Any feedback?
No. of entries
Information on EC 1.14.14.117 - aflatoxin B synthase
for references in articles please use BRENDA:EC1.14.14.117
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree 1 Oxidoreductases
1.14 Acting on paired donors, with incorporation or reduction of molecular oxygen
1.14.14 With reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen into the other donor
1.14.14.117 aflatoxin B synthase
IUBMB Comments
A cytochrome P-450 (heme-thiolate) protein. Isolated from the mold Aspergillus parasiticus.
The expected taxonomic range for this enzyme is: Aspergillus
Reaction Schemes
show+
2
+
2
=
+
2
+
+
+
+
2
+
2
=
+
2
+
+
+
Synonyms
aflQ, EC 1.14.13.175, ordA, more
topPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
aflQ
EC 1.14.13.175
-
-
formerly
-
ordA
ordA
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
8-O-methyldihydrosterigmatocystin + 2 [reduced NADPH-hemoprotein reductase] + 2 O2 = aflatoxin B2 + 2 [oxidized NADPH-hemoprotein reductase] + H2O + methanol + CO2
-
-
-
-
8-O-methylsterigmatocystin + 2 [reduced NADPH-hemoprotein reductase] + 2 O2 = aflatoxin B1 + 2 [oxidized NADPH-hemoprotein reductase] + H2O + methanol + CO2
(1)
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PATHWAY SOURCE
PATHWAYS
BRENDA
MetaCyc
aflatoxins B1 and G1 biosynthesis, aflatoxins B2 and G2 biosynthesis
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
8-O-methyldihydrosterigmatocystin + [reduced NADPH-hemoprotein reductase] + O2
aflatoxin B2 + methanol + CO2 + [oxidized NADPH-hemoprotein reductase] + H2O
8-O-methylsterigmatocystin + [reduced NADPH-hemoprotein reductase] + O2
aflatoxin B1 + 2 NADP+ + methanol + [oxidized NADPH-hemoprotein reductase] + H2O + CO2
8-O-methyldihydrosterigmatocystin + [reduced NADPH-hemoprotein reductase] + O2
aflatoxin B2 + methanol + CO2 + [oxidized NADPH-hemoprotein reductase] + H2O
-
Substrates: -
Products: -
Products: -
?
8-O-methyldihydrosterigmatocystin + [reduced NADPH-hemoprotein reductase] + O2
aflatoxin B2 + methanol + CO2 + [oxidized NADPH-hemoprotein reductase] + H2O
-
Substrates: -
Products: -
Products: -
?
8-O-methyldihydrosterigmatocystin + [reduced NADPH-hemoprotein reductase] + O2
aflatoxin B2 + methanol + CO2 + [oxidized NADPH-hemoprotein reductase] + H2O
-
Substrates: -
Products: -
Products: -
?
8-O-methyldihydrosterigmatocystin + [reduced NADPH-hemoprotein reductase] + O2
aflatoxin B2 + methanol + CO2 + [oxidized NADPH-hemoprotein reductase] + H2O
Substrates: -
Products: -
Products: -
?
8-O-methyldihydrosterigmatocystin + [reduced NADPH-hemoprotein reductase] + O2
aflatoxin B2 + methanol + CO2 + [oxidized NADPH-hemoprotein reductase] + H2O
Substrates: -
Products: -
Products: -
?
8-O-methyldihydrosterigmatocystin + [reduced NADPH-hemoprotein reductase] + O2
aflatoxin B2 + methanol + CO2 + [oxidized NADPH-hemoprotein reductase] + H2O
-
Substrates: -
Products: -
Products: -
?
8-O-methyldihydrosterigmatocystin + [reduced NADPH-hemoprotein reductase] + O2
aflatoxin B2 + methanol + CO2 + [oxidized NADPH-hemoprotein reductase] + H2O
-
Substrates: -
Products: -
Products: -
?
8-O-methylsterigmatocystin + [reduced NADPH-hemoprotein reductase] + O2
aflatoxin B1 + 2 NADP+ + methanol + [oxidized NADPH-hemoprotein reductase] + H2O + CO2
-
Substrates: preferred substrate
Products: -
Products: -
?
