. [DOI] [PMID: 9872995]
2.	Hemmati, S., Schmidt, T.J. and Fuss, E. (+)-Pinoresinol/(-)-lariciresinol reductase from Linum perenne Himmelszelt involved in the biosynthesis of justicidin B. FEBS Lett. 581 (2007) 603–610. [DOI] [PMID: 17257599]
3.	Nakatsubo, T., Mizutani, M., Suzuki, S., Hattori, T. and Umezawa, T. Characterization of Arabidopsis thaliana pinoresinol reductase, a new type of enzyme involved in lignan biosynthesis. J. Biol. Chem. 283 (2008) 15550–15557. [DOI] [PMID: 18347017]

[EC 1.23.1.3 created 2013]

1.23.1.4

Accepted name:

(–)-lariciresinol reductase

Reaction:

(+)-secoisolariciresinol + NADP⁺ = (–)-lariciresinol + NADPH + H⁺

For diagram of (#150)-lariciresinol biosynthesis, click here

Glossary:

(–)-lariciresinol = 4-[(2R,3S,4S)-4-[(4-hydroxy-3-methoxyphenyl)methyl]-3-(hydroxymethyl)oxolan-2-yl]-2-methoxyphenol
(+)-secoisolariciresinol = (2S,3S)-2,3-bis[(4-hydroxy-3-methoxyphenyl)methyl]butane-1,4-diol

Other name(s):

pinoresinol/lariciresinol reductase; pinoresinol-lariciresinol reductases; (–)-pinoresinol-(–)-lariciresinol reductase; PLR

Systematic name:

(+)-secoisolariciresinol:NADP⁺ oxidoreductase

Comments:

The reaction is catalysed in vivo in the opposite direction to that shown. A multifunctional enzyme that also reduces (–)-pinoresinol [EC 1.23.1.3, (–)-pinoresinol reductase]. Isolated from the plants Thuja plicata (western red cedar) [1] and Linum corymbulosum [2].

Links to other databases:

References:

1.	Fujita, M., Gang, D.R., Davin, L.B. and Lewis, N.G. Recombinant pinoresinol-lariciresinol reductases from western red cedar (Thuja plicata) catalyze opposite enantiospecific conversions. J. Biol. Chem. 274 (1999) 618–627. [DOI] [PMID: 9872995]
2.	Hemmati, S., Schmidt, T.J. and Fuss, E. (+)-Pinoresinol/(-)-lariciresinol reductase from Linum perenne Himmelszelt involved in the biosynthesis of justicidin B. FEBS Lett. 581 (2007) 603–610. [DOI] [PMID: 17257599]

[EC 1.23.1.4 created 2013]

1.97.1.3

Transferred entry:

sulfur reductase. Now EC 1.12.98.4, sulfhydrogenase, since hydrogen is known to be the electron donor.

[EC 1.97.1.3 created 1992, deleted 2013]

*EC

2.1.1.132

Accepted name:

precorrin-6B C5,15-methyltransferase (decarboxylating)

Reaction:

2 S-adenosyl-L-methionine + precorrin-6B = 2 S-adenosyl-L-homocysteine + precorrin-8X + CO₂ (overall reaction)
(1a) S-adenosyl-L-methionine + precorrin-6B = S-adenosyl-L-homocysteine + precorrin-7 + CO₂
(1b) S-adenosyl-L-methionine + precorrin-7 = S-adenosyl-L-homocysteine + precorrin-8X

For diagram of corrin biosynthesis (part 4), click here

Glossary:

precorrin-6B = precorrin-6Y

Other name(s):

precorrin-6 methyltransferase; precorrin-6Y methylase; precorrin-6Y C^5,15-methyltransferase (decarboxylating); cobL (gene name)

Systematic name:

S-adenosyl-L-methionine:1-precorrin-6B C^5,15-methyltransferase (C-12-decarboxylating)

Comments:

The enzyme participates in the aerobic (late cobalt insertion) adenosylcobalamin biosynthesis pathway. The enzyme from the bacterium Pseudomonas denitrificans is a fusion protein with two active sites; one catalyses the methylation at C-15 followed by decarboxylation of the C-12 acetate side chain, while the other catalyses the methylation at C-5. The corresponding activities in the anaerobic adenosylcobalamin biosynthesis pathway are catalysed by EC 2.1.1.196, cobalt-precorrin-6B (C15)-methyltransferase [decarboxylating], and EC 2.1.1.289, cobalt-precorrin-7 (C5)-methyltransferase, respectively.

Links to other databases:

BRENDA, EXPASY, Gene, KEGG, PDB, CAS registry number: 162995-22-4

References:

1.	Blanche, F., Famechon, A., Thibaut, D., Debussche, L., Cameron, B., Crouzet, J. Biosynthesis of vitamin B₁₂ in Pseudomonas denitrificans: the biosynthetic sequence from precorrin-6Y to precorrin-8X is catalyzed by the cobL gene product. J. Bacteriol. 174 (1992) 1050–1052. [DOI] [PMID: 1732195]
2.	Deery, E., Schroeder, S., Lawrence, A.D., Taylor, S.L., Seyedarabi, A., Waterman, J., Wilson, K.S., Brown, D., Geeves, M.A., Howard, M.J., Pickersgill, R.W. and Warren, M.J. An enzyme-trap approach allows isolation of intermediates in cobalamin biosynthesis. Nat. Chem. Biol. 8 (2012) 933–940. [DOI] [PMID: 23042036]

[EC 2.1.1.132 created 1999, modified 2013]

2.1.1.149

Deleted entry:

myricetin O-methyltransferase. Now covered by EC 2.1.1.267, flavonoid 3′,5′-methyltransferase.

[EC 2.1.1.149 created 2003, modified 2011, deleted 2013]

2.1.1.266

Accepted name:

23S rRNA (adenine²⁰³⁰-N⁶)-methyltransferase

Reaction:

S-adenosyl-L-methionine + adenine²⁰³⁰ in 23S rRNA = S-adenosyl-L-homocysteine + N⁶-methyladenine²⁰³⁰ in 23S rRNA

Other name(s):

YhiR protein; rlmJ (gene name); m⁶A²⁰³⁰ methyltransferase

Systematic name:

S-adenosyl-L-methionine:23S rRNA (adenine²⁰³⁰-N⁶)-methyltransferase

Comments:

The recombinant RlmJ protein is most active in methylating deproteinized 23S ribosomal subunit, and does not methylate the completely assembled 50S subunits [1].

Links to other databases:

References:

Golovina, A.Y., Dzama, M.M., Osterman, I.A., Sergiev, P.V., Serebryakova, M.V., Bogdanov, A.A. and Dontsova, O.A. The last rRNA methyltransferase of E. coli revealed: the yhiR gene encodes adenine-N6 methyltransferase specific for modification of A²⁰³⁰ of 23S ribosomal RNA. RNA 18 (2012) 1725–1734. [DOI] [PMID: 22847818]

[EC 2.1.1.266 created 2013]

2.1.1.267

Accepted name:

flavonoid 3′,5′-methyltransferase

Reaction:

(1) S-adenosyl-L-methionine + a 3′-hydroxyflavonoid = S-adenosyl-L-homocysteine + a 3′-methoxyflavonoid
(2) S-adenosyl-L-methionine + a 5′-hydroxy-3′-methoxyflavonoid = S-adenosyl-L-homocysteine + a 3′,5′-dimethoxyflavonoid

For diagram of anthocyanidin glucoside biosynthesis, click here

Glossary:

delphinidin = 3,3′,4′,5,5′,7-hexahydroxyflavylium
cyanidin = 3,3′,4′,5,7-pentahydroxyflavylium
myricetin = 3,3′,4′,5,5′,7-hexahydroxyflavone
quercetin = 3,3′,4′,5,7-pentahydroxyflavone

Other name(s):

AOMT; CrOMT2

Systematic name:

S-adenosyl-L-methionine:flavonoid 3′-O-methyltransferase

Comments:

Isolated from Vitis vinifera (grape) [2]. Most active with delphinidin 3-glucoside but also acts on cyanidin 3-glucoside, cyanidin, myricetin, quercetin and quercetin 3-glucoside. The enzyme from Catharanthus roseus was most active with myricetin [1].

Links to other databases:

References:

1.	Cacace, S., Schröder, G., Wehinger, E., Strack, D., Schmidt, J. and Schröder, J. A flavonol O-methyltransferase from Catharanthus roseus performing two sequential methylations. Phytochemistry 62 (2003) 127–137. [DOI] [PMID: 12482447]
2.	Hugueney, P., Provenzano, S., Verries, C., Ferrandino, A., Meudec, E., Batelli, G., Merdinoglu, D., Cheynier, V., Schubert, A. and Ageorges, A. A novel cation-dependent O-methyltransferase involved in anthocyanin methylation in grapevine. Plant Physiol. 150 (2009) 2057–2070. [DOI] [PMID: 19525322]

[EC 2.1.1.267 created 2013, modified 2014]

2.1.1.268

Accepted name:

tRNA^Thr (cytosine³²-N³)-methyltransferase

Reaction:

(1) S-adenosyl-L-methionine + cytosine³² in tRNA^Thr = S-adenosyl-L-homocysteine + N³-methylcytosine³² in tRNA^Thr
(2) S-adenosyl-L-methionine + cytosine³² in tRNA^Ser = S-adenosyl-L-homocysteine + N³-methylcytosine³² in tRNA^Ser

Other name(s):

ABP140; Trm140p

Systematic name:

S-adenosyl-L-methionine:tRNA^Thr (cytosine³²-N³)-methyltransferase

Comments:

The enzyme from Saccharomyces cerevisiae specifically methylates cytosine³² in tRNA^Thr and in tRNA^Ser.

Links to other databases:

References:

1.	Noma, A., Yi, S., Katoh, T., Takai, Y., Suzuki, T. and Suzuki, T. Actin-binding protein ABP140 is a methyltransferase for 3-methylcytidine at position 32 of tRNAs in Saccharomyces cerevisiae. RNA 17 (2011) 1111–1119. [DOI] [PMID: 21518805]
2.	D'Silva, S., Haider, S.J. and Phizicky, E.M. A domain of the actin binding protein Abp140 is the yeast methyltransferase responsible for 3-methylcytidine modification in the tRNA anti-codon loop. RNA 17 (2011) 1100–1110. [DOI] [PMID: 21518804]

[EC 2.1.1.268 created 2013]

*EC

2.3.1.25

Accepted name:

plasmalogen synthase

Reaction:

acyl-CoA + 1-O-(alk-1-enyl)glycero-3-phosphocholine = CoA + plasmenylcholine

Glossary:

1-O-(alk-1-enyl)glycero-3-phosphocholine = 1-alkenylglycerophosphocholine,
plasmenylcholine = 1-alkenyl-2-acylglycerophosphocholine

Other name(s):

lysoplasmenylcholine acyltransferase; O-1-alkenylglycero-3-phosphorylcholine acyltransferase; 1-alkenyl-glycero-3-phosphorylcholine:acyl-CoA acyltransferase; 1-alkenylglycerophosphocholine O-acyltransferase

Systematic name:

acyl-CoA:1-O-(alk-1-enyl)-glycero-3-phosphocholine 2-O-acyltransferase

Links to other databases:

BRENDA, EXPASY, Gene, KEGG, CAS registry number: 37257-10-6

References:

1.	Waku, K. and Lands, W.E.M. Acyl coenzyme A:1-alkenyl-glycero-3-phosphorylcholine acyltransferase action in plasmalogen biosynthesis. J. Biol. Chem. 243 (1968) 2654–2659. [PMID: 5689955]
2.	Arthur, G. and Choy, P.C. Acylation of 1-alkenyl-glycerophosphocholine and 1-acyl-glycerophosphocholine in guinea pig heart. Biochem. J. 236 (1986) 481–487. [PMID: 3753462]

[EC 2.3.1.25 created 1972, modified 2013]

*EC

2.3.1.47

Accepted name:

8-amino-7-oxononanoate synthase

Reaction:

pimeloyl-[acyl-carrier protein] + L-alanine = 8-amino-7-oxononanoate + CO₂ + holo-[acyl-carrier protein]

Glossary:

pimeloyl-[acyl-carrier protein] = 6-carboxyhexanoyl-[acyl-carrier protein]

Other name(s):

7-keto-8-aminopelargonic acid synthetase; 7-keto-8-aminopelargonic synthetase; 8-amino-7-oxopelargonate synthase; bioF (gene name)

Systematic name:

6-carboxyhexanoyl-[acyl-carrier protein]:L-alanine C-carboxyhexanoyltransferase (decarboxylating)

Comments:

A pyridoxal-phosphate protein. The enzyme catalyses the decarboxylative condensation of L-alanine and pimeloyl-[acyl-carrier protein], a key step in the pathway for biotin biosynthesis. Pimeloyl-CoA can be used with lower efficiency [5].

