EC |
1.3.1.126 |
Accepted name: |
2-epi-5-epi-valiolone dehydrogenase |
Reaction: |
2-epi-5-epi-valiolone + NAD+ = demethylgadusol + NADH + H+ |
Glossary: |
2-epi-5-epi-valiolone = (2S,3S,4S,5R)-2,3,4,5-tetrahydroxy-5-(hydroxymethyl)cyclohexan-1-one
demethylgadusol = (4R,5R)-2,3,4,5-tetrahydroxy-5-(hydroxymethyl)cyclohex-2-en-1-one |
Other name(s): |
gadusol synthase |
Systematic name: |
2-epi-5-epi-valiolone:NAD+ 2,3-oxidoreductase |
Comments: |
The enzyme, present in egg-laying vertebrates, is involved in biosynthesis of the UV absorbing compound gadusol. It is a bifunctional enzyme that also catalyses EC 2.1.1.391, demethylgadusol O-methyltransferase. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Osborn, A.R., Almabruk, K.H., Holzwarth, G., Asamizu, S., LaDu, J., Kean, K.M., Karplus, P.A., Tanguay, R.L., Bakalinsky, A.T. and Mahmud, T. De novo synthesis of a sunscreen compound in vertebrates. Elife 4 (2015) . [DOI] [PMID: 25965179] |
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[EC 1.3.1.126 created 2023] |
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EC |
2.1.1.391 |
Accepted name: |
demethylgadusol O-methyltransferase |
Reaction: |
S-adenosyl-L-methionine + demethylgadusol = S-adenosyl-L-homocysteine + gadusol |
Glossary: |
demethylgadusol = (4R,5R)-2,3,4,5-tetrahydroxy-5-(hydroxymethyl)cyclohex-2-en-1-one
gadusol = (4R,5R)-3,4,5-trihydroxy-5-(hydroxymethyl)-2-methoxycyclohex-2-en-1-one |
Other name(s): |
gadusol synthase; desmethyl gadusol O-methyltransferase |
Systematic name: |
S-adenosyl-L-methionine:demethylgadusol 2-O-methyltransferase |
Comments: |
The enzyme, present in egg-laying vertebrates, is involved in biosynthesis of the UV absorbing compound gadusol. It is a bifunctional enzyme that also catalyses EC 1.3.1.126, 2-epi-5-epi-valiolone dehydrogenase. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Osborn, A.R., Almabruk, K.H., Holzwarth, G., Asamizu, S., LaDu, J., Kean, K.M., Karplus, P.A., Tanguay, R.L., Bakalinsky, A.T. and Mahmud, T. De novo synthesis of a sunscreen compound in vertebrates. Elife 4 (2015) . [DOI] [PMID: 25965179] |
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[EC 2.1.1.391 created 2023] |
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EC |
2.7.1.188 |
Accepted name: |
2-epi-5-epi-valiolone 7-kinase |
Reaction: |
ATP + 2-epi-5-epi-valiolone = ADP + 2-epi-5-epi-valiolone 7-phosphate |
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For diagram of valiolone biosynthesis, click here |
Glossary: |
2-epi-5-epi-valiolone = (2S,3S,4S,5R)-2,3,4,5-tetrahydroxy-5-(hydroxymethyl)cyclohexan-1-one |
Other name(s): |
AcbM |
Systematic name: |
ATP:2-epi-5-epi-valiolone 7-phosphotransferase |
Comments: |
The enzyme, characterized from the bacterium Actinoplanes sp. SE50/110, is involved in the biosynthesis of the oligosaccharide acarbose. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Zhang, C.S., Stratmann, A., Block, O., Bruckner, R., Podeschwa, M., Altenbach, H.J., Wehmeier, U.F. and Piepersberg, W. Biosynthesis of the C7-cyclitol moiety of acarbose in Actinoplanes species SE50/110. 7-O-phosphorylation of the initial cyclitol precursor leads to proposal of a new biosynthetic pathway. J. Biol. Chem. 277 (2002) 22853–22862. [DOI] [PMID: 11937512] |
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[EC 2.7.1.188 created 2015] |
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EC |
4.2.3.152 |
Accepted name: |
2-epi-5-epi-valiolone synthase |
Reaction: |
α-D-sedoheptulopyranose 7-phosphate = 2-epi-5-epi-valiolone + phosphate |
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For diagram of valiolone biosynthesis, click here |
Glossary: |
2-epi-5-epi-valiolone = (2S,3S,4S,5R)-2,3,4,5-tetrahydroxy-5-(hydroxymethyl)cyclohexan-1-one |
