The Enzyme Database

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EC 1.3.3.16     
Accepted name: oxazoline dehydrogenase
Reaction: (1) a [protein]-(1S,4R)-2-(C-substituted-aminomethyl)-4-acyl-2-thiazoline + O2 = a [protein]-(S)-2-(C-substituted-aminomethyl)-4-acyl-1,3-thiazole + H2O2
(2) a [protein]-(S,S)-2-(C-substituted-aminomethyl)-4-acyl-2-oxazoline + O2 = a [protein]-(S)-2-(C-substituted-aminomethyl)-4-acyl-1,3-oxazole + H2O2
(3) a [protein]-(S,S)-2-(C-substituted-aminomethyl)-4-acyl-5-methyl-2-oxazoline + O2 = a [protein]-(S)-2-(C-substituted-aminomethyl)-4-acyl-5-methyl-1,3-oxazole + H2O2
Other name(s): azoline oxidase; thiazoline oxidase; cyanobactin oxidase; patG (gene name); mcaG (gene name); artG (gene name); lynG (gene name); tenG (gene name)
Systematic name: a [protein]-2-oxazoline:oxygen oxidoreductase (2-oxazole-forming)
Comments: Contains FMN. This enzyme oxidizes 2-oxazoline, 5-methyl-2-oxazoline, and 2-thiazoline within peptides, which were formed by EC 6.2.2.2, oxazoline synthase, and EC 6.2.2.3, thiazoline synthase, to the respective pyrrole-type rings. The enzyme is found as either a stand-alone protein or as a domain within a multifunctional protein (the G protein) that also functions as a peptidase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Li, Y.M., Milne, J.C., Madison, L.L., Kolter, R. and Walsh, C.T. From peptide precursors to oxazole and thiazole-containing peptide antibiotics: microcin B17 synthase. Science 274 (1996) 1188–1193. [PMID: 8895467]
2.  Schmidt, E.W., Nelson, J.T., Rasko, D.A., Sudek, S., Eisen, J.A., Haygood, M.G. and Ravel, J. Patellamide A and C biosynthesis by a microcin-like pathway in Prochloron didemni, the cyanobacterial symbiont of Lissoclinum patella. Proc. Natl. Acad. Sci. USA 102 (2005) 7315–7320. [PMID: 15883371]
3.  Bent, A.F., Mann, G., Houssen, W.E., Mykhaylyk, V., Duman, R., Thomas, L., Jaspars, M., Wagner, A. and Naismith, J.H. Structure of the cyanobactin oxidase ThcOx from Cyanothece sp. PCC 7425, the first structure to be solved at Diamond Light Source beamline I23 by means of S-SAD. Acta Crystallogr D Struct Biol 72 (2016) 1174–1180. [PMID: 27841750]
4.  Ghilarov, D., Stevenson, C.EM., Travin, D.Y., Piskunova, J., Serebryakova, M., Maxwell, A., Lawson, D.M. and Severinov, K. Architecture of microcin B17 synthetase: an octameric protein complex converting a ribosomally synthesized peptide into a DNA gyrase poison. Mol. Cell 73 (2019) 749–762.e5. [PMID: 30661981]
[EC 1.3.3.16 created 2020]
 