Links to other databases:

BRENDA, EXPASY, Gene, KEGG, PDB, CAS registry number: 9075-61-0

References:

1.	Eisenberg, M.A. and Star, C. Synthesis of 7-oxo-8-aminopelargonic acid, a biotin vitamer, in cell-free extracts of Escherichia coli biotin auxotrophs. J. Bacteriol. 96 (1968) 1291–1297. [PMID: 4879561]
2.	Alexeev, D., Alexeeva, M., Baxter, R.L., Campopiano, D.J., Webster, S.P. and Sawyer, L. The crystal structure of 8-amino-7-oxononanoate synthase: a bacterial PLP-dependent, acyl-CoA-condensing enzyme. J. Mol. Biol. 284 (1998) 401–419. [DOI] [PMID: 9813126]
3.	Ploux, O., Breyne, O., Carillon, S. and Marquet, A. Slow-binding and competitive inhibition of 8-amino-7-oxopelargonate synthase, a pyridoxal-5′-phosphate-dependent enzyme involved in biotin biosynthesis, by substrate and intermediate analogs. Kinetic and binding studies. Eur. J. Biochem. 259 (1999) 63–70. [PMID: 9914476]
4.	Webster, S.P. , Alexeev. D., Campopiano, D.J., Watt, R.M., Alexeeva, M., Sawyer, L. and Baxter, R. Mechanism of 8-amino-7-oxononanoate synthase: spectroscopic, kinetic, and crystallographic studies. Biochemistry 39 (2000) 516–528. [DOI] [PMID: 10642176]
5.	Lin, S., Hanson, R.E. and Cronan, J.E. Biotin synthesis begins by hijacking the fatty acid synthetic pathway. Nat. Chem. Biol. 6 (2010) 682–688. [DOI] [PMID: 20693992]

[EC 2.3.1.47 created 1976, modified 2013]

2.3.1.104

Deleted entry:

1-alkenylglycerophosphocholine O-acyltransferase. The activity is covered by EC 2.3.1.25, plasmalogen synthase

[EC 2.3.1.104 created 1989, deleted 2013]

*EC

2.3.1.140

Accepted name:

rosmarinate synthase

Reaction:

caffeoyl-CoA + (R)-3-(3,4-dihydroxyphenyl)lactate = CoA + rosmarinate

For diagram of rosmarinate biosynthesis, click here

Glossary:

(R)-3-(3,4-dihydroxyphenyl)lactate = (2R)-3-(3,4-dihydroxyphenyl)-2-hydroxypropanoate
rosmarinate = (2R)-3-(3,4-dihydroxyphenyl)-2-{[(2E)-3-(3,4-dihydroxyphenyl)prop-2-enoyl]oxy}propanoate

Other name(s):

rosmarinic acid synthase; caffeoyl-coenzyme A:3,4-dihydroxyphenyllactic acid caffeoyltransferase; 4-coumaroyl-CoA:4-hydroxyphenyllactic acid 4-coumaroyl transferase; RAS (gene name)

Systematic name:

caffeoyl-CoA:(R)-3-(3,4-dihydroxyphenyl)lactate 2′-O-caffeoyl-transferase

Comments:

Involved, with EC 1.1.1.237 (hydroxyphenylpyruvate reductase) in the biosynthesis of rosmarinic acid. Characterized from the plant Melissa officinalis L. (lemon balm).

Links to other databases:

BRENDA, EXPASY, KEGG, PDB, CAS registry number: 117590-80-4

References:

1.	Petersen, M. and Alfermann, A.W. Two new enzymes of rosmarinic acid biosynthesis from cell cultures of Coleus blumei: hydroxyphenylpyruvate reductase and rosmarinic acid synthase. Z. Naturforsch. C: Biosci. 43 (1988) 501–504.
2.	Petersen, M. S. Characterization of rosmarinic acid synthase from cell cultures of Coleus blumei. Phytochemistry 30 (1991) 2877–2881.
3.	Weitzel, C. and Petersen, M. Cloning and characterisation of rosmarinic acid synthase from Melissa officinalis L. Phytochemistry 72 (2011) 572–578. [DOI] [PMID: 21354582]

[EC 2.3.1.140 created 1992, modified 2013]

*EC

2.3.1.151

Accepted name:

2,3′,4,6-tetrahydroxybenzophenone synthase

Reaction:

3 malonyl-CoA + 3-hydroxybenzoyl-CoA = 4 CoA + 2,3′,4,6-tetrahydroxybenzophenone + 3 CO₂

For diagram of polyketides biosynthesis, click here

Other name(s):

benzophenone synthase (ambiguous); BPS (ambiguous)

Systematic name:

malonyl-CoA:3-hydroxybenzoyl-CoA malonyltransferase (decarboxylating, 2,3′,4,6-tetrahydroxybenzophenone-forming)

Comments:

Involved in the biosynthesis of plant xanthones. Benzoyl-CoA can replace 3-hydroxybenzoyl-CoA (cf. EC 2.3.1.220, 2,4,6-trihydroxybenzophenone synthase).

Links to other databases:

BRENDA, EXPASY, KEGG, PDB, CAS registry number: 175780-21-9

References:

1.	Beerhues, L. Benzophenone synthase from cultured cells of Centaurium erythraea. FEBS Lett. 383 (1996) 264–266. [DOI] [PMID: 8925910]

[EC 2.3.1.151 created 1999, modified 2013]

*EC

2.3.1.153

Accepted name:

anthocyanin 5-(6′′′-hydroxycinnamoyltransferase)

Reaction:

4-hydroxycinnamoyl-CoA + an anthocyanidin 3,5-di-O-β-D-glucoside = CoA + anthocyanidin 3-O-β-D-glucoside 5-O-β-D-(6-O-4-hydroxycinnamoylglucoside)

For diagram of anthocyanidin glucoside biosynthesis, click here

Glossary:

4-hydroxycinnamoyl-CoA = 4-coumaroyl-CoA

Systematic name:

4-hydroxycinnamoyl-CoA:anthocyanidin 3,5-di-O-β-D-glucoside 5-O-glucoside-6′′′-O-4-hydroxycinnamoyltransferase

Comments:

Isolated from the plant Gentiana triflora. Transfers the hydroxycinnamoyl group only to the C-5 glucoside of anthocyanin. Caffeoyl-CoA, but not malonyl-CoA, can substitute as an acyl donor.

Links to other databases:

BRENDA, EXPASY, KEGG, PDB, CAS registry number: 198841-53-1

References:

1.	Fujiwara, H., Tanaka, Y., Fukui, Y., Nakao, M., Ashikari, T., Kusumi, T. Anthocyanin 5-aromatic acyltransferase from Gentiana triflora. Purification, characterization and its role in anthocyanin biosynthesis. Eur. J. Biochem. 249 (1997) 45–51. [DOI] [PMID: 9363752]
2.	Fujiwara, H., Tanaka, Y., Yonekura-Sakakibara, K., Fukuchi-Mizutani, M., Nakao, M., Fukui, Y., Yamaguchi, M., Ashikari, T. and Kusumi, T. cDNA cloning, gene expression and subcellular localization of anthocyanin 5-aromatic acyltransferase from Gentiana triflora. Plant J. 16 (1998) 421–431. [DOI] [PMID: 9881162]

[EC 2.3.1.153 created 1999, modified 2013]

2.3.1.211

Accepted name:

bisdemethoxycurcumin synthase

Reaction:

2 4-coumaroyl-CoA + malonyl-CoA + H₂O = 3 CoA + bisdemethoxycurcumin + 2 CO₂

For diagram of curcumin biosynthesis, click here

Glossary:

bisdemethoxycurcumin = (1E,6E)-5-hydroxy-1,7-bis(4-hydroxyphenyl)hepta-1,4,6-trien-3-one

Other name(s):

CUS; curcuminoid synthase (ambiguous)

Systematic name:

4-coumaroyl-CoA:malonyl-CoA 4-coumaryltransferase (bisdemethoxycurcumin-forming)

Comments:

A polyketide synthase characterized from the plant Oryza sativa (rice) that catalyses the formation of the C₆-C₇-C₆ diarylheptanoid scaffold of bisdemethoxycurcumin. Unlike the process in the plant Curcuma longa (turmeric), where the conversion is carried out via a diketide intermediate by two different enzymes (EC 2.3.1.218, phenylpropanoylacetyl-CoA synthase and EC 2.3.1.217, curcumin synthase), the diketide intermediate formed by this enzyme remains within the enzyme’s cavity and is not released to the environment.

Links to other databases:

References:

1.	Morita, H., Wanibuchi, K., Nii, H., Kato, R., Sugio, S. and Abe, I. Structural basis for the one-pot formation of the diarylheptanoid scaffold by curcuminoid synthase from Oryza sativa. Proc. Natl. Acad. Sci. USA 107 (2010) 19778–19783. [DOI] [PMID: 21041675]

[EC 2.3.1.211 created 2013]

2.3.1.212

Accepted name:

benzalacetone synthase

Reaction:

4-coumaroyl-CoA + malonyl-CoA + H₂O = 2 CoA + 4-hydroxybenzalacetone + 2 CO₂

For diagram of benzalacetone biosynthesis, click here

Glossary:

4-hydroxybenzalacetone = 4-(4-hydroxyphenyl)but-3-en-2-one

Other name(s):

BAS

Systematic name:

4-coumaroyl-CoA:malonyl-CoA 4-coumaryltransferase (4-hydroxybenzalacetone-forming)

Comments:

A polyketide synthase that catalyses the C₆-C₄ skeleton of phenylbutanoids in higher plants.

Links to other databases:

References:

1.	Borejsza-Wysocki, W. and Hrazdina, G. Aromatic polyketide synthases (purification, characterization, and antibody development to benzalacetone synthase from raspberry fruits). Plant Physiol. 110 (1996) 791–799. [PMID: 12226219]
2.	Abe, I., Takahashi, Y., Morita, H. and Noguchi, H. Benzalacetone synthase. A novel polyketide synthase that plays a crucial role in the biosynthesis of phenylbutanones in Rheum palmatum. Eur. J. Biochem. 268 (2001) 3354–3359. [DOI] [PMID: 11389739]
3.	Zheng, D. and Hrazdina, G. Molecular and biochemical characterization of benzalacetone synthase and chalcone synthase genes and their proteins from raspberry (Rubus idaeus L.). Arch. Biochem. Biophys. 470 (2008) 139–145. [DOI] [PMID: 18068110]
4.	Morita, H., Shimokawa, Y., Tanio, M., Kato, R., Noguchi, H., Sugio, S., Kohno, T. and Abe, I. A structure-based mechanism for benzalacetone synthase from Rheum palmatum. Proc. Natl. Acad. Sci. USA 107 (2010) 669–673. [DOI] [PMID: 20080733]

[EC 2.3.1.212 created 2013]

2.3.1.213

Accepted name:

cyanidin 3-O-(6-O-glucosyl-2-O-xylosylgalactoside) 6′′′-O-hydroxycinnamoyltransferase

Reaction:

1-O-(4-hydroxycinnamoyl)-β-D-glucose + cyanidin 3-O-(6-O-β-D-glucosyl-2-O-β-D-xylosyl-β-D-galactoside) = β-D-glucose + cyanidin 3-O-[6-O-(6-O-4-hydroxycinnamoyl-β-D-glucosyl)-2-O-β-D-xylosyl-β-D-galactoside]

For diagram of cyanidin galactoside biosynthesis, click here

Glossary:

1-O-(4-hydroxycinnamoyl)-β-D-glucose = 1-O-(4-coumaroyl)-β-D-glucose
cyanidin = 3,3′,4′,5,7-pentahydroxyflavylium

Other name(s):

1-O-(4-hydroxycinnamoyl)-β-D-glucose:cyanidin 3-O-(2"-O-xylosyl-6"-O-glucosylgalactoside) 6′′′-O-(4-hydroxycinnamoyl)transferase

Systematic name:

1-O-(4-hydroxycinnamoyl)-β-D-glucose:cyanidin 3-O-(6-O-β-D-glucosyl-2-O-β-D-xylosyl-β-D-galactoside) 6′′′-O-(4-hydroxycinnamoyl)transferase

Comments:

Isolated from the plant Daucus carota (Afghan cultivar carrot). In addition to 1-O-(4-hydroxycinnamoyl)-β-D-glucose, the enzyme can use the 1-O-sinapoyl- and 1-O-feruloyl- derivatives of β-D-glucose.

