Information on EC 1.14.14.117 - aflatoxin B synthase

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The expected taxonomic range for this enzyme is: Aspergillus

EC NUMBER
COMMENTARY hide
1.14.14.117
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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 [reduced NADPH-hemoprotein reductase] + 2 O2 = aflatoxin B2 + 2 [oxidized NADPH-hemoprotein reductase] + H2O + methanol + CO2
show the reaction diagram
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8-O-methylsterigmatocystin + 2 [reduced NADPH-hemoprotein reductase] + 2 O2 = aflatoxin B1 + 2 [oxidized NADPH-hemoprotein reductase] + H2O + methanol + CO2
show the reaction diagram
(1)
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
aflatoxins B1 and G1 biosynthesis
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aflatoxins B2 and G2 biosynthesis
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Aflatoxin biosynthesis
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Biosynthesis of antibiotics
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SYSTEMATIC NAME
IUBMB Comments
8-O-methylsterigmatocystin,[reduced NADPH-hemoprotein reductase]:oxygen oxidoreductase (aflatoxin-B forming)
A heme-thiolate (P-450) enzyme. Isolated from the mold Aspergillus parasiticus.
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 + [reduced NADPH-hemoprotein reductase] + O2
aflatoxin B2 + methanol + CO2 + [oxidized NADPH-hemoprotein reductase] + H2O
show the reaction diagram
8-O-methylsterigmatocystin + [reduced NADPH-hemoprotein reductase] + O2
aflatoxin B1 + 2 NADP+ + methanol + [oxidized NADPH-hemoprotein reductase] + H2O + 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 + [reduced NADPH-hemoprotein reductase] + O2
aflatoxin B2 + methanol + CO2 + [oxidized NADPH-hemoprotein reductase] + H2O
show the reaction diagram
8-O-methylsterigmatocystin + [reduced NADPH-hemoprotein reductase] + O2
aflatoxin B1 + 2 NADP+ + methanol + [oxidized NADPH-hemoprotein reductase] + H2O + CO2
show the reaction diagram
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 29°C
0.0012
8-O-methylsterigmatocystin
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in 50 mM phosphate buffer, pH 7.5, at 29°C
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 29°C
34.11
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after 148.3fold purification, using 8-O-methylsterigmatocystin as substrate, at pH 7.5 and 29°C
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
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
60000
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x * 60000, SDS-PAGE
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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