 
EC 1.13.11.84     
Accepted name: crocetin dialdehyde synthase
Reaction: zeaxanthin + 2 O2 = crocetin dialdehyde + 2 3β-hydroxy-β-cyclocitral (overall reaction)
(1a) zeaxanthin + O2 = 3β-hydroxy-8′-apo-β-carotenal + 3β-hydroxy-β-cyclocitral
(1b) 3β-hydroxy-8′-apo-β-carotenal + O2 = crocetin dialdehyde + 3β-hydroxy-β-cyclocitral
Glossary: crocetin dialdehyde = 8,8′-diapocarotene-8,8′-dial
zeaxanthin = (3R,3′R)-β,β-carotene-3,3′-diol
3β-hydroxy-β-cyclocitral = (4R)-4-hydroxy-2,6,6-trimethylcyclohex-1-en-1-carboxaldehyde
Other name(s): CCD2; zeaxanthin 7,8-dioxygenase
Systematic name: zeaxanthin:oxygen 7′,8′-oxidoreductase (bond-cleaving)
Comments: The enzyme, characterized from the plant Crocus sativus (saffron), acts twice, cleaving 3β-hydroxy-β-cyclocitral off each 3-hydroxy end group. It is part of the zeaxanthin degradation pathway in that plant, leading to the different compounds that impart the color, flavor and aroma of the saffron spice. The enzyme can similarly cleave the 7-8 double bond of other carotenoids with a 3-hydroxy-β-carotenoid end group.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Frusciante, S., Diretto, G., Bruno, M., Ferrante, P., Pietrella, M., Prado-Cabrero, A., Rubio-Moraga, A., Beyer, P., Gomez-Gomez, L., Al-Babili, S. and Giuliano, G. Novel carotenoid cleavage dioxygenase catalyzes the first dedicated step in saffron crocin biosynthesis. Proc. Natl. Acad. Sci. USA 111 (2014) 12246–12251. [DOI] [PMID: 25097262]
2.  Ahrazem, O., Rubio-Moraga, A., Berman, J., Capell, T., Christou, P., Zhu, C. and Gomez-Gomez, L. The carotenoid cleavage dioxygenase CCD2 catalysing the synthesis of crocetin in spring crocuses and saffron is a plastidial enzyme. New Phytol. 209 (2016) 650–663. [DOI] [PMID: 26377696]
3.  Ahrazem, O., Diretto, G., Argandona, J., Rubio-Moraga, A., Julve, J.M., Orzaez, D., Granell, A. and Gomez-Gomez, L. Evolutionarily distinct carotenoid cleavage dioxygenases are responsible for crocetin production in Buddleja davidii. J. Exp. Bot. 68 (2017) 4663–4677. [DOI] [PMID: 28981773]
[EC 1.13.11.84 created 2011 as EC 1.14.99.42, modified 2014, transferred 2017 to EC 1.13.11.84]
 
 
EC 1.14.13.196     
Accepted name: L-ornithine N5-monooxygenase [NAD(P)H]
Reaction: L-ornithine + NAD(P)H + H+ + O2 = N5-hydroxy-L-ornithine + NAD(P)+ + H2O
Other name(s): SidA (ambiguous)
Systematic name: L-ornithine,NAD(P)H:oxygen oxidoreductase (N5-hydroxylating)
Comments: A flavoprotein (FAD). The enzyme from the pathogenic fungus Aspergillus fumigatus catalyses a step in the biosynthesis of the siderophores triacetylfusarinine and desferriferricrocin, while the enzyme from the bacterium Kutzneria sp. 744 is involved in the biosynthesis of piperazate, a building block of the kutzneride family of antifungal antibiotics. Activity of the fungal enzyme is higher with NADPH, due to the fact that following the reduction of the flavin, NADP+ (but not NAD+) stabilizes the C4a-hydroperoxyflavin intermediate that oxidizes the substrate [3]. cf. EC 1.14.13.195, L-ornithine N5-monooxygenase (NADPH).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Chocklett, S.W. and Sobrado, P. Aspergillus fumigatus SidA is a highly specific ornithine hydroxylase with bound flavin cofactor. Biochemistry 49 (2010) 6777–6783. [DOI] [PMID: 20614882]
2.  Franceschini, S., Fedkenheuer, M., Vogelaar, N.J., Robinson, H.H., Sobrado, P. and Mattevi, A. Structural insight into the mechanism of oxygen activation and substrate selectivity of flavin-dependent N-hydroxylating monooxygenases. Biochemistry 51 (2012) 7043–7045. [DOI] [PMID: 22928747]
3.  Romero, E., Fedkenheuer, M., Chocklett, S.W., Qi, J., Oppenheimer, M. and Sobrado, P. Dual role of NADP(H) in the reaction of a flavin dependent N-hydroxylating monooxygenase. Biochim. Biophys. Acta 1824 (2012) 850–857. [DOI] [PMID: 22465572]
4.  Neumann, C.S., Jiang, W., Heemstra, J.R., Jr., Gontang, E.A., Kolter, R. and Walsh, C.T. Biosynthesis of piperazic acid via N5-hydroxy-ornithine in Kutzneria spp. 744. ChemBioChem 13 (2012) 972–976. [DOI] [PMID: 22522643]
[EC 1.14.13.196 created 2014]
 
