The Enzyme Database

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EC 1.10.3.6     
Accepted name: rifamycin-B oxidase
Reaction: rifamycin B + O2 = rifamycin O + H2O2
Other name(s): rifamycin B oxidase
Systematic name: rifamycin-B:oxygen oxidoreductase
Comments: Acts also on benzene-1,4-diol and, more slowly, on some other p-quinols. Not identical with EC 1.10.3.1 (catechol oxidase), EC 1.10.3.2 (laccase), EC 1.10.3.4 (o-aminophenol oxidase) or EC 1.10.3.5 (3-hydroxyanthranilate oxidase).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 84932-52-5
References:
1.  Han, M.H., Seong, B.-L., Son, H.-J. and Mheen, T.-I. Rifamycin B oxidase from Monocillium spp., a new type of diphenol oxidase. FEBS Lett. 151 (1983) 36–40. [DOI] [PMID: 6825839]
[EC 1.10.3.6 created 1986]
 
 
EC 1.13.11.66     
Accepted name: hydroquinone 1,2-dioxygenase
Reaction: benzene-1,4-diol + O2 = (2Z,4E)-4-hydroxy-6-oxohexa-2,4-dienoate
For diagram of 4-nitrophenol metabolism, click here
Glossary: benzene-1,4-diol = hydroquinone
(2Z,4E)-4-hydroxy-6-oxohexa-2,4-dienoate = 4-hydroxymuconic semialdehyde
Other name(s): hydroquinone dioxygenase; benzene-1,4-diol:oxygen 1,2-oxidoreductase (decyclizing)
Systematic name: benzene-1,4-diol:oxygen 1,2-oxidoreductase (ring-opening)
Comments: The enzyme is an extradiol-type dioxygenase, and is a member of the nonheme-iron(II)-dependent dioxygenase family. It catalyses the ring cleavage of a wide range of hydroquinone substrates to produce the corresponding 4-hydroxymuconic semialdehydes.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Miyauchi, K., Adachi, Y., Nagata, Y. and Takagi, M. Cloning and sequencing of a novel meta-cleavage dioxygenase gene whose product is involved in degradation of γ-hexachlorocyclohexane in Sphingomonas paucimobilis. J. Bacteriol. 181 (1999) 6712–6719. [PMID: 10542173]
2.  Moonen, M.J., Synowsky, S.A., van den Berg, W.A., Westphal, A.H., Heck, A.J., van den Heuvel, R.H., Fraaije, M.W. and van Berkel, W.J. Hydroquinone dioxygenase from pseudomonas fluorescens ACB: a novel member of the family of nonheme-iron(II)-dependent dioxygenases. J. Bacteriol. 190 (2008) 5199–5209. [DOI] [PMID: 18502867]
3.  Shen, W., Liu, W., Zhang, J., Tao, J., Deng, H., Cao, H. and Cui, Z. Cloning and characterization of a gene cluster involved in the catabolism of p-nitrophenol from Pseudomonas putida DLL-E4. Bioresour. Technol. 101 (2010) 7516–7522. [DOI] [PMID: 20466541]
[EC 1.13.11.66 created 2012]
 
 
EC 1.14.13.116     
Accepted name: geranylhydroquinone 3′′-hydroxylase
Reaction: geranylhydroquinone + NADPH + H+ + O2 = 3′′-hydroxygeranylhydroquinone + NADP+ + H2O
Glossary: 3′′-hydroxygeranylhydroquinone = 2-[(2Z)-3-(hydroxymethyl)-7-methylocta-2,6-dien-1-yl]benzene-1,4-diol
Other name(s): GHQ 3′′-hydroxylase
Systematic name: geranylhydroquinone,NADPH:oxygen oxidoreductase (3′′-hydroxylating)
Comments: Contains cytochrome P-450.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Yamamoto, H., Inoue, K., Li, S.M. and Heide, L. Geranylhydroquinone 3′′-hydroxylase, a cytochrome P-450 monooxygenase from Lithospermum erythrorhizon cell suspension cultures. Planta 210 (2000) 312–317. [DOI] [PMID: 10664138]
[EC 1.14.13.116 created 2010]
 