Links to other databases:

References:

1.	Gläßgen, W.E. and Seitz, H.U. Acylation of anthocyanins with hydroxycinnamic acids via 1-O-acylglucosides by protein preparations from cell cultures of Daucus carota L. Planta 186 (1992) 582–585. [PMID: 24186789]

[EC 2.3.1.213 created 2013]

2.3.1.214

Accepted name:

pelargonidin 3-O-(6-caffeoylglucoside) 5-O-(6-O-malonylglucoside) 4′′′-malonyltransferase

Reaction:

malonyl-CoA + 4′′′-demalonylsalvianin = CoA + salvianin

For diagram of salvianin biosynthesis, click here

Glossary:

salvianin = pelargonidin 3-O-(6-caffeoyl-β-D-glucoside) 5-O-(4,6-di-O-malonyl-β-D-glucoside)
4′′′-demalonylsalvianin = pelargonidin 3-O-(6-caffeoyl-β-D-glucoside) 5-O-(6-O-malonyl-β-D-glucoside)

Other name(s):

malonyl-CoA:anthocyanin 5-glucoside 4′′′-O-malonyltransferase; Ss5MaT2

Systematic name:

malonyl-CoA:4′′′-demalonylsalvianin 4′′′-O-malonyltransferase

Comments:

Isolated from the plant Salvia splendens (scarlet sage).

Links to other databases:

References:

Suzuki, H., Sawada, S., Watanabe, K., Nagae, S., Yamaguchi, M.A., Nakayama, T. and Nishino, T. Identification and characterization of a novel anthocyanin malonyltransferase from scarlet sage (Salvia splendens) flowers: an enzyme that is phylogenetically separated from other anthocyanin acyltransferases. Plant J. 38 (2004) 994–1003. [DOI] [PMID: 15165190]

[EC 2.3.1.214 created 2013]

2.3.1.215

Accepted name:

anthocyanidin 3-O-glucoside 6′′-O-acyltransferase

Reaction:

4-hydroxycinnamoyl-CoA + an anthocyanidin 3-O-β-D-glucoside = CoA + an anthocyanidin 3-O-[6-O-(4-hydroxycinnamoyl)-β-D-glucoside]

For diagram of anthocyanidin acylglucoside biosynthesis, click here and for diagram of salvianin biosynthesis, click here

Glossary:

4-hydroxycinnamoyl-CoA = 4-coumaroyl-CoA
3,4-dihydroxycinnamoyl-CoA = caffeoyl-CoA
cyanidin = 3,3′,4′,5,7-pentahydroxyflavylium
delphinidin = 3,3′,4′,5,5′,7-hexahydroxyflavylium

Systematic name:

4-hydroxycinnamoyl-CoA:anthocyanin-3-O-glucoside 6′′-O-acyltransferase

Comments:

Isolated from the plants Perilla frutescens and Gentiana triflora (clustered gentian). Acts on a range of anthocyanidin 3-O-glucosides, 3,5-di-O-glucosides and cyanidin 3-rutinoside. It did not act on delphinidin 3,3′,7-tri-O-glucoside. Recombinant Perilla frutescens enzyme could utilize caffeoyl-CoA but not malonyl-CoA as alternative acyl donor.

Links to other databases:

References:

1.	Fujiwara, H., Tanaka, Y., Fukui, Y., Ashikari, T., Yamaguchi, M. and Kusumi, T. Purification and characterization of anthocyanin 3-aromatic acyltransferase from Perilla frutescens. Plant Sci. 137 (1998) 87–94.
2.	Yonekura-Sakakibara, K., Tanaka, Y., Fukuchi-Mizutani, M., Fujiwara, H., Fukui, Y., Ashikari, T., Murakami, Y., Yamaguchi, M. and Kusumi, T. Molecular and biochemical characterization of a novel hydroxycinnamoyl-CoA: anthocyanin 3-O-glucoside-6"-O-acyltransferase from Perilla frutescens. Plant Cell Physiol. 41 (2000) 495–502. [DOI] [PMID: 10845463]

[EC 2.3.1.215 created 2013]

2.3.1.216

Accepted name:

5,7-dihydroxy-2-methylchromone synthase

Reaction:

5 malonyl-CoA = 5 CoA + 5,7-dihydroxy-2-methyl-4H-chromen-4-one + 5 CO₂ + H₂O

For diagram of polyketides biosynthesis, click here

Other name(s):

pentaketide chromone synthase

Systematic name:

malonyl-CoA:malonyl-CoA malonyltransferase (5,7-dihydroxy-2-methyl-4H-chromen-4-one-forming)

Comments:

A polyketide synthase from the plant Aloe arborescens (aloe).

Links to other databases:

References:

1.	Abe, I., Utsumi, Y., Oguro, S., Morita, H., Sano, Y. and Noguchi, H. A plant type III polyketide synthase that produces pentaketide chromone. J. Am. Chem. Soc. 127 (2005) 1362–1363. [DOI] [PMID: 15686354]

[EC 2.3.1.216 created 2013]

2.3.1.217

Accepted name:

curcumin synthase

Reaction:

feruloyl-CoA + feruloylacetyl-CoA + H₂O = 2 CoA + curcumin + CO₂

For diagram of curcumin biosynthesis, click here

Glossary:

curcumin = (1E,6E)-5-hydroxy-1,7-bis(4-hydroxy-3-methoxyphenyl)hepta-1,4,6-trien-3-one
feruloylacetyl-CoA = feruloyl-diketide-CoA

Other name(s):

CURS; CURS1 (gene name); CURS2 (gene name); CURS3 (gene name)

Systematic name:

feruloyl-CoA:feruloylacetyl-CoA feruloyltransferase (curcumin-forming)

Comments:

A polyketide synthase from the plant Curcuma longa (turmeric). Three isoforms exist, CURS1, CURS2 and CURS3. While CURS1 and CURS2 prefer feruloyl-CoA as a starter substrate, CURS3 can accept 4-coumaroyl-CoA equally well [2] (see EC 2.3.1.219, demethoxycurcumin synthase).

Links to other databases:

References:

1.	Katsuyama, Y., Kita, T., Funa, N. and Horinouchi, S. Curcuminoid biosynthesis by two type III polyketide synthases in the herb Curcuma longa. J. Biol. Chem. 284 (2009) 11160–11170. [DOI] [PMID: 19258320]
2.	Katsuyama, Y., Kita, T. and Horinouchi, S. Identification and characterization of multiple curcumin synthases from the herb Curcuma longa. FEBS Lett. 583 (2009) 2799–2803. [DOI] [PMID: 19622354]
3.	Katsuyama, Y., Miyazono, K., Tanokura, M., Ohnishi, Y. and Horinouchi, S. Structural and biochemical elucidation of mechanism for decarboxylative condensation of β-keto acid by curcumin synthase. J. Biol. Chem. 286 (2011) 6659–6668. [DOI] [PMID: 21148316]

[EC 2.3.1.217 created 2013]

2.3.1.218

Accepted name:

phenylpropanoylacetyl-CoA synthase

Reaction:

(1) feruloyl-CoA + malonyl-CoA = feruloylacetyl-CoA + CO₂ + CoA
(2) 4-coumaroyl-CoA + malonyl-CoA = (4-coumaroyl)acetyl-CoA + CO₂ + CoA

For diagram of curcumin biosynthesis, click here

Glossary:

feruloylacetyl-CoA = feruloyl-diketide-CoA
(4-coumaroyl)acetyl-CoA = 4-coumaroyl-diketide-CoA
phenylpropanoylacetyl-CoA = phenylpropanoyl-diketide-CoA

Other name(s):

phenylpropanoyl-diketide-CoA synthase; DCS

Systematic name:

phenylpropanoyl-CoA:malonyl-CoA phenylpropanoyl-transferase (decarboxylating)

Comments:

The enzyme has been characterized from the plant Curcuma longa (turmeric). It prefers feruloyl-CoA, and has no activity with cinnamoyl-CoA.

Links to other databases:

References:

1.	Katsuyama, Y., Kita, T., Funa, N. and Horinouchi, S. Curcuminoid biosynthesis by two type III polyketide synthases in the herb Curcuma longa. J. Biol. Chem. 284 (2009) 11160–11170. [DOI] [PMID: 19258320]

[EC 2.3.1.218 created 2013]

2.3.1.219

Accepted name:

demethoxycurcumin synthase

Reaction:

(1) 4-coumaroyl-CoA + feruloylacetyl-CoA + H₂O = 2 CoA + demethoxycurcumin + CO₂
(2) 4-coumaroyl-CoA + (4-coumaroyl)acetyl-CoA + H₂O = 2 CoA + bisdemethoxycurcumin + CO₂

For diagram of curcumin biosynthesis, click here

Glossary:

demethoxycurcumin = (1E,6E)-5-hydroxy-1-(4-hydroxy-3-methoxyphenyl)-7-(4-hydroxyphenyl)hepta-1,4,6-trien-3-one
bisdemethoxycurcumin = (1E,6E)-5-hydroxy-1,7-bis(4-hydroxyphenyl)hepta-1,4,6-trien-3-one
feruloylacetyl-CoA = feruloyl-diketide-CoA
(4-coumaroyl)acetyl-CoA = 4-coumaroyl-diketide-CoA

Other name(s):

CURS3

Systematic name:

4-coumaroyl-CoA:feruloylacetyl-CoA feruloyltransferase (demethoxycurcumin-forming)

Comments:

A polyketide synthase from the plant Curcuma longa (turmeric). Three isoforms exist, CURS1, CURS2 and CURS3. While CURS1 and CURS2 prefer feruloyl-CoA as a starter substrate (cf. EC 2.3.1.217, curcumin synthase), CURS3 can accept 4-coumaroyl-CoA equally well [1].

Links to other databases:

References:

1.	Katsuyama, Y., Kita, T. and Horinouchi, S. Identification and characterization of multiple curcumin synthases from the herb Curcuma longa. FEBS Lett. 583 (2009) 2799–2803. [DOI] [PMID: 19622354]

[EC 2.3.1.219 created 2013]

2.3.1.220

Accepted name:

2,4,6-trihydroxybenzophenone synthase

Reaction:

3 malonyl-CoA + benzoyl-CoA = 4 CoA + 2,4,6-trihydroxybenzophenone + 3 CO₂

For diagram of polyketides biosynthesis, click here

Other name(s):

benzophenone synthase (ambiguous); BPS (ambiguous)

Systematic name:

malonyl-CoA:benzoyl-CoA malonyltransferase (2,4,6-trihydroxybenzophenone-forming)

Comments:

Involved in the biosynthesis of plant xanthones. The enzyme from the plant Hypericum androsaemum L can use 3-hydroxybenzoyl-CoA instead of benzoyl-CoA, but with lower activity (cf. EC 2.3.1.151, 2,3′,4,6-tetrahydroxybenzophenone synthase).