 
EC 1.14.99.42      
Transferred entry: zeaxanthin 7,8-dioxygenase. Now EC 1.13.11.84, crocetin dialdehyde synthase
[EC 1.14.99.42 created 2011, modified 2014, deleted 2017]
 
 
EC 2.1.1.101     
Accepted name: macrocin O-methyltransferase
Reaction: S-adenosyl-L-methionine + macrocin = S-adenosyl-L-homocysteine + tylosin
For diagram of tylosin biosynthesis, click here
Other name(s): macrocin methyltransferase; S-adenosyl-L-methionine-macrocin O-methyltransferase; MOMT (ambiguous); tylF (gene name)
Systematic name: S-adenosyl-L-methionine:macrocin 3′′′-O-methyltransferase
Comments: Requires Mg2+, Mn2+ or Co2+. The 3-hydroxy group of the 2-O-methyl-6-deoxy-D-allose moiety in the macrolide antibiotic macrosin acts as methyl acceptor, generating tylosin, another macrolide antibiotic. Isolated from the bacterium Streptomyces fradiae. Not identical with EC 2.1.1.102, demethylmacrocin O-methyltransferase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 79468-52-3
References:
1.  Bauer, N.J., Kreuzman, A.J., Dotzlaf, J.E. and Yeh, W.-K. Purification, characterization, and kinetic mechanism of S-adenosyl-L-methionine:macrocin O-methyltransferase from Streptomyces fradiae. J. Biol. Chem. 263 (1988) 15619–15625. [PMID: 3170601]
2.  Kreuzman, A.J., Turner, J.R. and Yeh, W.-K. Two distinctive O-methyltransferases catalyzing penultimate and terminal reactions of macrolide antibiotic (tylosin) biosynthesis. Substrate specificity, enzyme inhibition, and kinetic mechanism. J. Biol. Chem. 263 (1988) 15626–15633. [PMID: 3170602]
[EC 2.1.1.101 created 1992]
 
 
EC 2.1.1.102     
Accepted name: demethylmacrocin O-methyltransferase
Reaction: S-adenosyl-L-methionine + demethylmacrocin = S-adenosyl-L-homocysteine + macrocin
For diagram of tylosin biosynthesis, click here
Other name(s): demethylmacrocin methyltransferase; DMOMT
Systematic name: S-adenosyl-L-methionine:demethylmacrocin 2′′′-O-methyltransferase
Comments: Requires Mg2+. The enzyme, isolated from the bacterium Streptomyces fradiae, is involved in the biosynthesis of the macrolide antibiotic tylosin. The 2-hydroxy group of a 6-deoxy-D-allose moiety in demethylmacrocin acts as the methyl acceptor. Also acts on demethyllactenocin, giving lactenocin. Not identical with EC 2.1.1.101 macrocin O-methyltransferase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 120313-64-6
References:
1.  Kreuzman, A.J., Turner, J.R. and Yeh, W.-K. Two distinctive O-methyltransferases catalyzing penultimate and terminal reactions of macrolide antibiotic (tylosin) biosynthesis. Substrate specificity, enzyme inhibition, and kinetic mechanism. J. Biol. Chem. 263 (1988) 15626–15633. [PMID: 3170602]
[EC 2.1.1.102 created 1992]
 