 
EC 2.1.1.295     
Accepted name: 2-methyl-6-phytyl-1,4-hydroquinone methyltransferase
Reaction: (1) S-adenosyl-L-methionine + 2-methyl-6-phytylbenzene-1,4-diol = S-adenosyl-L-homocysteine + 2,3-dimethyl-6-phytylbenzene-1,4-diol
(2) S-adenosyl-L-methionine + 2-methyl-6-all-trans-nonaprenylbenzene-1,4-diol = S-adenosyl-L-homocysteine + plastoquinol
(3) S-adenosyl-L-methionine + 6-geranylgeranyl-2-methylbenzene-1,4-diol = S-adenosyl-L-homocysteine + 6-geranylgeranyl-2,3-dimethylbenzene-1,4-diol
For diagram of tocopherol biosynthesis, click here and for diagram of tocotrienol biosynthesis, click here
Other name(s): VTE3 (gene name); 2-methyl-6-solanyl-1,4-hydroquinone methyltransferase; MPBQ/MSBQ methyltransferase; MPBQ/MSBQ MT
Systematic name: S-adenosyl-L-methionine:2-methyl-6-phytyl-1,4-benzoquinol C-3-methyltransferase
Comments: Involved in the biosynthesis of plastoquinol, as well as vitamin E (tocopherols and tocotrienols).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Shintani, D.K., Cheng, Z. and DellaPenna, D. The role of 2-methyl-6-phytylbenzoquinone methyltransferase in determining tocopherol composition in Synechocystis sp. PCC6803. FEBS Lett. 511 (2002) 1–5. [DOI] [PMID: 11821038]
2.  Cheng, Z., Sattler, S., Maeda, H., Sakuragi, Y., Bryant, D.A. and DellaPenna, D. Highly divergent methyltransferases catalyze a conserved reaction in tocopherol and plastoquinone synthesis in cyanobacteria and photosynthetic eukaryotes. Plant Cell 15 (2003) 2343–2356. [DOI] [PMID: 14508009]
3.  Van Eenennaam, A.L., Lincoln, K., Durrett, T.P., Valentin, H.E., Shewmaker, C.K., Thorne, G.M., Jiang, J., Baszis, S.R., Levering, C.K., Aasen, E.D., Hao, M., Stein, J.C., Norris, S.R. and Last, R.L. Engineering vitamin E content: from Arabidopsis mutant to soy oil. Plant Cell 15 (2003) 3007–3019. [DOI] [PMID: 14630966]
[EC 2.1.1.295 created 2014]
 
 
EC 2.5.1.115     
Accepted name: homogentisate phytyltransferase
Reaction: phytyl diphosphate + homogentisate = diphosphate + 2-methyl-6-phytylbenzene-1,4-diol + CO2
For diagram of the homogentisate pathways, click here
Glossary: 2-methyl-6-phytylbenzene-1,4-diol = MPBQ
Other name(s): HPT; VTE2 (gene name)
Systematic name: phytyl diphosphate:homogentisate phytyltransferase
Comments: Requires Mg2+ for activity [3]. Involved in the biosynthesis of the vitamin E tocopherols. While the enzyme from the cyanobacterium Synechocystis PCC 6803 has an appreciable activity with geranylgeranyl diphosphate (EC 2.5.1.116, homogentisate geranylgeranyltransferase), the enzyme from the plant Arabidopsis thaliana has only a low activity with that substrate [1,3,4].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Collakova, E. and DellaPenna, D. Isolation and functional analysis of homogentisate phytyltransferase from Synechocystis sp. PCC 6803 and Arabidopsis. Plant Physiol. 127 (2001) 1113–1124. [PMID: 11706191]
2.  Savidge, B., Weiss, J.D., Wong, Y.H., Lassner, M.W., Mitsky, T.A., Shewmaker, C.K., Post-Beittenmiller, D. and Valentin, H.E. Isolation and characterization of homogentisate phytyltransferase genes from Synechocystis sp. PCC 6803 and Arabidopsis. Plant Physiol. 129 (2002) 321–332. [DOI] [PMID: 12011362]
3.  Sadre, R., Gruber, J. and Frentzen, M. Characterization of homogentisate prenyltransferases involved in plastoquinone-9 and tocochromanol biosynthesis. FEBS Lett. 580 (2006) 5357–5362. [DOI] [PMID: 16989822]
4.  Yang, W., Cahoon, R.E., Hunter, S.C., Zhang, C., Han, J., Borgschulte, T. and Cahoon, E.B. Vitamin E biosynthesis: functional characterization of the monocot homogentisate geranylgeranyl transferase. Plant J. 65 (2011) 206–217. [DOI] [PMID: 21223386]
[EC 2.5.1.115 created 2014]
 