Links to other databases:

References:

1.	Schmidt, W. and Beerhues, L. Alternative pathways of xanthone biosynthesis in cell cultures of Hypericum androsaemum L. FEBS Lett. 420 (1997) 143–146. [DOI] [PMID: 9459298]
2.	Nualkaew, N., Morita, H., Shimokawa, Y., Kinjo, K., Kushiro, T., De-Eknamkul, W., Ebizuka, Y. and Abe, I. Benzophenone synthase from Garcinia mangostana L. pericarps. Phytochemistry 77 (2012) 60–69. [DOI] [PMID: 22390826]

[EC 2.3.1.220 created 2013]

2.3.1.221

Accepted name:

noranthrone synthase

Reaction:

7 malonyl-CoA + hexanoyl-[acyl-carrier protein] = 7 CoA + norsolorinic acid anthrone + [acyl-carrier protein] + 7 CO₂ + 2 H₂O

For diagram of polyketides biosynthesis, click here

Glossary:

norsolorinic acid anthrone = noranthrone = 2-hexanoyl-1,3,6,8-tetrahydroxyanthracen-9(10H)-one

Other name(s):

polyketide synthase A (ambiguous); PksA (ambiguous); norsolorinic acid anthrone synthase

Systematic name:

malonyl-CoA:hexanoate malonyltransferase (norsolorinic acid anthrone-forming)

Comments:

A multi-domain polyketide synthase involved in the synthesis of aflatoxins in the fungus Aspergillus parasiticus. The hexanoyl starter unit is provided to the acyl-carrier protein (ACP) domain by a dedicated fungal fatty acid synthase [1].

Links to other databases:

References:

1.	Crawford, J.M., Thomas, P.M., Scheerer, J.R., Vagstad, A.L., Kelleher, N.L. and Townsend, C.A. Deconstruction of iterative multidomain polyketide synthase function. Science 320 (2008) 243–246. [DOI] [PMID: 18403714]
2.	Crawford, J.M., Korman, T.P., Labonte, J.W., Vagstad, A.L., Hill, E.A., Kamari-Bidkorpeh, O., Tsai, S.C. and Townsend, C.A. Structural basis for biosynthetic programming of fungal aromatic polyketide cyclization. Nature 461 (2009) 1139–1143. [DOI] [PMID: 19847268]
3.	Korman, T.P., Crawford, J.M., Labonte, J.W., Newman, A.G., Wong, J., Townsend, C.A. and Tsai, S.C. Structure and function of an iterative polyketide synthase thioesterase domain catalyzing Claisen cyclization in aflatoxin biosynthesis. Proc. Natl. Acad. Sci. USA 107 (2010) 6246–6251. [DOI] [PMID: 20332208]

[EC 2.3.1.221 created 2013]

2.3.1.222

Accepted name:

phosphate propanoyltransferase

Reaction:

propanoyl-CoA + phosphate = CoA + propanoyl phosphate

Other name(s):

PduL

Systematic name:

propanoyl-CoA:phosphate propanoyltransferase

Comments:

Part of the degradation pathway for propane-1,2-diol .

Links to other databases:

References:

Liu, Y., Leal, N.A., Sampson, E.M., Johnson, C.L., Havemann, G.D. and Bobik, T.A. PduL is an evolutionarily distinct phosphotransacylase involved in B₁₂-dependent 1,2-propanediol degradation by Salmonella enterica serovar typhimurium LT2. J. Bacteriol. 189 (2007) 1589–1596. [DOI] [PMID: 17158662]

[EC 2.3.1.222 created 2013]

*EC

2.3.2.1

Accepted name:

D-glutamyltransferase

Reaction:

(1) D-glutamine + D-glutamate = NH₃ + γ-D-glutamyl-D-glutamate
(2) L(or D)-glutamine + (γ-D-glutamyl)_n-[peptide] = NH₃ + (γ-D-glutamyl)_n+1-[peptide]

Other name(s):

D-glutamyl transpeptidase; D-γ-glutamyl transpeptidase

Systematic name:

glutamine:D-glutamyl-peptide 5-glutamyltransferase

Comments:

The enzyme catalyses two reactions. The first is the transfer of a glutamyl residue from L- or D-glutamine to D-glutamate via a γ linkage, forming γ-glutamyl-D-glutamate, and the second is the transfer of additional glutamyl residues to the peptide, extending the polypeptide chain.

Links to other databases:

BRENDA, EXPASY, Gene, KEGG, CAS registry number: 9030-02-8

References:

1.	Williams, W.J. and Thorne, C.B. Biosynthesis of glutamyl peptides from glutamine by a transfer reaction. J. Biol. Chem. 210 (1954) 203–217. [PMID: 13201582]
2.	Williams, W.J., Litwin, J. and Thorne, C.B. Further studies on the biosynthesis of γ-glutamyl peptides by transfer reactions. J. Biol. Chem. 212 (1955) 427–438. [PMID: 13233245]

[EC 2.3.2.1 created 1961, modified 1976, modified 2013]

*EC

2.4.1.62

Accepted name:

ganglioside galactosyltransferase

Reaction:

UDP-α-D-galactose + an N-acetyl-β-D-galactosaminyl-(1→4)-[α-N-acetylneuraminyl-(2→3)]-β-D-galactosyl-(1→4)-β-D-glucosyl-(1↔1)-ceramide = UDP + a β-D-galactosyl-(1→3)-N-acetyl-β-D-galactosaminyl-(1→4)-[α-N-acetylneuraminyl-(2→3)]-β-D-galactosyl-(1→4)-β-D-glucosyl-(1↔1)-ceramide

For diagram of ganglioside biosynthesis, click here

Glossary:

N-acetyl-β-D-galactosaminyl-(1→4)-[α-N-acetylneuraminyl-(2→3)]-β-D-galactosyl-(1→4)-β-D-glucosyl-(1↔1)-ceramide = ganglioside GM2
a β-D-galactosyl-(1→3)-N-acetyl-β-D-galactosaminyl-(1→4)-[α-N-acetylneuraminyl-(2→3)]-β-D-galactosyl-(1→4)-β-D-glucosyl-(1↔1)-ceramide = gangloside GM1a

Other name(s):

UDP-galactose—ceramide galactosyltransferase; uridine diphosphogalactose-ceramide galactosyltransferase; UDP galactose-LAC Tet-ceramide α-galactosyltransferase; UDP-galactose-GM2 galactosyltransferase; uridine diphosphogalactose-GM2 galactosyltransferase; uridine diphosphate D-galactose:glycolipid galactosyltransferase; UDP-galactose:N-acetylgalactosaminyl-(N-acetylneuraminyl) galactosyl-glucosyl-ceramide galactosyltransferase; UDP-galactose-GM2 ganglioside galactosyltransferase; GM1-synthase; UDP-galactose:N-acetyl-D-galactosaminyl-(N-acetylneuraminyl)-D-galactosyl-D-glucosyl-N-acylsphingosine β-1,3-D-galactosyltransferase; UDP-galactose:N-acetyl-D-galactosaminyl-(N-acetylneuraminyl)-D-galactosyl-(1→4)-β-D-glucosyl-N-acylsphingosine 3-β-D-galactosyltransferase

Systematic name:

UDP-α-D-galactose:N-acetyl-β-D-galactosaminyl-(1→4)-[α-N-acetylneuraminyl-(2→3)]-β-D-galactosyl-(1→4)-β-D-glucosyl-(1↔1)-ceramide 3-β-D-galactosyltransferase

Comments:

The substrate is also known as gangloside GM2, the product as gangloside GM1a

Links to other databases:

BRENDA, EXPASY, Gene, KEGG, CAS registry number: 37217-28-0

References:

1.	Basu, S., Kaufman, B. and Roseman, S. Conversion of Tay-Sachs ganglioside to monosialoganglioside by brain uridine diphosphate D-galactose: glycolipid galactosyltransferase. J. Biol. Chem. 240 (1965) 4115–4117. [PMID: 5842076]
2.	Yip, G.B. and Dain, J.A. The enzymic synthesis of ganglioside. II. UDP-galactose: N-acetylgalactosaminyl-(N-acetylneuraminyl)galactosyl-glucosyl-ceramide galactosyltransferase in rat brain. Biochim. Biophys. Acta 206 (1970) 252–260. [DOI] [PMID: 4987145]
3.	Yip, M.C.M. and Dain, J.A. Frog brain uridine diphosphate galactose-N-acetylgalactosaminyl-N-acetylneuraminylgalactosylglucosylceramide galactosyltransferase. Biochem. J. 118 (1970) 247–252. [PMID: 5484669]

[EC 2.4.1.62 created 1972, modified 2013]

*EC

2.4.1.116

Accepted name:

cyanidin 3-O-rutinoside 5-O-glucosyltransferase

Reaction:

UDP-α-D-glucose + cyanidin-3-O-rutinoside = UDP + cyanidin 3-O-rutinoside 5-O-β-D-glucoside

For diagram of anthocyanidin rutoside biosynthesis, click here

Glossary:

cyanidin 3-O-rutinoside = cyanidin-3-O-α-L-rhamnosyl-(1→6)-β-D-glucoside
cyanidin = 3,3′,4′,5,7-pentahydroxyflavylium

Other name(s):

uridine diphosphoglucose-cyanidin 3-rhamnosylglucoside 5-O-glucosyltransferase; cyanidin-3-rhamnosylglucoside 5-O-glucosyltransferase; UDP-glucose:cyanidin-3-O-D-rhamnosyl-1,6-D-glucoside 5-O-D-glucosyltransferase

Systematic name:

UDP-α-D-glucose:cyanidin-3-O-α-L-rhamnosyl-(1→6)-β-D-glucoside 5-O-β-D-glucosyltransferase

Comments:

Isolated from the plants Silene dioica (red campion) [1], Iris ensata (Japanese iris) [2] and Iris hollandica (Dutch iris) [3]. Also acts on the 3-O-rutinosides of pelargonidin, delphinidin and malvidin, but not the corresponding glucosides or 6-acylglucosides. The enzyme does not catalyse the glucosylation of the 5-hydroxy group of cyanidin 3-glucoside.

Links to other databases:

BRENDA, EXPASY, KEGG, CAS registry number: 70248-66-7

References:

1.	Kamsteeg, J., van Brederode, J. and van Nigtevecht, G. Identification, properties, and genetic control of UDP-glucose: cyanidin-3-rhamnosyl-(1→6)-glucoside-5-O-glucosyltransferase isolated from petals of the red campion (Silene dioica). Biochem. Genet. 16 (1978) 1059–1071. [PMID: 751641]
2.	Yabuya, T., Yamaguchi, M., Imayama, T., Katoh, K. and Ino I. Anthocyanin 5-O-glucosyltransferase in flowers of Iris ensata. Plant Sci. 162 (2002) 779–784.
3.	Imayama, T., Yoshihara, Y., Fukuchi-Mizutani, M., Tanaka, Y., Ino, I. and Yabuya, T. Isolation and characterization of a cDNA clone of UDP-glucose:anthocyanin 5-O-glucosyltransferase in Iris hollandica. Plant Sci. 167 (2004) 1243–1248.

[EC 2.4.1.116 created 1984 (EC 2.4.1.235 created 2004, incorporated 2006), modified 2006, modified 2013]

*EC

2.4.1.238

Accepted name:

delphinidin 3,5-di-O-glucoside 3′-O-glucosyltransferase

Reaction:

UDP-α-D-glucose + delphinidin 3,5-di-O-β-D-glucoside = UDP + delphinidin 3,3′,5-tri-O-β-D-glucoside

For diagram of anthocyanidin glucoside biosynthesis, click here

Glossary:

delphinidin = 3,3′,4′,5,5′,7-hexahydroxyflavylium

Other name(s):

UDP-glucose:anthocyanin 3′-O-glucosyltransferase; 3’GT

Systematic name:

UDP-α-D-glucose:delphinidin-3,5-di-O-β-D-glucoside 3′-O-glucosyltransferase

Comments:

Isolated from the plant Gentiana triflora (clustered gentian).

