Information on EC 1.14.13.175 - aflatoxin B synthase

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The expected taxonomic range for this enzyme is: Aspergillus

EC NUMBER
COMMENTARY hide
1.14.13.175
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RECOMMENDED NAME
GeneOntology No.
aflatoxin B synthase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
8-O-methyldihydrosterigmatocystin + 2 NADPH + 2 H+ + 2 O2 = aflatoxin B2 + 2 NADP+ + H2O + methanol + CO2
show the reaction diagram
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8-O-methylsterigmatocystin + 2 NADPH + 2 H+ + 2 O2 = aflatoxin B1 + 2 NADP+ + H2O + methanol + CO2
show the reaction diagram
(1)
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Aflatoxin biosynthesis
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aflatoxins B1 and G1 biosynthesis
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aflatoxins B2 and G2 biosynthesis
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SYSTEMATIC NAME
IUBMB Comments
8-O-methylsterigmatocystin,NADPH:O2 oxidoreductase (aflatoxin-B forming)
A heme-thiolate (P-450) enzyme. Isolated from the mold Aspergillus parasiticus.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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UniProt
Manually annotated by BRENDA team
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Manually annotated by BRENDA team
ATCC 56775
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
8-O-methyldihydrosterigmatocystin + 2 NADPH + 2 H+ + 2 O2
aflatoxin B2 + 2 NADP+ + H2O + methanol + CO2
show the reaction diagram
8-O-methylsterigmatocystin + 2 NADPH + 2 H+ + 2 O2
aflatoxin B1 + 2 NADP+ + H2O + methanol + CO2
show the reaction diagram
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
8-O-methyldihydrosterigmatocystin + 2 NADPH + 2 H+ + 2 O2
aflatoxin B2 + 2 NADP+ + H2O + methanol + CO2
show the reaction diagram
8-O-methylsterigmatocystin + 2 NADPH + 2 H+ + 2 O2
aflatoxin B1 + 2 NADP+ + H2O + methanol + CO2
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0134
8-O-methyldihydrosterigmatocystin
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in 50 mM phosphate buffer, pH 7.5, at 29C
0.0012
8-O-methylsterigmatocystin
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in 50 mM phosphate buffer, pH 7.5, at 29C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.23
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enzyme from supernatant, using 8-O-methylsterigmatocystin as substrate, at pH 7.5 and 29C
34.11
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after 148.3fold purification, using 8-O-methylsterigmatocystin as substrate, at pH 7.5 and 29C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25 - 30
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate precipitation, QMA anion exchange column chromatography, and Bio-Gel P-200 gel filtration
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Saccharomyces cerevisiae strain InvSc1
expressed in Saccharomyces cerevisiae strain INVSc2
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A143S
the mutation affects enzymatic activity (approximately 50% of the enzyme activity which converts O-methylsterigmatocystin to aflatoxin B1 is lost)
H400L
the mutation results in a loss of the monooxygenase activity
I528Y
the mutation does not affect enzymatic activity
A143S
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the mutation affects enzymatic activity (approximately 50% of the enzyme activity which converts O-methylsterigmatocystin to aflatoxin B1 is lost)
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H400L
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the mutation results in a loss of the monooxygenase activity
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I528Y
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the mutation does not affect enzymatic activity
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