1-deoxypentalenic acid 11beta-hydroxylase | |||||||||
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Identifiers | |||||||||
EC no. | 1.14.11.35 | ||||||||
Databases | |||||||||
IntEnz | IntEnz view | ||||||||
BRENDA | BRENDA entry | ||||||||
ExPASy | NiceZyme view | ||||||||
KEGG | KEGG entry | ||||||||
MetaCyc | metabolic pathway | ||||||||
PRIAM | profile | ||||||||
PDB structures | RCSB PDB PDBe PDBsum | ||||||||
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1-deoxypentalenic acid 11beta-hydroxylase (EC 1.14.11.35, PTLH (gene), SAV2991 (gene), PNTH (gene)) is an enzyme with systematic name 1-deoxypentalenic acid,2-oxoglutarate:oxygen oxidoreductase. This enzyme catalyses the following chemical reaction
- 1-deoxypentalenate + 2-oxoglutarate + O2 1-deoxy-11beta-hydroxypentalenate + succinate + CO2
1-Deoxypentalenic acid 11beta-hydroxylase contains Fe(II) and ascorbate.
References
- You Z, Omura S, Ikeda H, Cane DE (May 2006). "Pentalenolactone biosynthesis. Molecular cloning and assignment of biochemical function to PtlH, a non-heme iron dioxygenase of Streptomyces avermitilis". Journal of the American Chemical Society. 128 (20): 6566–7. doi:10.1021/ja061469i. PMC 2533727. PMID 16704250.
- You Z, Omura S, Ikeda H, Cane DE, Jogl G (December 2007). "Crystal structure of the non-heme iron dioxygenase PtlH in pentalenolactone biosynthesis". The Journal of Biological Chemistry. 282 (50): 36552–60. doi:10.1074/jbc.M706358200. PMC 3010413. PMID 17942405.
External links
- 1-deoxypentalenic+acid+11beta-hydroxylase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
Oxidoreductases: dioxygenases, including steroid hydroxylases (EC 1.14) | |
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1.14.11: 2-oxoglutarate | |
1.14.13: NADH or NADPH | |
1.14.14: reduced flavin or flavoprotein | |
1.14.15: reduced iron–sulfur protein | |
1.14.16: reduced pteridine (BH4 dependent) | |
1.14.17: reduced ascorbate | |
1.14.18-19: other | |
1.14.99 - miscellaneous |
Enzymes | |
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