Biology:1-Deoxypentalenic acid 11beta-hydroxylase
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Short description: Class of enzymes
1-deoxypentalenic acid 11beta-hydroxylase | |||||||||
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Identifiers | |||||||||
EC number | 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.[1][2] This enzyme catalyses the following chemical reaction
- 1-deoxypentalenate + 2-oxoglutarate + O2 [math]\displaystyle{ \rightleftharpoons }[/math] 1-deoxy-11beta-hydroxypentalenate + succinate + CO2
1-Deoxypentalenic acid 11beta-hydroxylase contains Fe(II) and ascorbate.
References
- ↑ "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. May 2006. doi:10.1021/ja061469i. PMID 16704250.
- ↑ "Crystal structure of the non-heme iron dioxygenase PtlH in pentalenolactone biosynthesis". The Journal of Biological Chemistry 282 (50): 36552–60. December 2007. doi:10.1074/jbc.M706358200. PMID 17942405.
External links
- 1-deoxypentalenic+acid+11beta-hydroxylase at the US National Library of Medicine Medical Subject Headings (MeSH)
Original source: https://en.wikipedia.org/wiki/1-Deoxypentalenic acid 11beta-hydroxylase.
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