Information on EC 1.14.15.11 - pentalenic acid synthase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
1.14.15.11
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RECOMMENDED NAME
GeneOntology No.
pentalenic acid synthase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
1-deoxypentalenate + reduced ferredoxin + O2 = pentalenate + oxidized ferredoxin + H2O
show the reaction diagram
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
neopentalenoketolactone and pentalenate biosynthesis
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SYSTEMATIC NAME
IUBMB Comments
1-deoxypentalenate,reduced ferredoxin:O2 oxidoreductase
A heme-thiolate enzyme (P-450). Isolated from the bacterium Streptomyces avermitilis. The product, pentalenate, is a co-metabolite from pentalenolactone biosynthesis.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
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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
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
1-deoxypentalenic acid + reduced ferredoxin + O2
pentalenic acid + oxidized ferredoxin + H2O
show the reaction diagram
compactin + reduced ferredoxin + O2
pravastatin + oxidized ferredoxin + H2O
show the reaction diagram
compactin + reduced putidaredoxin + O2
pravastatin + oxidized putidaredoxin + H2O
show the reaction diagram
diclofenac + reduced ferredoxin + O2
4'-hydroxydiclofenac + oxidized ferredoxin + H2O
show the reaction diagram
diclofenac + reduced putidaredoxin + O2
4'-hydroxydiclofenac + oxidized putidaredoxin + H2O
show the reaction diagram
additional information
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.027
1-deoxypentalenic acid
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pH 8.0, 25C
0.039
Compactin
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pH 7.4, 30C
0.19
diclofenac
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pH 7.4, 30C
additional information
diclofenac
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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
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.018
Compactin
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pH 7.4, 30C
0.36
diclofenac
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pH 7.4, 30C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.48
Compactin
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pH 7.4, 30C
1.9
diclofenac
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pH 7.4, 30C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
PDB
SCOP
CATH
ORGANISM
UNIPROT
Streptomyces avermitilis (strain ATCC 31267 / DSM 46492 / JCM 5070 / NBRC 14893 / NCIMB 12804 / NRRL 8165 / MA-4680)
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
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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
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escheirchia coli
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expression in Escherichia coli
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