Other name(s): |
AcbC; ValA; CetA; SalQ; C7-cyclitol synthase |
Systematic name: |
α-D-sedoheptulopyranose-7-phosphate phosphate-lyase (cyclizing; 2-epi-5-epi-valiolone-forming) |
Comments: |
The enzyme is highly specific for α-D-sedoheptulopyranose 7-phosphate. It requires a divalent metal ion (Zn2+ or Co2+) and an NAD+ cofactor, which is transiently reduced during the reaction. The enzyme is involved in the biosynthesis of C7N-aminocyclitol natural products, such as the valienamine moiety of the antidiabetic drug acarbose and the crop protectant validamycin A. cf. EC 4.2.3.155, 2-epi-valiolone synthase and EC 4.2.3.154, demethyl-4-deoxygadusol synthase. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
References: |
1. |
Stratmann, A., Mahmud, T., Lee, S., Distler, J., Floss, H.G. and Piepersberg, W. The AcbC protein from Actinoplanes species is a C7-cyclitol synthase related to 3-dehydroquinate synthases and is involved in the biosynthesis of the α-glucosidase inhibitor acarbose. J. Biol. Chem. 274 (1999) 10889–10896. [DOI] [PMID: 10196166] |
2. |
Yu, Y., Bai, L., Minagawa, K., Jian, X., Li, L., Li, J., Chen, S., Cao, E., Mahmud, T., Floss, H.G., Zhou, X. and Deng, Z. Gene cluster responsible for validamycin biosynthesis in Streptomyces hygroscopicus subsp. jinggangensis 5008. Appl. Environ. Microbiol. 71 (2005) 5066–5076. [DOI] [PMID: 16151088] |
3. |
Wu, X., Flatt, P.M., Schlorke, O., Zeeck, A., Dairi, T. and Mahmud, T. A comparative analysis of the sugar phosphate cyclase superfamily involved in primary and secondary metabolism. ChemBioChem 8 (2007) 239–248. [DOI] [PMID: 17195255] |
4. |
Choi, W.S., Wu, X., Choeng, Y.H., Mahmud, T., Jeong, B.C., Lee, S.H., Chang, Y.K., Kim, C.J. and Hong, S.K. Genetic organization of the putative salbostatin biosynthetic gene cluster including the 2-epi-5-epi-valiolone synthase gene in Streptomyces albus ATCC 21838. Appl. Microbiol. Biotechnol. 80 (2008) 637–645. [DOI] [PMID: 18648803] |
5. |
Kean, K.M., Codding, S.J., Asamizu, S., Mahmud, T. and Karplus, P.A. Structure of a sedoheptulose 7-phosphate cyclase: ValA from Streptomyces hygroscopicus. Biochemistry 53 (2014) 4250–4260. [DOI] [PMID: 24832673] |
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[EC 4.2.3.152 created 2015, modified 2016] |
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EC |
4.2.3.154 |
Accepted name: |
demethyl-4-deoxygadusol synthase |
Reaction: |
D-sedoheptulose 7-phosphate = demethyl-4-deoxygadusol + phosphate + H2O |
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For diagram of valiolone biosynthesis, click here |
Glossary: |
demethyl-4-deoxygadusol = 2,3,5-trihydroxy-5-(hydroxymethyl)cyclohex-2-en-1-one |
Other name(s): |
Nos2 (gene name); Anb2 (gene name) |
Systematic name: |
D-sedoheptulose-7-phosphate phosphate-lyase (cyclizing; demethyl-4-deoxygadusol-forming) |
Comments: |
The enzyme, characterized from the cyanobacterium Nostoc punctiforme PCC 73102, is involved in the biosynthesis of the sunscreen compound shinorine. It requires a divalent metal ion (Zn2+ or Co2+) and an NAD+ cofactor, which is transiently reduced during the reaction. cf. EC 4.2.3.152, 2-epi-5-epi-valiolone synthase and EC 4.2.3.155, 2-epi-valiolone synthase. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
References: |
1. |
Balskus, E.P. and Walsh, C.T. The genetic and molecular basis for sunscreen biosynthesis in cyanobacteria. Science 329 (2010) 1653–1656. [DOI] [PMID: 20813918] |
2. |
Asamizu, S., Xie, P., Brumsted, C.J., Flatt, P.M. and Mahmud, T. Evolutionary divergence of sedoheptulose 7-phosphate cyclases leads to several distinct cyclic products. J. Am. Chem. Soc. 134 (2012) 12219–12229. [DOI] [PMID: 22741921] |