 
EC 2.5.1.116     
Accepted name: homogentisate geranylgeranyltransferase
Reaction: geranylgeranyl diphosphate + homogentisate = diphosphate + 6-geranylgeranyl-2-methylbenzene-1,4-diol + CO2
For diagram of the homogentisate pathways, click here
Glossary: 6-geranylgeranyl-2-methylbenzene-1,4-diol = MGGBQ
Other name(s): HGGT; slr1736 (gene name)
Systematic name: geranylgeranyl diphosphate:homogentisate geranylgeranyltransferase
Comments: Requires Mg2+ for activity. Involved in the biosynthesis of the vitamin E, tocotrienols. While the enzyme from the bacterium Synechocystis PCC 6803 has higher activity with phytyl diphosphate (EC 2.5.1.115, homogentisate phytyltransferase), the enzymes from barley, rice and wheat have only a low activity with that substrate [2].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Collakova, E. and DellaPenna, D. Isolation and functional analysis of homogentisate phytyltransferase from Synechocystis sp. PCC 6803 and Arabidopsis. Plant Physiol. 127 (2001) 1113–1124. [PMID: 11706191]
2.  Cahoon, E.B., Hall, S.E., Ripp, K.G., Ganzke, T.S., Hitz, W.D. and Coughlan, S.J. Metabolic redesign of vitamin E biosynthesis in plants for tocotrienol production and increased antioxidant content. Nat. Biotechnol. 21 (2003) 1082–1087. [DOI] [PMID: 12897790]
3.  Yang, W., Cahoon, R.E., Hunter, S.C., Zhang, C., Han, J., Borgschulte, T. and Cahoon, E.B. Vitamin E biosynthesis: functional characterization of the monocot homogentisate geranylgeranyl transferase. Plant J. 65 (2011) 206–217. [DOI] [PMID: 21223386]
[EC 2.5.1.116 created 2014]
 
 
EC 2.5.1.117     
Accepted name: homogentisate solanesyltransferase
Reaction: all-trans-nonaprenyl diphosphate + homogentisate = diphosphate + 2-methyl-6-all-trans-nonaprenylbenzene-1,4-diol + CO2
For diagram of the homogentisate pathways, click here
Glossary: 2-methyl-6-all-trans-nonaprenylbenzene-1,4-diol = 2-methyl-6-solanesylbenzene-1,4-diol = MSBQ
Other name(s): HST; PDS2 (gene name)
Systematic name: all-trans-nonaprenyl diphosphate:homogentisate nonaprenyltransferase
Comments: Requires Mg2+ for activity. Part of the biosynthesis pathway of plastoquinol-9. The enzymes purified from the plant Arabidopsis thaliana and the alga Chlamydomonas reinhardtii are also active in vitro with unsaturated C10-C20 prenyl diphosphates, producing main products that are not decarboxylated [2].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Sadre, R., Gruber, J. and Frentzen, M. Characterization of homogentisate prenyltransferases involved in plastoquinone-9 and tocochromanol biosynthesis. FEBS Lett. 580 (2006) 5357–5362. [DOI] [PMID: 16989822]
2.  Sadre, R., Frentzen, M., Saeed, M. and Hawkes, T. Catalytic reactions of the homogentisate prenyl transferase involved in plastoquinone-9 biosynthesis. J. Biol. Chem. 285 (2010) 18191–18198. [DOI] [PMID: 20400515]
[EC 2.5.1.117 created 2014]
 
 
EC 5.5.1.24     
Accepted name: tocopherol cyclase
Reaction: (1) δ-tocopherol = 2-methyl-6-phytylbenzene-1,4-diol
(2) γ-tocopherol = 2,3-dimethyl-6-phytylbenzene-1,4-diol
(3) δ-tocotrienol = 6-geranylgeranyl-2-methylbenzene-1,4-diol
(4) γ-tocotrienol = 6-geranylgeranyl-2,3-dimethylbenzene-1,4-diol
For diagram of tocopherol biosynthesis, click here and for diagram of tocotrienol biosynthesis, click here
Other name(s): VTE1 (gene name); SXD1 (gene name); δ/γ-tocopherol lyase (decyclizing)
Systematic name: δ/γ-tocopherol lyase (ring-opening)
Comments: The enzyme has been described from plants and cyanobacteria. It has similar activity with all four listed benzoquinol substrates. Involved in the biosynthesis of vitamin E (tocopherols and tocotrienols).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Porfirova, S., Bergmuller, E., Tropf, S., Lemke, R. and Dormann, P. Isolation of an Arabidopsis mutant lacking vitamin E and identification of a cyclase essential for all tocopherol biosynthesis. Proc. Natl. Acad. Sci. USA 99 (2002) 12495–12500. [DOI] [PMID: 12213958]
2.  Sattler, S.E., Cahoon, E.B., Coughlan, S.J. and DellaPenna, D. Characterization of tocopherol cyclases from higher plants and cyanobacteria. Evolutionary implications for tocopherol synthesis and function. Plant Physiol. 132 (2003) 2184–2195. [DOI] [PMID: 12913173]
[EC 5.5.1.24 created 2013]
 
 


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