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Information on EC 1.14.14.117 - aflatoxin B synthase and Organism(s) Aspergillus parasiticus and UniProt Accession O13345

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IUBMB Comments
A cytochrome P-450 (heme-thiolate) protein. Isolated from the mold Aspergillus parasiticus.
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This record set is specific for:
Aspergillus parasiticus
UNIPROT: O13345
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The taxonomic range for the selected organisms is: Aspergillus parasiticus
The expected taxonomic range for this enzyme is: Aspergillus
Synonyms
aflQ, EC 1.14.13.175, ordA, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SYSTEMATIC NAME
IUBMB Comments
8-O-methylsterigmatocystin,[reduced NADPH-hemoprotein reductase]:oxygen oxidoreductase (aflatoxin-B forming)
A cytochrome P-450 (heme-thiolate) protein. Isolated from the mold Aspergillus parasiticus.
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
-
-
-
?
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 SUBSTRATE
NATURAL 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
-
-
-
?
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
-
in 50 mM phosphate buffer, pH 7.5, at 29°C
0.0012
8-O-methylsterigmatocystin
-
in 50 mM phosphate buffer, pH 7.5, at 29°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.23
-
enzyme from supernatant, using 8-O-methylsterigmatocystin as substrate, at pH 7.5 and 29°C
34.11
-
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
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
the enzyme is involved in the biosynthesis of aflatoxins B1, G1, B2, and G2
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
60000
-
x * 60000, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
-
x * 60000, SDS-PAGE
PROTEIN VARIANTS
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
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
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Yu, J.; Chang, P.K.; Ehrlich, K.C.; Cary, J.W.; Montalbano, B.; Dyer, J.M.; Bhatnagar, D.; Cleveland, T.E.
Characterization of the critical amino acids of an Aspergillus parasiticus cytochrome P-450 monooxygenase encoded by ordA that is involved in the biosynthesis of aflatoxins B1, G1, B2, and G2
Appl. Environ. Microbiol.
64
4834-4841
1998
Aspergillus parasiticus (O13345), Aspergillus parasiticus SRRC 143 (O13345)
Manually annotated by BRENDA team
Bhatnagar, D.
Enzymological evidence for separate pathways for aflatoxin B1 and B2 biosynthesis
Biochemistry
30
4343-4350
1991
Aspergillus flavus, Aspergillus flavus SRRC 141, Aspergillus parasiticus, Aspergillus parasiticus SRRC 163
Manually annotated by BRENDA team
Udwary, D.W.; Casillas, L.K.; Townsend, C.A.
Synthesis of 11-hydroxyl O-methylsterigmatocystin and the role of a cytochrome P-450 in the final step of aflatoxin biosynthesis
J. Am. Chem. Soc.
124
5294-5303
2002
Aspergillus parasiticus, Aspergillus parasiticus SU-1
Manually annotated by BRENDA team
Jamali, M.; Karimipour, M.; Shams-Ghahfarokhi, M.; Amani, A.; Razzaghi-Abyaneh, M.
Expression of aflatoxin genes aflO (omtB) and aflQ (ordA) differentiates levels of aflatoxin production by Aspergillus flavus strains from soils of pistachio orchards
Res. Microbiol.
164
293-299
2013
Aspergillus flavus, Aspergillus flavus PFCC 101, Aspergillus flavus PFCC 116, Aspergillus flavus PFCC 137, Aspergillus flavus PFCC 176, Aspergillus flavus PFCC 209, Aspergillus flavus PFCC 247, Aspergillus flavus PFCC 267, Aspergillus flavus PFCC 309, Aspergillus parasiticus, Aspergillus parasiticus NRRL 2999, Aspergillus parasiticus PFCC 14
Manually annotated by BRENDA team