Links to other databases:

BRENDA, EXPASY, KEGG, CAS registry number: 380231-41-4

References:

Fukuchi-Mizutani, M., Okuhara, H., Fukui, Y., Nakao, M., Katsumoto, Y., Yonekura-Sakakibara, K., Kusumi, T., Hase, T. and Tanaka, Y. Biochemical and molecular characterization of a novel UDP-glucose:anthocyanin 3′-O-glucosyltransferase, a key enzyme for blue anthocyanin biosynthesis, from gentian. Plant Physiol. 132 (2003) 1652–1663. [DOI] [PMID: 12857844]

[EC 2.4.1.238 created 2004, modified 2013]

*EC

2.4.1.275

Accepted name:

neolactotriaosylceramide β-1,4-galactosyltransferase

Reaction:

UDP-α-D-galactose + N-acetyl-β-D-glucosaminyl-(1→3)-β-D-galactosyl-(1→4)-β-D-glucosyl-(1↔1)-ceramide = UDP + β-D-galactosyl-(1→4)-N-acetyl-β-D-glucosaminyl-(1→3)-β-D-galactosyl-(1→4)-β-D-glucosyl-(1↔1)-ceramide

For diagram of neolactotetraosylceramide biosynthesis, click here

Glossary:

N-acetyl-β-D-glucosaminyl-(1→3)-β-D-galactosyl-(1→4)-β-D-glucosyl-(1↔1)-ceramide = neolactotriaosylceramide

Other name(s):

β4Gal-T4; UDP-galactose:N-acetyl-β-D-glucosaminyl-(1→3)-β-D-galactosyl-(1→4)-β-D-glucosyl-(1↔1)-ceramide β-1,4-galactosyltransferase; lactotriaosylceramide β-1,4-galactosyltransferase (incorrect)

Systematic name:

UDP-α-D-galactose:N-acetyl-β-D-glucosaminyl-(1→3)-β-D-galactosyl-(1→4)-β-D-glucosyl-(1↔1)-ceramide 4-β-D-galactosyltransferase

Links to other databases:

References:

Schwientek, T., Almeida, R., Levery, S.B., Holmes, E.H., Bennett, E. and Clausen, H. Cloning of a novel member of the UDP-galactose:β-N-acetylglucosamine β1,4-galactosyltransferase family, β4Gal-T4, involved in glycosphingolipid biosynthesis. J. Biol. Chem. 273 (1998) 29331–29340. [DOI] [PMID: 9792633]

[EC 2.4.1.275 created 2011, modified 2013]

2.4.1.294

Accepted name:

cyanidin 3-O-galactosyltransferase

Reaction:

UDP-α-D-galactose + cyanidin = UDP + cyanidin 3-O-β-D-galactoside

For diagram of cyanidin galactoside biosynthesis, click here

Glossary:

cyanidin = 3,3′,4′,5,7-pentahydroxyflavylium

Other name(s):

UDP-galactose:cyanidin galactosyltransferase

Systematic name:

UDP-α-D-galactose:cyanidin 3-O-galactosyltransferase

Comments:

Isolated from the plant Daucus carota (Afghan cultivar carrot).

Links to other databases:

References:

1.	Rose, A., Glassgen, W.E., Hopp, W. and Seitz, H.U. Purification and characterization of glycosyltransferases involved in anthocyanin biosynthesis in cell-suspension cultures of Daucus carota L. Planta 198 (1996) 397–403. [PMID: 8717136]

[EC 2.4.1.294 created 2013]

2.4.1.295

Accepted name:

anthocyanin 3-O-sambubioside 5-O-glucosyltransferase

Reaction:

UDP-α-D-glucose + an anthocyanidin 3-O-β-D-sambubioside = UDP + an anthocyanidin 5-O-β-D-glucoside 3-O-β-D-sambubioside

For diagram of anthocyanidin sambubioside biosynthesis, click here

Glossary:

anthocyanidin 3-O-β-D-sambubioside = anthocyanidin 3-O-(β-D-xylosyl-(1→2)-β-D-glucoside)

Systematic name:

UDP-α-D-glucose:anthocyanidin-3-O-β-D-sambubioside 5-O-glucosyltransferase

Comments:

Isolated from the plant Matthiola incana (stock). No activity with anthocyanidin 3-O-glucosides.

Links to other databases:

References:

1.	Teusch, M., Forkmann, G. and Seyffert, W. Genetic control of UDP-glucose: anthocyanin 5-O-glucosyltransferase from flowers of Matthiola incana R.Br. Planta 168 (1986) 586–591. [PMID: 24232337]

[EC 2.4.1.295 created 2013]

2.4.1.296

Accepted name:

anthocyanidin 3-O-coumaroylrutinoside 5-O-glucosyltransferase

Reaction:

UDP-α-D-glucose + an anthocyanidin 3-O-[2-O-(4-coumaroyl)-α-L-rhamnosyl-(1→6)-β-D-glucoside] = UDP + an anthocyanidin 3-O-[2-O-(4-coumaroyl)-α-L-rhamnosyl-(1→6)-β-D-glucoside] 5-O-β-D-glucoside

For diagram of anthocyanidin rutoside biosynthesis, click here

Systematic name:

UDP-α-D-glucose:anthocyanidin-3-O-[3-O-(4-coumaroyl)-α-L-rhamnosyl-(1→6)-β-D-glucoside] 5-O-β-D-glucosyltransferase

Comments:

Isolated from the plant Petunia hybrida. It does not act on an anthocyanidin 3-O-rutinoside

Links to other databases:

References:

1.	Jonsson, L.M.V., Aarsman, M.E.G., van Diepen, J., de Vlaming, P., Smit, N. and Schram, A.W. Properties and genetic control of anthocyanin 5-O-glucosyltransferase in flowers of Petunia hybrida. Planta 160 (1984) 341–347. [PMID: 24258583]

[EC 2.4.1.296 created 2013]

2.4.1.297

Accepted name:

anthocyanidin 3-O-glucoside 2′′-O-glucosyltransferase

Reaction:

UDP-α-D-glucose + an anthocyanidin 3-O-β-D-glucoside = UDP + an anthocyanidin 3-O-sophoroside

For diagram of anthocyanidin glycoside biosynthesis, click here

Glossary:

anthocyanidin 3-O-sophoroside = anthocyanidin 3-O-(β-D-glucosyl(1→2)-β-D-glucoside)

Other name(s):

3GGT

Systematic name:

UDP-α-D-glucose:anthocyanidin-3-O-glucoside 2′′-O-glucosyltransferase

Comments:

Isolated from Ipomoea nil (Japanese morning glory).

Links to other databases:

References:

Morita, Y., Hoshino, A., Kikuchi, Y., Okuhara, H., Ono, E., Tanaka, Y., Fukui, Y., Saito, N., Nitasaka, E., Noguchi, H. and Iida, S. Japanese morning glory dusky mutants displaying reddish-brown or purplish-gray flowers are deficient in a novel glycosylation enzyme for anthocyanin biosynthesis, UDP-glucose:anthocyanidin 3-O-glucoside-2′′-O-glucosyltransferase, due to 4-bp insertions in the gene. Plant J. 42 (2005) 353–363. [DOI] [PMID: 15842621]

[EC 2.4.1.297 created 2013]

2.4.1.298

Accepted name:

anthocyanidin 3-O-glucoside 5-O-glucosyltransferase

Reaction:

UDP-α-D-glucose + an anthocyanidin 3-O-β-D-glucoside = UDP + an anthocyanidin 3,5-di-O-β-D-glucoside

For diagram of anthocyanidin glucoside biosynthesis, click here

Other name(s):

UDP-glucose:anthocyanin 5-O-glucosyltransferase

Systematic name:

UDP-α-D-glucose:anthocyanidin-3-O-β-D-glucoside 5-O-glucosyltransferase

Comments:

Isolated from the plants Perilla frutescens var. crispa, Verbena hybrida [1], Dahlia variabilis [2] and Gentiana triflora (clustered gentian) [3]. It will also act on anthocyanidin 3-O-(6-O-malonylglucoside) [2] and is much less active with hydroxycinnamoylglucose derivatives [3]. There is no activity in the absence of the 3-O-glucoside group.

Links to other databases:

References:

1.	Yamazaki, M., Gong, Z., Fukuchi-Mizutani, M., Fukui, Y., Tanaka, Y., Kusumi, T. and Saito, K. Molecular cloning and biochemical characterization of a novel anthocyanin 5-O-glucosyltransferase by mRNA differential display for plant forms regarding anthocyanin. J. Biol. Chem. 274 (1999) 7405–7411. [DOI] [PMID: 10066805]
2.	Ogata, J., Sakamoto, T., Yamaguchi, M., Kawanobu, S., Yoshitama, K. Isolation and characterization of anthocyanin 5-O-glucosyltransferase from flowers of Dahlia variabilis. J. Plant Physiol. 158 (2001) 709–714.
3.	Nakatsuka, T., Sato, K., Takahashi, H., Yamamura, S. and Nishihara, M. Cloning and characterization of the UDP-glucose:anthocyanin 5-O-glucosyltransferase gene from blue-flowered gentian. J. Exp. Bot. 59 (2008) 1241–1252. [DOI] [PMID: 18375606]

[EC 2.4.1.298 created 2013]

2.4.1.299

Accepted name:

cyanidin 3-O-glucoside 5-O-glucosyltransferase (acyl-glucose)

Reaction:

1-O-sinapoyl-β-D-glucose + cyanidin 3-O-β-D-glucoside = sinapate + cyanidin 3,5-di-O-β-D-glucoside

For diagram of anthocyanidin glucoside biosynthesis, click here

Glossary:

sinapate = 4-hydroxy-3,5-dimethoxycinnamate
cyanidin = 3,3′,4′,5,7-pentahydroxyflavylium

Other name(s):

AA5GT

Systematic name:

1-O-sinapoyl-β-D-glucose:cyanidin-3-O-β-D-glucoside 5-O-β-D-glucosyltransferase

Comments:

Isolated from the plant Dianthus caryophyllus (carnation). Also acts on other anthocyanidins and with other acyl-glucose donors. cf. EC 2.4.1.298, anthocyanidin 3-O-glucoside 5-O-glucosyltransferase.

Links to other databases:

References:

1.	Matsuba, Y., Sasaki, N., Tera, M., Okamura, M., Abe, Y., Okamoto, E., Nakamura, H., Funabashi, H., Takatsu, M., Saito, M., Matsuoka, H., Nagasawa, K. and Ozeki, Y. A novel glucosylation reaction on anthocyanins catalyzed by acyl-glucose-dependent glucosyltransferase in the petals of carnation and delphinium. Plant Cell 22 (2010) 3374–3389. [DOI] [PMID: 20971893]
2.	Nishizaki, Y., Matsuba, Y., Okamoto, E., Okamura, M., Ozeki, Y. and Sasaki, N. Structure of the acyl-glucose-dependent anthocyanin 5-O-glucosyltransferase gene in carnations and its disruption by transposable elements in some varieties. Mol. Genet. Genomics 286 (2011) 383–394. [DOI] [PMID: 22048706]

[EC 2.4.1.299 created 2013]

2.4.1.300

Accepted name:

cyanidin 3-O-glucoside 7-O-glucosyltransferase (acyl-glucose)

Reaction:

1-O-vanilloyl-β-D-glucose + cyanidin 3-O-β-D-glucoside = vanillate + cyanidin 3,7-di-O-β-D-glucoside

For diagram of anthocyanidin glucoside biosynthesis, click here

Glossary:

vanillate = 4-hydroxy-3-methoxybenzoate
cyanidin = 3,3′,4′,5,7-pentahydroxyflavylium

Other name(s):

AA7GT

Systematic name:

1-O-vanilloyl-β-D-glucose:cyanidin-3-O-β-D-glucoside 7-O-β-D-glucosyltransferase

Comments:

Isolated from the plant Delphinium grandiflorum (delphinium). Also acts on other anthocyanidins and with other acyl-glucose derivatives.

Links to other databases:

References:

Matsuba, Y., Sasaki, N., Tera, M., Okamura, M., Abe, Y., Okamoto, E., Nakamura, H., Funabashi, H., Takatsu, M., Saito, M., Matsuoka, H., Nagasawa, K. and Ozeki, Y. A novel glucosylation reaction on anthocyanins catalyzed by acyl-glucose-dependent glucosyltransferase in the petals of carnation and delphinium. Plant Cell 22 (2010) 3374–3389. [DOI] [PMID: 20971893]

[EC 2.4.1.300 created 2013]

2.4.2.49

Accepted name:

neamine phosphoribosyltransferase

Reaction:

neamine + 5-phospho-α-D-ribose 1-diphosphate = 5′′-phosphoribostamycin + diphosphate

For diagram of neamine and ribostamycin biosynthesis, click here

Glossary:

neamine = (2R,3S,4R,5R,6R)-5-amino-2-(aminomethyl)-6-{[(1R,2R,3S,4R,6S)-4,6-diamino-2,3-dihydroxycyclohexyl]oxy}oxane-3,4-diol
ribostamycin = (2R,3S,4R,5R,6R)-5-amino-2-(aminomethyl)-6-{[(1R,2R,3S,4R,6S)-4,6-diamino-2-{[(2S,3R,4S,5R)-3,4-dihydroxy-5-(hydroxymethyl)oxolan-2-yl]oxy}-3-hydroxycyclohexyl]oxy}oxane-3,4-diol

Other name(s):

btrL (gene name); neoM (gene name)

Systematic name:

neamine:5-phospho-α-D-ribose 1-diphosphate phosphoribosyltransferase

Comments:

Involved in the biosynthetic pathways of several clinically important aminocyclitol antibiotics, including ribostamycin, neomycin and butirosin. The enzyme requires a divalent metal ion, optimally Mg²⁺, Ni²⁺ or Co²⁺.

