A heme-thiolate enzyme (P-450). Isolated from the bacterium Streptomyces avermitilis. The product, pentalenate, is a co-metabolite from pentalenolactone biosynthesis.
A heme-thiolate enzyme (P-450). Isolated from the bacterium Streptomyces avermitilis. The product, pentalenate, is a co-metabolite from pentalenolactone biosynthesis.
enzyme additionally catalyzes the hydroxylation of daidzein to 7,3',4'-trihydroxyisoflavone with apparent Km and kcat values for daidzein of 21.83 mM and 15.01 per min in the presence of putidaredoxin and putidaredoxin reductase, respectively
enzyme additionally catalyzes the hydroxylation of daidzein to 7,3',4'-trihydroxyisoflavone with apparent Km and kcat values for daidzein of 21.83 mM and 15.01 per min in the presence of putidaredoxin and putidaredoxin reductase, respectively
no substrates: pentalenene, 1-deoxy-11beta-hydroxypentalenic acid, 1-deoxy-11-oxopentalenic acid, or the corresponding methyl esters of 1-deoxy-11beta-hydroxypentalenic acid, 1-deoxy-11-oxopentalenic acid and 1-deoxypentalenic acid, respectively
no substrates: pentalenene, 1-deoxy-11beta-hydroxypentalenic acid, 1-deoxy-11-oxopentalenic acid, or the corresponding methyl esters of 1-deoxy-11beta-hydroxypentalenic acid, 1-deoxy-11-oxopentalenic acid and 1-deoxypentalenic acid, respectively
enzyme additionally catalyzes the hydroxylation of daidzein to 7,3',4'-trihydroxyisoflavone with apparent Km and kcat values for daidzein of 21.83 mM and 15.01 per min in the presence of putidaredoxin and putidaredoxin reductase, respectively
CYP105D7 binds diclofenac in a slightly cooperative manner with an affinity of 65 microM and a Hill coefficient of 1.16, pH not specified in the publication, temperature not specified in the publication
CYP105D7 binds diclofenac in a slightly cooperative manner with an affinity of 65 microM and a Hill coefficient of 1.16, pH not specified in the publication, temperature not specified in the publication
disruption of the sav7469 gene encoding pentalenic acid synthase abolishes production of pentalenic acid. The deletion mutant accumulates 1-deoxypentalenic acid. Recombinant enzyme prepared from Escherichia coli catalyzes the oxidative conversion of 1-deoxypentalenic acid to pentalenic acid in the presence of the electron-transport partners, ferredoxin and ferredoxin reductase, both in vivo and in vitro
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
in complex with diclofenac, at 2.2 A resolution. The distal pocket of CYP105D7 contains two diclofenac molecules. The C3' and C4' atoms of the dichlorophenyl ring of one diclofenac molecule are positioned near the heme iron
molecular docking of compactin, compactin is directly hydrogen bonded with residues Thr79, Arg81, Leu178, Thr391, and Ile392 and its C6 position is proximate to the heme group. Molecular docking of diclofenac
Takamatsu, S.; Xu, L.H.; Fushinobu, S.; Shoun, H.; Komatsu, M.; Cane, D.E.; Ikeda, H.
Pentalenic acid is a shunt metabolite in the biosynthesis of the pentalenolactone family of metabolites: hydroxylation of 1-deoxypentalenic acid mediated by CYP105D7 (SAV_7469) of Streptomyces avermitilis
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Enzyme Nomenclature
1.14.15.11 pentalenic acid synthase
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