8-O-methylsterigmatocystin + [reduced NADPH-hemoprotein reductase] + O2
aflatoxin B1 + 2 NADP+ + methanol + [oxidized NADPH-hemoprotein reductase] + H2O + CO2
-
Substrates: preferred substrate
Products: -
Products: -
?
8-O-methylsterigmatocystin + [reduced NADPH-hemoprotein reductase] + O2
aflatoxin B1 + 2 NADP+ + methanol + [oxidized NADPH-hemoprotein reductase] + H2O + CO2
-
Substrates: -
Products: -
Products: -
?
8-O-methylsterigmatocystin + [reduced NADPH-hemoprotein reductase] + O2
aflatoxin B1 + 2 NADP+ + methanol + [oxidized NADPH-hemoprotein reductase] + H2O + CO2
Substrates: -
Products: -
Products: -
?
8-O-methylsterigmatocystin + [reduced NADPH-hemoprotein reductase] + O2
aflatoxin B1 + 2 NADP+ + methanol + [oxidized NADPH-hemoprotein reductase] + H2O + CO2
-
Substrates: preferred substrate
Products: -
Products: -
?
8-O-methylsterigmatocystin + [reduced NADPH-hemoprotein reductase] + O2
aflatoxin B1 + 2 NADP+ + methanol + [oxidized NADPH-hemoprotein reductase] + H2O + CO2
Substrates: -
Products: -
Products: -
?
8-O-methylsterigmatocystin + [reduced NADPH-hemoprotein reductase] + O2
aflatoxin B1 + 2 NADP+ + methanol + [oxidized NADPH-hemoprotein reductase] + H2O + CO2
-
Substrates: preferred substrate
Products: -
Products: -
?
8-O-methylsterigmatocystin + [reduced NADPH-hemoprotein reductase] + O2
aflatoxin B1 + 2 NADP+ + methanol + [oxidized NADPH-hemoprotein reductase] + H2O + CO2
-
Substrates: -
Products: -
Products: -
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
8-O-methyldihydrosterigmatocystin + [reduced NADPH-hemoprotein reductase] + O2
aflatoxin B2 + methanol + CO2 + [oxidized NADPH-hemoprotein reductase] + H2O
8-O-methylsterigmatocystin + [reduced NADPH-hemoprotein reductase] + O2
aflatoxin B1 + 2 NADP+ + methanol + [oxidized NADPH-hemoprotein reductase] + H2O + CO2
8-O-methyldihydrosterigmatocystin + [reduced NADPH-hemoprotein reductase] + O2
aflatoxin B2 + methanol + CO2 + [oxidized NADPH-hemoprotein reductase] + H2O
-
Substrates: -
Products: -
Products: -
?
8-O-methyldihydrosterigmatocystin + [reduced NADPH-hemoprotein reductase] + O2
aflatoxin B2 + methanol + CO2 + [oxidized NADPH-hemoprotein reductase] + H2O
-
Substrates: -
Products: -
Products: -
?
8-O-methyldihydrosterigmatocystin + [reduced NADPH-hemoprotein reductase] + O2
aflatoxin B2 + methanol + CO2 + [oxidized NADPH-hemoprotein reductase] + H2O
-
Substrates: -
Products: -
Products: -
?
8-O-methyldihydrosterigmatocystin + [reduced NADPH-hemoprotein reductase] + O2
aflatoxin B2 + methanol + CO2 + [oxidized NADPH-hemoprotein reductase] + H2O
Substrates: -
Products: -
Products: -
?
8-O-methyldihydrosterigmatocystin + [reduced NADPH-hemoprotein reductase] + O2
aflatoxin B2 + methanol + CO2 + [oxidized NADPH-hemoprotein reductase] + H2O
Substrates: -
Products: -
Products: -
?
8-O-methyldihydrosterigmatocystin + [reduced NADPH-hemoprotein reductase] + O2
aflatoxin B2 + methanol + CO2 + [oxidized NADPH-hemoprotein reductase] + H2O
-
Substrates: -
Products: -
Products: -
?
8-O-methyldihydrosterigmatocystin + [reduced NADPH-hemoprotein reductase] + O2
aflatoxin B2 + methanol + CO2 + [oxidized NADPH-hemoprotein reductase] + H2O
-
Substrates: -
Products: -
Products: -
?