 
EC 2.4.1.271     
Accepted name: crocetin glucosyltransferase
Reaction: (1) UDP-α-D-glucose + crocetin = UDP + β-D-glucosyl crocetin
(2) UDP-α-D-glucose + β-D-glucosyl crocetin = UDP + bis(β-D-glucosyl) crocetin
(3) UDP-α-D-glucose + β-D-gentiobiosyl crocetin = UDP + β-D-gentiobiosyl β-D-glucosyl crocetin
For diagram of crocin biosynthesis, click here
Other name(s): crocetin GTase; UGTCs2; UGT75L6; UDP-glucose:crocetin glucosyltransferase; UDP-glucose:crocetin 8-O-D-glucosyltransferase
Systematic name: UDP-α-D-glucose:crocetin 8-O-D-glucosyltransferase
Comments: In the plants Crocus sativus and Gardenia jasminoides this enzyme esterifies a free carboxyl group of crocetin and some crocetin glycosyl esters. The enzyme from Gardenia can also form glucosyl esters with 4-coumarate, caffeate and ferulate [3].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Côté, F., Cormier, F., Dufresne, C. and Willemot, C. Properties of a glucosyltransferase involved in crocin synthesis. Plant Sci. 153 (2000) 55–63.
2.  Moraga, A.R., Nohales, P.F., Perez, J.A. and Gomez-Gomez, L. Glucosylation of the saffron apocarotenoid crocetin by a glucosyltransferase isolated from Crocus sativus stigmas. Planta 219 (2004) 955–966. [DOI] [PMID: 15605174]
3.  Nagatoshi, M., Terasaka, K., Owaki, M., Sota, M., Inukai, T., Nagatsu, A. and Mizukami, H. UGT75L6 and UGT94E5 mediate sequential glucosylation of crocetin to crocin in Gardenia jasminoides. FEBS Lett. 586 (2012) 1055–1061. [DOI] [PMID: 22569263]
[EC 2.4.1.271 created 2011]
 
 
EC 2.4.1.318     
Accepted name: demethyllactenocin mycarosyltransferase
Reaction: dTDP-β-L-mycarose + demethyllactenocin = dTDP + demethylmacrocin
For diagram of tylosin biosynthesis, click here
Glossary: dTDP-β-L-mycarose = dTDP-2,6-dideoxy-3-C-methyl-β-L-ribo-hexose
demethyllactenocin = [(2R,3R,4E,6E,9R,11R,12S,13S,14R)-12-{[3,6-dideoxy-3-(dimethylamino)-D-glucopyranosyl]oxy}-2-ethyl-14-hydroxy-5,9,13-trimethyl-8,16-dioxo-11-(2-oxoethyl)oxacyclohexadeca-4,6-dien-3-yl]methyl 6-deoxy-D-allopyranoside
Other name(s): tylCV (gene name); tylC5 (gene name)
Systematic name: dTDP-β-L-mycarose:demethyllactenocin 4′-O-α-L-mycarosyltransferase
Comments: The enzyme participates in the biosynthetic pathway of the macrolide antibiotic tylosin, which is produced by several species of Streptomyces bacteria.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Bate, N., Butler, A.R., Smith, I.P. and Cundliffe, E. The mycarose-biosynthetic genes of Streptomyces fradiae, producer of tylosin. Microbiology 146 (2000) 139–146. [DOI] [PMID: 10658660]
[EC 2.4.1.318 created 2014]
 
 
EC 2.4.1.330     
Accepted name: β-D-glucosyl crocetin β-1,6-glucosyltransferase
Reaction: (1) UDP-α-D-glucose + β-D-glucosyl crocetin = UDP + β-D-gentiobiosyl crocetin
(2) UDP-α-D-glucose + bis(β-D-glucosyl) crocetin = UDP + β-D-gentiobiosyl β-D-glucosyl crocetin
(3) UDP-α-D-glucose + β-D-gentiobiosyl β-D-glucosyl crocetin = UDP + crocin
For diagram of crocin biosynthesis, click here
Glossary: crocin = bis(β-D-gentiobiosyl) crocetin
crocetin = (2E,4E,6E,8E,10E,12E,14E)-2,6,11,15-tetramethylhexadeca-2,4,6,8,10,12,14-heptaenedioate
Other name(s): UGT94E5; UDP-glucose:crocetin glucosyl ester glucosyltransferasee
Systematic name: UDP-α-D-glucose:β-D-glucosyl crocetin β-1,6-glucosyltransferase
Comments: The enzyme, characterized from the plant Gardenia jasminoides, adds a glucose to several crocetin glycosyl esters, but not to crocetin (cf. EC 2.4.1.271, crocetin glucosyltransferase).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Nagatoshi, M., Terasaka, K., Owaki, M., Sota, M., Inukai, T., Nagatsu, A. and Mizukami, H. UGT75L6 and UGT94E5 mediate sequential glucosylation of crocetin to crocin in Gardenia jasminoides. FEBS Lett. 586 (2012) 1055–1061. [DOI] [PMID: 22569263]
[EC 2.4.1.330 created 2014]
 
 


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