Links to other databases:

References:

1.	Kudo, F., Fujii, T., Kinoshita, S. and Eguchi, T. Unique O-ribosylation in the biosynthesis of butirosin. Bioorg. Med. Chem. 15 (2007) 4360–4368. [DOI] [PMID: 17482823]

[EC 2.4.2.49 created 2013]

2.4.2.50

Accepted name:

cyanidin 3-O-galactoside 2′′-O-xylosyltransferase

Reaction:

UDP-α-D-xylose + cyanidin 3-O-β-D-galactoside = UDP + cyanidin 3-O-(β-D-xylosyl-(1→2)-β-D-galactoside)

For diagram of cyanidin galactoside biosynthesis, click here

Glossary:

cyanidin = 3,3′,4′,5,7-pentahydroxyflavylium

Other name(s):

CGXT

Systematic name:

UDP-α-D-xylose:cyanidin-3-O-β-D-galactoside 2′′-O-xylosyltransferase

Comments:

Isolated from the plant Daucus carota (Afghan cultivar carrot).

Links to other databases:

References:

1.	Rose, A., Glassgen, W.E., Hopp, W. and Seitz, H.U. Purification and characterization of glycosyltransferases involved in anthocyanin biosynthesis in cell-suspension cultures of Daucus carota L. Planta 198 (1996) 397–403. [PMID: 8717136]

[EC 2.4.2.50 created 2013]

2.4.2.51

Accepted name:

anthocyanidin 3-O-glucoside 2′′′-O-xylosyltransferase

Reaction:

UDP-α-D-xylose + an anthocyanidin 3-O-β-D-glucoside = UDP + an anthocyanidin 3-O-β-D-sambubioside

For diagram of anthocyanidin sambubioside biosynthesis, click here

Glossary:

anthocyanidin 3-O-β-D-sambubioside = anthocyanidin 3-O-(β-D-xylosyl-(1→2)-β-D-glucoside)

Other name(s):

uridine 5′-diphosphate-xylose:anthocyanidin 3-O-glucose-xylosyltransferase; UGT79B1

Systematic name:

UDP-α-D-xylose:anthocyanidin-3-O-β-D-glucoside 2′′′-O-xylosyltransferase

Comments:

Isolated from the plants Matthiola incana (stock) [1] and Arabidopsis thaliana (mouse-eared cress) [2]. The enzyme has similar activity with the 3-glucosides of pelargonidin, cyanidin, delphinidin, quercetin and kaempferol as well as with cyanidin 3-O-rhamnosyl-(1→6)-glucoside and cyanidin 3-O-(6-acylglucoside). There is no activity with other UDP-sugars or with cyanidin 3,5-diglucoside.

Links to other databases:

References:

1.	Teusch, M. Uridine 5′-diphosphate-xylose:anthocyanidin 3-O-glucose-xylosyltransferase from petals of Matthiola incana R.Br. Planta 169 (1986) 559–563. [PMID: 24232765]
2.	Yonekura-Sakakibara, K., Fukushima, A., Nakabayashi, R., Hanada, K., Matsuda, F., Sugawara, S., Inoue, E., Kuromori, T., Ito, T., Shinozaki, K., Wangwattana, B., Yamazaki, M. and Saito, K. Two glycosyltransferases involved in anthocyanin modification delineated by transcriptome independent component analysis in Arabidopsis thaliana. Plant J. 69 (2012) 154–167. [DOI] [PMID: 21899608]

[EC 2.4.2.51 created 2013]

2.6.1.100

Accepted name:

L-glutamine:2-deoxy-scyllo-inosose aminotransferase

Reaction:

L-glutamine + 2-deoxy-scyllo-inosose = 2-oxoglutaramate + 2-deoxy-scyllo-inosamine

For diagram of paromamine biosynthesis, click here

Glossary:

2-deoxy-scyllo-inosose = (2S,3R,4S,5R)-2,3,4,5-tetrahydroxycyclohexan-1-one

Other name(s):

btrR (gene name); neoB (gene name); kanB (gene name)

Systematic name:

L-glutamine:2-deoxy-scyllo-inosose aminotransferase

Comments:

Involved in the biosynthetic pathways of several clinically important aminocyclitol antibiotics, including kanamycin, butirosin, neomycin and ribostamycin. Also catalyses EC 2.6.1.101, L-glutamine:5-amino-2,3,4-trihydroxycyclohexanone aminotransferase [2].

Links to other databases:

References:

1.	Tamegai, H., Eguchi, T. and Kakinuma, K. First identification of Streptomyces genes involved in the biosynthesis of 2-deoxystreptamine-containing aminoglycoside antibiotics^--genetic and evolutionary analysis of L-glutamine:2-deoxy-scyllo-inosose aminotransferase genes. J. Antibiot. (Tokyo) 55 (2002) 1016–1018. [PMID: 12546424]
2.	Huang, F., Haydock, S.F., Mironenko, T., Spiteller, D., Li, Y. and Spencer, J.B. The neomycin biosynthetic gene cluster of Streptomyces fradiae NCIMB 8233: characterisation of an aminotransferase involved in the formation of 2-deoxystreptamine. Org. Biomol. Chem. 3 (2005) 1410–1418. [DOI] [PMID: 15827636]
3.	Kudo, F., Yamamoto, Y., Yokoyama, K., Eguchi, T. and Kakinuma, K. Biosynthesis of 2-deoxystreptamine by three crucial enzymes in Streptomyces fradiae NBRC 12773. J. Antibiot. (Tokyo) 58 (2005) 766–774. [DOI] [PMID: 16506694]
4.	Jnawali, H.N., Subba, B., Liou, K. and Sohng, J.K. Functional characterization of kanB by complementing in engineered Streptomyces fradiae Δneo6::tsr. Biotechnol. Lett. 31 (2009) 869–875. [DOI] [PMID: 19219581]

[EC 2.6.1.100 created 2013]

2.6.1.101

Accepted name:

L-glutamine:3-amino-2,3-dideoxy-scyllo-inosose aminotransferase

Reaction:

L-glutamine + 3-amino-2,3-dideoxy-scyllo-inosose = 2-oxoglutaramate + 2-deoxystreptamine

For diagram of paromamine biosynthesis, click here

Glossary:

3-amino-2,3-dideoxy-scyllo-inosose = (2R,3S,4R,5S)-5-amino-2,3,4-trihydroxycyclohexan-1-one

Systematic name:

L-glutamine:5-amino-2,3,4-trihydroxycyclohexanone aminotransferase

Comments:

Involved in the biosynthetic pathways of several clinically important aminocyclitol antibiotics, including kanamycin, butirosin, neomycin and ribostamycin. Also catalyses EC 2.6.1.100, L-glutamine:2-deoxy-scyllo-inosose aminotransferase.

Links to other databases:

References:

1.	Huang, F., Haydock, S.F., Mironenko, T., Spiteller, D., Li, Y. and Spencer, J.B. The neomycin biosynthetic gene cluster of Streptomyces fradiae NCIMB 8233: characterisation of an aminotransferase involved in the formation of 2-deoxystreptamine. Org. Biomol. Chem. 3 (2005) 1410–1418. [DOI] [PMID: 15827636]
2.	Kudo, F., Yamamoto, Y., Yokoyama, K., Eguchi, T. and Kakinuma, K. Biosynthesis of 2-deoxystreptamine by three crucial enzymes in Streptomyces fradiae NBRC 12773. J. Antibiot. (Tokyo) 58 (2005) 766–774. [DOI] [PMID: 16506694]

[EC 2.6.1.101 created 2013]

2.7.7.84

Accepted name:

2′-5′ oligoadenylate synthase

Reaction:

3 ATP = pppA2′p5’A2′p5’A + 2 diphosphate

Glossary:

pppA2′p5’A2′p5’A = 5′-triphosphoadenylyl-(2′→5′)-adenylyl-(2′→5′)-adenosine

Other name(s):

OAS

Systematic name:

ATP:ATP adenylyltransferase (2′-5′ linkages-forming)

Comments:

The enzyme is activated by binding to double-stranded RNA. The resulting product binds to and activates RNase L, which subsequently degrades the RNA. Oligoadenylates of chain lengths 2, 4 and 5 are also produced. The dimer does not have any known biological activity [2].

Links to other databases:

References:

1.	Kerr, I.M. and Brown, R.E. pppA2′p5’A2′p5’A: an inhibitor of protein synthesis synthesized with an enzyme fraction from interferon-treated cells. Proc. Natl. Acad. Sci. USA 75 (1978) 256–260. [DOI] [PMID: 272640]
2.	Martin, E.M., Birdsall, N.J., Brown, R.E. and Kerr, I.M. Enzymic synthesis, characterisation and nuclear-magnetic-resonance spectra of pppA2′p5’A2′p5’A and related oligonucleotides: comparison with chemically synthesised material. Eur. J. Biochem. 95 (1979) 295–307. [DOI] [PMID: 456356]
3.	Hartmann, R., Justesen, J., Sarkar, S.N., Sen, G.C. and Yee, V.C. Crystal structure of the 2′-specific and double-stranded RNA-activated interferon-induced antiviral protein 2′-5′-oligoadenylate synthetase. Mol. Cell 12 (2003) 1173–1185. [DOI] [PMID: 14636576]
4.	Hovanessian, A.G. and Justesen, J. The human 2′-5′oligoadenylate synthetase family: unique interferon-inducible enzymes catalyzing 2′-5′ instead of 3′-5′ phosphodiester bond formation. Biochimie 89 (2007) 779–788. [DOI] [PMID: 17408844]

[EC 2.7.7.84 created 2013]

2.7.8.38

Accepted name:

archaetidylserine synthase

Reaction:

(1) CDP-2,3-bis-(O-geranylgeranyl)-sn-glycerol + L-serine = CMP + 2,3-bis-(O-geranylgeranyl)-sn-glycero-1-phospho-L-serine
(2) CDP-2,3-bis-(O-phytanyl)-sn-glycerol + L-serine = CMP + 2,3-bis-(O-phytanyl)-sn-glycero-1-phospho-L-serine

For diagram of archaetidylserine biosynthesis, click here

Glossary:

CDP-2,3-bis-(O-geranylgeranyl)-sn-glycerol = CDP-unsaturated archaeol
2,3-bis-(O-geranylgeranyl)-sn-glycero-1-phospho-L-serine = unsaturated archaetidylserine
CDP-2,3-bis-(O-phytanyl)-sn-glycerol = CDP archaeol
2,3-bis-(O-phytanyl)-sn-glycero-1-phospho-L-serine = archaetidylserine

Systematic name:

CDP-2,3-bis-(O-geranylgeranyl)-sn-glycerol:L-serine 2,3-bis-(O-geranylgeranyl)-sn-glycerol phosphotransferase

Comments:

Requires Mn²⁺. Isolated from the archaeon Methanothermobacter thermautotrophicus.

Links to other databases:

References:

1.	Morii, H. and Koga, Y. CDP-2,3-di-O-geranylgeranyl-sn-glycerol:L-serine O-archaetidyltransferase (archaetidylserine synthase) in the methanogenic archaeon Methanothermobacter thermautotrophicus. J. Bacteriol. 185 (2003) 1181–1189. [DOI] [PMID: 12562787]

[EC 2.7.8.38 created 2013, modified 2013]

3.1.4.55

Accepted name:

phosphoribosyl 1,2-cyclic phosphate phosphodiesterase

Reaction:

5-phospho-α-D-ribose 1,2-cyclic phosphate + H₂O = α-D-ribose 1,5-bisphosphate

For diagram of phosphonate metabolism, click here

Other name(s):

phnP (gene name)

Systematic name:

5-phospho-α-D-ribose 1,2-cyclic phosphate 2-phosphohydrolase (α-D-ribose 1,5-bisphosphate-forming)

Comments:

Binds Mn²⁺ and Zn²⁺. Isolated from the bacterium Escherichia coli, where it participates in the degradation of methylphosphonate.