8-O-methylsterigmatocystin + [reduced NADPH-hemoprotein reductase] + O2
aflatoxin B1 + 2 NADP+ + methanol + [oxidized NADPH-hemoprotein reductase] + H2O + CO2
-
Substrates: preferred substrate
Products: -
Products: -
?
8-O-methylsterigmatocystin + [reduced NADPH-hemoprotein reductase] + O2
aflatoxin B1 + 2 NADP+ + methanol + [oxidized NADPH-hemoprotein reductase] + H2O + CO2
-
Substrates: preferred substrate
Products: -
Products: -
?
8-O-methylsterigmatocystin + [reduced NADPH-hemoprotein reductase] + O2
aflatoxin B1 + 2 NADP+ + methanol + [oxidized NADPH-hemoprotein reductase] + H2O + CO2
-
Substrates: -
Products: -
Products: -
?
8-O-methylsterigmatocystin + [reduced NADPH-hemoprotein reductase] + O2
aflatoxin B1 + 2 NADP+ + methanol + [oxidized NADPH-hemoprotein reductase] + H2O + CO2
Substrates: -
Products: -
Products: -
?
8-O-methylsterigmatocystin + [reduced NADPH-hemoprotein reductase] + O2
aflatoxin B1 + 2 NADP+ + methanol + [oxidized NADPH-hemoprotein reductase] + H2O + CO2
-
Substrates: preferred substrate
Products: -
Products: -
?
8-O-methylsterigmatocystin + [reduced NADPH-hemoprotein reductase] + O2
aflatoxin B1 + 2 NADP+ + methanol + [oxidized NADPH-hemoprotein reductase] + H2O + CO2
Substrates: -
Products: -
Products: -
?
8-O-methylsterigmatocystin + [reduced NADPH-hemoprotein reductase] + O2
aflatoxin B1 + 2 NADP+ + methanol + [oxidized NADPH-hemoprotein reductase] + H2O + CO2
-
Substrates: preferred substrate
Products: -
Products: -
?
8-O-methylsterigmatocystin + [reduced NADPH-hemoprotein reductase] + O2
aflatoxin B1 + 2 NADP+ + methanol + [oxidized NADPH-hemoprotein reductase] + H2O + CO2
-
Substrates: -
Products: -
Products: -
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0134
8-O-methyldihydrosterigmatocystin
-
in 50 mM phosphate buffer, pH 7.5, at 29Ā°C
0.0012
8-O-methylsterigmatocystin
-
in 50 mM phosphate buffer, pH 7.5, at 29Ā°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.23
-
enzyme from supernatant, using 8-O-methylsterigmatocystin as substrate, at pH 7.5 and 29Ā°C
34.11
-
after 148.3fold purification, using 8-O-methylsterigmatocystin as substrate, at pH 7.5 and 29Ā°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25 - 30
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
metabolism
the enzyme is involved in the biosynthesis of aflatoxins B1, G1, B2, and G2
metabolism
-
the enzyme is involved in the biosynthesis of aflatoxins B1, G1, B2, and G2
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). AFLQ_ASPPU
Aspergillus parasiticus (strain ATCC 56775 / NRRL 5862 / SRRC 143 / SU-1)
528
1
60189
Swiss-Prot
Secretory Pathway (Reliability: 1)
ORDA_ASPFA
Aspergillus flavus (strain ATCC MYA-384 / AF70)
528
0
60223
Swiss-Prot
Secretory Pathway (Reliability: 1)
ORDA_ASPFL
528
0
60211
Swiss-Prot
Secretory Pathway (Reliability: 1)
ORDA_ASPFN
Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 / SRRC 167)
528
0
60211
Swiss-Prot
Secretory Pathway (Reliability: 1)
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
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
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
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate precipitation, QMA anion exchange column chromatography, and Bio-Gel P-200 gel filtration
ammonium sulfate precipitation, QMA anion exchange column chromatography, and Bio-Gel P-200 gel filtration
-
ammonium sulfate precipitation, QMA anion exchange column chromatography, and Bio-Gel P-200 gel filtration
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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)
brenda
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
brenda
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
brenda
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
brenda
EXTERNAL LINKS (specific for EC-Number 1.14.14.117)
html completed
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
About BRENDA
Social media
Help
Survey
Download
Contribution
Legal
Curated at
Member of