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[EC 4.2.3.154 created 2016] |
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EC |
4.2.3.155 |
Accepted name: |
2-epi-valiolone synthase |
Reaction: |
D-sedoheptulose 7-phosphate = 2-epi-valiolone + phosphate |
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For diagram of valiolone biosynthesis, click here |
Glossary: |
2-epi-valiolone = (2S,3S,4S,5S)-2,3,4,5-tetrahydroxy-5-(hydroxymethyl)cyclohexan-1-one |
Systematic name: |
D-sedoheptulose-7-phosphate phosphate-lyase (cyclizing; 2-epi-valiolone-forming) |
Comments: |
The enzyme, characterized from the bacteria Actinosynnema mirum and Stigmatella aurantiaca DW4/3-1, produces 2-epi-valiolone, which is believed to function as a precursor in aminocyclitol biosynthesis. It requires a divalent metal ion (Zn2+ or Co2+) and an NAD+ cofactor, which is transiently reduced during the reaction. cf. EC 4.2.3.152, 2-epi-5-epi-valiolone synthase and EC 4.2.3.154, demethyl-4-deoxygadusol synthase. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Asamizu, S., Xie, P., Brumsted, C.J., Flatt, P.M. and Mahmud, T. Evolutionary divergence of sedoheptulose 7-phosphate cyclases leads to several distinct cyclic products. J. Am. Chem. Soc. 134 (2012) 12219–12229. [DOI] [PMID: 22741921] |
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[EC 4.2.3.155 created 2016] |
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EC |
5.1.3.33 |
Accepted name: |
2-epi-5-epi-valiolone epimerase |
Reaction: |
2-epi-5-epi-valiolone = 5-epi-valiolone |
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For diagram of valiolone biosynthesis, click here |
Glossary: |
2-epi-5-epi-valiolone= (2S,3S,4S,5R)-2,3,4,5-tetrahydroxy-5-(hydroxymethyl)cyclohexanone
5-epi-valiolone = (2R,3S,4S,5R)-2,3,4,5-tetrahydroxy-5-(hydroxymethyl)cyclohexanone |
Other name(s): |
CetB; EVE |
Systematic name: |
2-epi-5-epi-valiolone 2-epimerase |
Comments: |
The enzyme, characterized from the bacterium Actinomyces sp. Lu 9419, is involved in the biosynthesis of the antitumor agent cetoniacytone A. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Wu, X., Flatt, P.M., Xu, H. and Mahmud, T. Biosynthetic gene cluster of cetoniacytone A, an unusual aminocyclitol from the endosymbiotic Bacterium Actinomyces sp. Lu 9419. ChemBioChem 10 (2009) 304–314. [DOI] [PMID: 19101977] |
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[EC 5.1.3.33 created 2015] |
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EC |
5.1.3.35 |
Accepted name: |
2-epi-5-epi-valiolone 7-phosphate 2-epimerase |
Reaction: |
2-epi-5-epi-valiolone 7-phosphate = 5-epi-valiolone 7-phosphate |
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For diagram of valiolone biosynthesis, click here |
Glossary: |
2-epi-5-epi-valiolone 7-phosphate = (2S,3S,4S,5R)-2,3,4,5-tetrahydroxy-5-(phosphonooxymethyl)cyclohexanone
5-epi-valiolone 7-phosphate = (2R,3S,4S,5R)-2,3,4,5-tetrahydroxy-5-(phosphonooxymethyl)cyclohexanone
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Other name(s): |
AcbO |
Systematic name: |
2-epi-5-epi-valiolone-7-phosphate 2-epimerase |
Comments: |
The enzyme, isolated from the bacterium Actinoplanes sp. SE 50/110, is involved in the biosynthesis of the α-glucosidase inhibitor acarbose. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Zhang, C.S., Podeschwa, M., Altenbach, H.J., Piepersberg, W. and Wehmeier, U.F. The acarbose-biosynthetic enzyme AcbO from Actinoplanes sp. SE 50/110 is a 2-epi-5-epi-valiolone-7-phosphate 2-epimerase. FEBS Lett. 540 (2003) 47–52. [DOI] [PMID: 12681481] |
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[EC 5.1.3.35 created 2015] |
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