Links to other databases:

References:

1.	Podzelinska, K., He, S.M., Wathier, M., Yakunin, A., Proudfoot, M., Hove-Jensen, B., Zechel, D.L. and Jia, Z. Structure of PhnP, a phosphodiesterase of the carbon-phosphorus lyase pathway for phosphonate degradation. J. Biol. Chem. 284 (2009) 17216–17226. [DOI] [PMID: 19366688]
2.	Hove-Jensen, B., McSorley, F.R. and Zechel, D.L. Physiological role of phnP-specified phosphoribosyl cyclic phosphodiesterase in catabolism of organophosphonic acids by the carbon-phosphorus lyase pathway. J. Am. Chem. Soc. 133 (2011) 3617–3624. [DOI] [PMID: 21341651]
3.	He, S.M., Wathier, M., Podzelinska, K., Wong, M., McSorley, F.R., Asfaw, A., Hove-Jensen, B., Jia, Z. and Zechel, D.L. Structure and mechanism of PhnP, a phosphodiesterase of the carbon-phosphorus lyase pathway. Biochemistry 50 (2011) 8603–8615. [DOI] [PMID: 21830807]

[EC 3.1.4.55 created 2013]

3.1.7.4

Deleted entry:

Now recognized as two enzymes EC 4.2.1.133, copal-8-ol diphosphate synthase and EC 4.2.3.141 sclareol synthase

[EC 3.1.7.4 created 2008, deleted 2013]

3.5.4.33

Accepted name:

tRNA(adenine³⁴) deaminase

Reaction:

adenine³⁴ in tRNA + H₂O = hypoxanthine³⁴ in tRNA + NH₃

Other name(s):

tRNA:A34 deaminase; tadA protein; ADAT2-ADAT3 complex; TADA; tRNA adenosine deaminase arginine; AtTadA; tadA/ecADAT2; tRNA A:34 deaminase

Systematic name:

tRNA(adenine³⁴) aminohydrolase

Comments:

The enzyme is involved in editing of tRNA. The active site contains Zn²⁺ [1].

Links to other databases:

References:

1.	Spears, J.L., Rubio, M.A., Gaston, K.W., Wywial, E., Strikoudis, A., Bujnicki, J.M., Papavasiliou, F.N. and Alfonzo, J.D. A single zinc ion is sufficient for an active Trypanosoma brucei tRNA editing deaminase. J. Biol. Chem. 286 (2011) 20366–20374. [DOI] [PMID: 21507956]
2.	Delannoy, E., Le Ret, M., Faivre-Nitschke, E., Estavillo, G.M., Bergdoll, M., Taylor, N.L., Pogson, B.J., Small, I., Imbault, P. and Gualberto, J.M. Arabidopsis tRNA adenosine deaminase arginine edits the wobble nucleotide of chloroplast tRNA^Arg(ACG) and is essential for efficient chloroplast translation. Plant Cell 21 (2009) 2058–2071. [DOI] [PMID: 19602623]
3.	Kuratani, M., Ishii, R., Bessho, Y., Fukunaga, R., Sengoku, T., Shirouzu, M., Sekine, S. and Yokoyama, S. Crystal structure of tRNA adenosine deaminase (TadA) from Aquifex aeolicus. J. Biol. Chem. 280 (2005) 16002–16008. [DOI] [PMID: 15677468]
4.	Wolf, J., Gerber, A.P. and Keller, W. tadA, an essential tRNA-specific adenosine deaminase from Escherichia coli. EMBO J. 21 (2002) 3841–3851. [DOI] [PMID: 12110595]
5.	Lee, W.H., Kim, Y.K., Nam, K.H., Priyadarshi, A., Lee, E.H., Kim, E.E., Jeon, Y.H., Cheong, C. and Hwang, K.Y. Crystal structure of the tRNA-specific adenosine deaminase from Streptococcus pyogenes. Proteins 68 (2007) 1016–1019. [DOI] [PMID: 17554781]
6.	Ragone, F.L., Spears, J.L., Wohlgamuth-Benedum, J.M., Kreel, N., Papavasiliou, F.N. and Alfonzo, J.D. The C-terminal end of the Trypanosoma brucei editing deaminase plays a critical role in tRNA binding. RNA 17 (2011) 1296–1306. [DOI] [PMID: 21602302]

[EC 3.5.4.33 created 2013]

3.5.4.34

Accepted name:

tRNA^Ala(adenine³⁷) deaminase

Reaction:

adenine³⁷ in tRNA^Ala + H₂O = hypoxanthine³⁷ in tRNA^Ala + NH₃

Other name(s):

ADAT1; Tad1p

Systematic name:

tRNA^Ala(adenine³⁷) aminohydrolase

Comments:

The enzyme deaminates adenosine³⁷ to inosine in eukaryotic tRNA^Ala [1]. tRNA editing is strictly dependent on Mg²⁺ [2].

Links to other databases:

References:

1.	Maas, S., Gerber, A.P. and Rich, A. Identification and characterization of a human tRNA-specific adenosine deaminase related to the ADAR family of pre-mRNA editing enzymes. Proc. Natl. Acad. Sci. USA 96 (1999) 8895–8900. [DOI] [PMID: 10430867]
2.	Gerber, A., Grosjean, H., Melcher, T. and Keller, W. Tad1p, a yeast tRNA-specific adenosine deaminase, is related to the mammalian pre-mRNA editing enzymes ADAR1 and ADAR2. EMBO J. 17 (1998) 4780–4789. [DOI] [PMID: 9707437]
3.	Keegan, L.P., Gerber, A.P., Brindle, J., Leemans, R., Gallo, A., Keller, W. and O'Connell, M.A. The properties of a tRNA-specific adenosine deaminase from Drosophila melanogaster support an evolutionary link between pre-mRNA editing and tRNA modification. Mol. Cell Biol. 20 (2000) 825–833. [DOI] [PMID: 10629039]

[EC 3.5.4.34 created 2013]

3.5.4.35

Accepted name:

tRNA(cytosine⁸) deaminase

Reaction:

cytosine⁸ in tRNA + H₂O = uracil⁸ in tRNA + NH₃

Other name(s):

CDAT8

Systematic name:

tRNA(cytosine⁸) aminohydrolase

Comments:

The enzyme from Methanopyrus kandleri specifically catalyses the deamination of cytosine at position 8 of tRNA in 30 different tRNAs. This cytosine-to-uracil editing guarantees the proper folding and functionality of the tRNAs.

Links to other databases:

References:

1.	Randau, L., Stanley, B.J., Kohlway, A., Mechta, S., Xiong, Y. and Söll, D. A cytidine deaminase edits C to U in transfer RNAs in Archaea. Science 324 (2009) 657–659. [DOI] [PMID: 19407206]

[EC 3.5.4.35 created 2013]

3.5.4.36

Accepted name:

mRNA(cytosine⁶⁶⁶⁶) deaminase

Reaction:

cytosine⁶⁶⁶⁶ in apolipoprotein B mRNA + H₂O = uracil⁶⁶⁶⁶ in apolipoprotein B mRNA + NH₃

Other name(s):

APOBEC-1 (catalytic component of an RNA-editing complex); APOBEC1 (catalytic subunit); apolipoprotein B mRNA-editing enzyme 1 (catalytic component of an RNA-editing complex); apoB mRNA-editing enzyme catalytic polypeptide 1 (catalytic component of an RNA-editing complex); apoB mRNA editing complex; apolipoprotein B mRNA editing enzyme; REPR

Systematic name:

mRNA(cytosine⁶⁶⁶⁶) aminohydrolase

Comments:

The apolipoprotein B mRNA editing enzyme complex catalyses the editing of apolipoprotein B mRNA at cytidine⁶⁶⁶⁶ to uridine, thereby transforming the codon for glutamine-2153 to a termination codon. Editing results in translation of a truncated apolipoprotein B isoform (apoB-48) with distinct functions in lipid transport. The catalytic component (APOBEC-1) contains zinc at the active site [3].

Links to other databases:

References:

1.	Chester, A., Weinreb, V., Carter, C.W., Jr. and Navaratnam, N. Optimization of apolipoprotein B mRNA editing by APOBEC1 apoenzyme and the role of its auxiliary factor, ACF. RNA 10 (2004) 1399–1411. [DOI] [PMID: 15273326]
2.	Fujino, T., Navaratnam, N., Jarmuz, A., von Haeseler, A. and Scott, J. C-→U editing of apolipoprotein B mRNA in marsupials: identification and characterisation of APOBEC-1 from the American opossum Monodelphus domestica. Nucleic Acids Res. 27 (1999) 2662–2671. [DOI] [PMID: 10373583]
3.	Barnes, C. and Smith, H.C. Apolipoprotein B mRNA editing in vitro is a zinc-dependent process. Biochem. Biophys. Res. Commun. 197 (1993) 1410–1414. [DOI] [PMID: 8280158]
4.	Chester, A., Somasekaram, A., Tzimina, M., Jarmuz, A., Gisbourne, J., O'Keefe, R., Scott, J. and Navaratnam, N. The apolipoprotein B mRNA editing complex performs a multifunctional cycle and suppresses nonsense-mediated decay. EMBO J. 22 (2003) 3971–3982. [DOI] [PMID: 12881431]

[EC 3.5.4.36 created 2013]

3.6.1.64

Accepted name:

inosine diphosphate phosphatase

Reaction:

(1) IDP + H₂O = IMP + phosphate
(2) dIDP + H₂O = dIMP + phosphate

Other name(s):

(deoxy)inosine diphosphatase; NUDT16

Systematic name:

inosine diphosphate phosphatase

Comments:

The human enzyme also hydrolyses GDP and dGDP, and to a lesser extent ITP, dITP and XTP.

Links to other databases:

References:

1.	Iyama, T., Abolhassani, N., Tsuchimoto, D., Nonaka, M. and Nakabeppu, Y. NUDT16 is a (deoxy)inosine diphosphatase, and its deficiency induces accumulation of single-strand breaks in nuclear DNA and growth arrest. Nucleic Acids Res. 38 (2010) 4834–4843. [DOI] [PMID: 20385596]

[EC 3.6.1.64 created 2013]

4.1.3.42

Accepted name:

(4S)-4-hydroxy-2-oxoglutarate aldolase

Reaction:

(4S)-4-hydroxy-2-oxoglutarate = pyruvate + glyoxylate

Glossary:

(4S)-4-hydroxy-2-oxoglutatrate = (S)-2-hydroxy-4-oxopentanedioate = L-4-hydroxy-2-oxoglutarate

Other name(s):

2-oxo-4-hydroxyglutarate aldolase (ambiguous); hydroxyketoglutaric aldolase (ambiguous); 4-hydroxy-2-ketoglutaric aldolase (ambiguous); 2-keto-4-hydroxyglutaric aldolase (ambiguous); 4-hydroxy-2-ketoglutarate aldolase (ambiguous); 2-keto-4-hydroxyglutarate aldolase (ambiguous); 2-oxo-4-hydroxyglutaric aldolase (ambiguous); hydroxyketoglutarate aldolase (ambiguous); 2-keto-4-hydroxybutyrate aldolase (ambiguous); 4-hydroxy-2-oxoglutarate glyoxylate-lyase (ambiguous); eda (gene name)

Systematic name:

(4S)-4-hydroxy-2-oxoglutarate glyoxylate-lyase (pyruvate-forming)

Comments:

The enzyme from the bacterium Escherichia coli, which is specific for the (S)-enantiomer, is trifunctional, and also catalyses the reaction of EC 4.1.2.14, 2-dehydro-3-deoxy-phosphogluconate aldolase, and the β-decarboxylation of oxaloacetate. cf. EC 4.1.3.16, 4-hydroxy-2-oxoglutarate aldolase.

