Information on EC 1.14.13.170 - pentalenolactone D synthase

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The expected taxonomic range for this enzyme is: Streptomyces

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EC NUMBER
COMMENTARY hide
1.14.13.170
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RECOMMENDED NAME
GeneOntology No.
pentalenolactone D synthase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
1-deoxy-11-oxopentalenate + NADPH + H+ + O2 = pentalenolactone D + NADP+ + H2O
show the reaction diagram
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
pentalenolactone biosynthesis
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Biosynthesis of antibiotics
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SYSTEMATIC NAME
IUBMB Comments
1-deoxy-11-oxopentalenate,NADH:oxygen oxidoreductase (pentalenolactone-D forming)
A FAD-dependent oxygenase. Isolated from the bacteria Streptomyces exfoliatus and Streptomyces arenae. The ketone undergoes a biological Baeyer-Villiger reaction. Part of the pathway of pentalenolactone biosynthesis.
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
1-deoxy-11-oxopentalenic acid + NADPH + H+ + O2
pentalenolactone D + NADP+ + H2O
show the reaction diagram
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
66915
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x * 66915, His6-tagged enzyme, MALDI-TOF mass spectrometry
67480
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x * 67480, His6-tagged enzyme, MALDI-TOF mass spectrometry
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Ni-NTA column chromatography
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3) cells
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LINKS TO OTHER DATABASES (specific for EC-Number 1.14.13.170)
ExplorEnz
ExPASy
KEGG
MetaCyc
SABIO-RK
NCBI: PubMed, Protein, Nucleotide, Structure, Genome, OMIM
IUBMB Enzyme Nomenclature
PROSITE Database of protein families and domains
InterPro (database of protein families, domains and functional sites)