Links to other databases:

BRENDA, EXPASY, Gene, GTD, KEGG, PDB, CAS registry number: 9030-81-3

References:

1.	Nishihara, H. and Dekker, E.E. Purification, substrate specificity and binding, β-decarboxylase activity, and other properties of Escherichia coli 2-keto-4-hydroxyglutarate aldolase. J. Biol. Chem. 247 (1972) 5079–5087. [PMID: 4560498]
2.	Patil, R.V. and Dekker, E.E. Cloning, nucleotide sequence, overexpression, and inactivation of the Escherichia coli 2-keto-4-hydroxyglutarate aldolase gene. J. Bacteriol. 174 (1992) 102–107. [DOI] [PMID: 1339418]

[EC 4.1.3.42 created 2013]

4.2.3.141

Accepted name:

sclareol synthase

Reaction:

(13E)-8α-hydroxylabd-13-en-15-yl diphosphate + H₂O = sclareol + diphosphate

For diagram of hydroxylabdenyl diphosphate derived diterpenoids, click here

Glossary:

sclareol = (13R)-labd-14-ene-8α,13-diol
(13E)-8α-hydroxylabd-13-en-15-yl diphosphate = 8-hydroxycopalyl diphosphate

Other name(s):

Systematic name:

(13E)-8α-hydroxylabd-13-en-15-yl-diphosphate-lyase (sclareol-forming)

Comments:

Isolated from the plant Salvia sclarea (clary sage). Originally thought to be synthesized in one step from geranylgeranyl diphosphate it is now known to require two enzymes, EC 4.2.1.133, copal-8-ol diphosphate synthase and EC 4.2.3.141, sclareol synthase. Sclareol is used in perfumery.

Links to other databases:

References:

Caniard, A., Zerbe, P., Legrand, S., Cohade, A., Valot, N., Magnard, J.L., Bohlmann, J. and Legendre, L. Discovery and functional characterization of two diterpene synthases for sclareol biosynthesis in Salvia sclarea (L.) and their relevance for perfume manufacture. BMC Plant Biol. 12:119 (2012). [DOI] [PMID: 22834731]

[EC 4.2.3.141 created 2013, modified 2017]

4.2.3.142

Accepted name:

7-epizingiberene synthase [(2Z,6Z)-farnesyl diphosphate cyclizing]

Reaction:

(2Z,6Z)-farnesyl diphosphate = 7-epizingiberene + diphosphate

Glossary:

7-epizingiberene = (5R)-2-methyl-5-[(2R)-6-methylhept-5-en-2-yl]cyclohexa-1,3-diene

Other name(s):

ShZIS (gene name)

Systematic name:

(2Z,6Z)-farnesyl-diphosphate lyase (cyclizing; 7-epizingiberene-forming)

Comments:

Isolated from the plant Solanum habrochaites. 7-Epizingiberene is a whitefly repellant.

Links to other databases:

References:

Bleeker, P.M., Mirabella, R., Diergaarde, P.J., Vandoorn, A., Tissier, A., Kant, M.R., Prins, M., de Vos, M., Haring, M.A. and Schuurink, R.C. Improved herbivore resistance in cultivated tomato with the sesquiterpene biosynthetic pathway from a wild relative. Proc. Natl. Acad. Sci. USA 109 (2012) 20124–20129. [DOI] [PMID: 23169639]

[EC 4.2.3.142 created 2013]

4.3.99.4

Accepted name:

choline trimethylamine-lyase

Reaction:

choline = trimethylamine + acetaldehyde

Other name(s):

cutC (gene name)

Systematic name:

choline trimethylamine-lyase (acetaldehyde-forming)

Comments:

The enzyme utilizes a glycine radical to break the C-N bond in choline. Found in choline-degrading anaerobic bacteria.

Links to other databases:

References:

1.	Craciun, S. and Balskus, E.P. Microbial conversion of choline to trimethylamine requires a glycyl radical enzyme. Proc. Natl. Acad. Sci. USA 109 (2012) 21307–21312. [DOI] [PMID: 23151509]

[EC 4.3.99.4 created 2013]

4.7 carbon-phosphorus lyases

4.7.1 carbon-phosphorus lyases (only sub-subclass identified to date)

4.7.1.1

Accepted name:

α-D-ribose 1-methylphosphonate 5-phosphate C-P-lyase

Reaction:

α-D-ribose 1-methylphosphonate 5-phosphate + S-adenosyl-L-methionine + reduced electron acceptor = α-D-ribose 1,2-cyclic phosphate 5-phosphate + methane + L-methionine + 5′-deoxyadenosine + oxidized electron acceptor

For diagram of phosphonate metabolism, click here

Other name(s):

phnJ (gene name)

Systematic name:

α-D-ribose-1-methylphosphonate-5-phosphate C-P-lyase (methane-forming)

Comments:

This radical SAM (AdoMet) enzyme is part of the C-P lyase complex, which is responsible for processing phophonates into usable phosphate. Contains an [4Fe-4S] cluster. The enzyme from the bacterium Escherichia coli can act on additional α-D-ribose phosphonate substrates with different substituents attached to the phosphonate phosphorus (e.g. α-D-ribose-1-[N-(phosphonomethyl)glycine]-5-phosphate and α-D-ribose-1-(2-N-acetamidomethylphosphonate)-5-phosphate).

Links to other databases:

References:

1.	Kamat, S.S., Williams, H.J. and Raushel, F.M. Intermediates in the transformation of phosphonates to phosphate by bacteria. Nature 480 (2011) 570–573. [DOI] [PMID: 22089136]
2.	Jochimsen, B., Lolle, S., McSorley, F.R., Nabi, M., Stougaard, J., Zechel, D.L. and Hove-Jensen, B. Five phosphonate operon gene products as components of a multi-subunit complex of the carbon-phosphorus lyase pathway. Proc. Natl. Acad. Sci. USA 108 (2011) 11393–11398. [DOI] [PMID: 21705661]
3.	Zhang, Q. and van der Donk, W.A. Answers to the carbon-phosphorus lyase conundrum. ChemBioChem 13 (2012) 627–629. [DOI] [PMID: 22334536]

[EC 4.7.1.1 created 2013, modified 2016]

5.3.2.7

Accepted name:

ascopyrone tautomerase

Reaction:

1,5-anhydro-4-deoxy-D-glycero-hex-3-en-2-ulose = 1,5-anhydro-4-deoxy-D-glycero-hex-1-en-3-ulose

For diagram of the anhydrofructose pathway, click here

Glossary:

ascopyrone M = 1,5-anhydro-4-deoxy-D-glycero-hex-3-en-2-ulose = (6S)-4-hydroxy-6-(hydroxymethyl)-2H-pyran-3(6H)-one
ascopyrone P = 1,5-anhydro-4-deoxy-D-glycero-hex-1-en-3-ulose = (2S)-5-hydroxy-2-(hydroxymethyl)-2H-pyran-4(3H)-one

Other name(s):

ascopyrone isomerase; ascopyrone intramolecular oxidoreductase; 1,5-anhydro-D-glycero-hex-3-en-2-ulose tautomerase; APM tautomerase; ascopyrone P tautomerase; APTM

Systematic name:

1,5-anhydro-4-deoxy-D-glycero-hex-3-en-2-ulose Δ³-Δ¹-isomerase

Comments:

This enzyme catalyses one of the steps in the anhydrofructose pathway, which leads to the degradation of glycogen and starch via 1,5-anhydro-D-fructose [1,2]. The other enzymes involved in this pathway are EC 4.2.1.110 (aldos-2-ulose dehydratase), EC 4.2.1.111 (1,5-anhydro-D-fructose dehydratase) and EC 4.2.2.13 [exo-(1→4)-α-D-glucan lyase]. Ascopyrone P is an anti-oxidant [2].

Links to other databases:

References:

1.	Yu, S., Refdahl, C. and Lundt, I. Enzymatic description of the anhydrofructose pathway of glycogen degradation; I. Identification and purification of anhydrofructose dehydratase, ascopyrone tautomerase and α-1,4-glucan lyase in the fungus Anthracobia melaloma. Biochim. Biophys. Acta 1672 (2004) 120–129. [DOI] [PMID: 15110094]
2.	Yu, S. and Fiskesund, R. The anhydrofructose pathway and its possible role in stress response and signaling. Biochim. Biophys. Acta 1760 (2006) 1314–1322. [DOI] [PMID: 16822618]

[EC 5.3.2.7 created 2006 as EC 5.3.3.15, transferred 2012 to EC 5.3.2.7]

5.3.2.8

Accepted name:

4-oxalomesaconate tautomerase

Reaction:

(1E)-4-oxobut-1-ene-1,2,4-tricarboxylate = (1E,3E)-4-hydroxybuta-1,3-diene-1,2,4-tricarboxylate

For diagram of the protocatechuate 3,4-cleavage pathway, click here

Glossary:

(1E)-4-oxobut-1-ene-1,2,4-tricarboxylate = keto tautomer of 4-oxalomesaconate
(1E,3E)-4-hydroxybuta-1,3-diene-1,2,4-tricarboxylate = one of the enol tautomers of 4-oxalomesaconate

Other name(s):

GalD

Systematic name:

4-oxalomesaconate keto—enol-isomerase

Comments:

This enzyme has been characterized from the bacterium Pseudomonas putida KT2440 and is involved in the degradation pathway of syringate and 3,4,5-trihydroxybenzoate. It catalyses the interconversion of two of the tautomers of 4-oxalomesaconate, a reaction that can also occur spontaneously.

Links to other databases:

References:

1.	Nogales, J., Canales, A., Jiménez-Barbero, J., Serra B., Pingarrón, J. M., García, J. L. and Díaz, E. Unravelling the gallic acid degradation pathway in bacteria: the gal cluster from Pseudomonas putida. Mol. Microbiol. 79 (2011) 359–374. [DOI] [PMID: 21219457]

[EC 5.3.2.8 created 2011 as EC 5.3.3.16, modified 2011, transferred 2012 to EC 5.3.2.8]

5.3.3.15

Transferred entry:

ascopyrone tautomerase. Now EC 5.3.2.7, ascopyrone tautomerase

[EC 5.3.3.15 created 2006, deleted 2013]

5.3.3.16

Transferred entry:

4-oxalomesaconate tautomerase. Now EC 5.3.2.8, 4-oxalomesaconate tautomerase

[EC 5.3.3.16 created 2011, modified 2011, deleted 2013]

5.4.3.10

Accepted name:

phenylalanine aminomutase (L-β-phenylalanine-forming)

Reaction:

L-phenylalanine = L-β-phenylalanine

Glossary:

L-β-phenylalanine = (R)-3-amino-3-phenylpropanoate

Systematic name:

L-phenylalanine 2,3-aminomutase [(R)-3-amino-3-phenylpropanoate-forming]

Comments:

The enzyme contains the cofactor 3,5-dihydro-5-methylidene-4H-imidazol-4-one (MIO). This unique cofactor is formed autocatalytically by cyclization and dehydration of the three amino-acid residues alanine, serine and glycine. cf. EC 5.4.3.11, phenylalanine aminomutase (D-β-phenylalanine-forming).

Links to other databases:

References:

1.	Feng, L., Wanninayake, U., Strom, S., Geiger, J. and Walker, K.D. Mechanistic, mutational, and structural evaluation of a Taxus phenylalanine aminomutase. Biochemistry 50 (2011) 2919–2930. [DOI] [PMID: 21361343]

[EC 5.4.3.10 created 2013]

5.4.3.11

Accepted name:

phenylalanine aminomutase (D-β-phenylalanine-forming)

Reaction:

L-phenylalanine = D-β-phenylalanine

Glossary:

D-β-phenylalanine = (S)-3-amino-3-phenylpropanoate

Other name(s):

admH (gene name); L-phenylalanine 2,3-aminomutase [(S)-3-amino-3-phenylpropanoate]

Systematic name:

L-phenylalanine 2,3-aminomutase [(S)-3-amino-3-phenylpropanoate-forming]

Comments:

The enzyme from the bacterium Pantoea agglomerans produces D-β-phenylalanine, an intermediate in the biosynthesis of the polyketide non-ribosomal antibiotic andrimid. The enzyme contains the cofactor 3,5-dihydro-5-methylidene-4H-imidazol-4-one (MIO), which is formed autocatalytically by cyclization and dehydration of the three amino-acid residues alanine, serine and glycine. cf. EC 5.4.3.10, phenylalanine aminomutase (L-β-phenylalanine-forming).

Links to other databases: