BRENDA - Enzyme Database show
show all sequences of 1.14.14.117

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

Yu, J.; Chang, P.K.; Ehrlich, K.C.; Cary, J.W.; Montalbano, B.; Dyer, J.M.; Bhatnagar, D.; Cleveland, T.E.; Appl. Environ. Microbiol. 64, 4834-4841 (1998)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
expressed in Saccharomyces cerevisiae strain InvSc1
Aspergillus parasiticus
Engineering
Amino acid exchange
Commentary
Organism
A143S
the mutation affects enzymatic activity (approximately 50% of the enzyme activity which converts O-methylsterigmatocystin to aflatoxin B1 is lost)
Aspergillus parasiticus
H400L
the mutation results in a loss of the monooxygenase activity
Aspergillus parasiticus
I528Y
the mutation does not affect enzymatic activity
Aspergillus parasiticus
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
8-O-methyldihydrosterigmatocystin + [reduced NADPH-hemoprotein reductase] + O2
Aspergillus parasiticus
-
aflatoxin B2 + methanol + CO2 + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
?
8-O-methyldihydrosterigmatocystin + [reduced NADPH-hemoprotein reductase] + O2
Aspergillus parasiticus SRRC 143
-
aflatoxin B2 + methanol + CO2 + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
?
8-O-methylsterigmatocystin + [reduced NADPH-hemoprotein reductase] + O2
Aspergillus parasiticus
-
aflatoxin B1 + 2 NADP+ + methanol + [oxidized NADPH-hemoprotein reductase] + H2O + CO2
-
-
?
8-O-methylsterigmatocystin + [reduced NADPH-hemoprotein reductase] + O2
Aspergillus parasiticus SRRC 143
-
aflatoxin B1 + 2 NADP+ + methanol + [oxidized NADPH-hemoprotein reductase] + H2O + CO2
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Aspergillus parasiticus
O13345
-
-
Aspergillus parasiticus SRRC 143
O13345
-
-
Source Tissue
Source Tissue
Commentary
Organism
Textmining
mycelium
-
Aspergillus parasiticus
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
8-O-methyldihydrosterigmatocystin + [reduced NADPH-hemoprotein reductase] + O2
-
721325
Aspergillus parasiticus
aflatoxin B2 + methanol + CO2 + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
8-O-methyldihydrosterigmatocystin + [reduced NADPH-hemoprotein reductase] + O2
-
721325
Aspergillus parasiticus SRRC 143
aflatoxin B2 + methanol + CO2 + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
8-O-methylsterigmatocystin + [reduced NADPH-hemoprotein reductase] + O2
-
721325
Aspergillus parasiticus
aflatoxin B1 + 2 NADP+ + methanol + [oxidized NADPH-hemoprotein reductase] + H2O + CO2
-
-
-
?
8-O-methylsterigmatocystin + [reduced NADPH-hemoprotein reductase] + O2
-
721325
Aspergillus parasiticus SRRC 143
aflatoxin B1 + 2 NADP+ + methanol + [oxidized NADPH-hemoprotein reductase] + H2O + CO2
-
-
-
?
Cloned(Commentary) (protein specific)
Commentary
Organism
expressed in Saccharomyces cerevisiae strain InvSc1
Aspergillus parasiticus
Engineering (protein specific)
Amino acid exchange
Commentary
Organism
A143S
the mutation affects enzymatic activity (approximately 50% of the enzyme activity which converts O-methylsterigmatocystin to aflatoxin B1 is lost)
Aspergillus parasiticus
H400L
the mutation results in a loss of the monooxygenase activity
Aspergillus parasiticus
I528Y
the mutation does not affect enzymatic activity
Aspergillus parasiticus
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
8-O-methyldihydrosterigmatocystin + [reduced NADPH-hemoprotein reductase] + O2
Aspergillus parasiticus
-
aflatoxin B2 + methanol + CO2 + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
?
8-O-methyldihydrosterigmatocystin + [reduced NADPH-hemoprotein reductase] + O2
Aspergillus parasiticus SRRC 143
-
aflatoxin B2 + methanol + CO2 + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
?
8-O-methylsterigmatocystin + [reduced NADPH-hemoprotein reductase] + O2
Aspergillus parasiticus
-
aflatoxin B1 + 2 NADP+ + methanol + [oxidized NADPH-hemoprotein reductase] + H2O + CO2
-
-
?
8-O-methylsterigmatocystin + [reduced NADPH-hemoprotein reductase] + O2
Aspergillus parasiticus SRRC 143
-
aflatoxin B1 + 2 NADP+ + methanol + [oxidized NADPH-hemoprotein reductase] + H2O + CO2
-
-
?
Source Tissue (protein specific)
Source Tissue
Commentary
Organism
Textmining
mycelium
-
Aspergillus parasiticus
-
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
8-O-methyldihydrosterigmatocystin + [reduced NADPH-hemoprotein reductase] + O2
-
721325
Aspergillus parasiticus
aflatoxin B2 + methanol + CO2 + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
8-O-methyldihydrosterigmatocystin + [reduced NADPH-hemoprotein reductase] + O2
-
721325
Aspergillus parasiticus SRRC 143
aflatoxin B2 + methanol + CO2 + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
8-O-methylsterigmatocystin + [reduced NADPH-hemoprotein reductase] + O2
-
721325
Aspergillus parasiticus
aflatoxin B1 + 2 NADP+ + methanol + [oxidized NADPH-hemoprotein reductase] + H2O + CO2
-
-
-
?
8-O-methylsterigmatocystin + [reduced NADPH-hemoprotein reductase] + O2
-
721325
Aspergillus parasiticus SRRC 143
aflatoxin B1 + 2 NADP+ + methanol + [oxidized NADPH-hemoprotein reductase] + H2O + CO2
-
-
-
?
General Information
General Information
Commentary
Organism
metabolism
the enzyme is involved in the biosynthesis of aflatoxins B1, G1, B2, and G2
Aspergillus parasiticus
General Information (protein specific)
General Information
Commentary
Organism
metabolism
the enzyme is involved in the biosynthesis of aflatoxins B1, G1, B2, and G2
Aspergillus parasiticus
Other publictions for EC 1.14.14.117
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [C]
Temperature Range [C]
Temperature Stability [C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [C] (protein specific)
Temperature Range [C] (protein specific)
Temperature Stability [C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
723750
Jamali
Expression of aflatoxin genes ...
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
Res. Microbiol.
164
293-299
2013
-
-
-
-
-
-
-
-
-
-
-
-
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12
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
722440
Udwary
Synthesis of 11-hydroxyl O-met ...
Aspergillus parasiticus, Aspergillus parasiticus SU-1
J. Am. Chem. Soc.
124
5294-5303
2002
-
-
1
-
-
-
-
-
1
-
1
4
-
4
-
-
-
-
-
-
-
-
4
1
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
1
-
1
4
-
-
-
-
-
-
-
-
4
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
721325
Yu
Characterization of the critic ...
Aspergillus parasiticus, Aspergillus parasiticus SRRC 143
Appl. Environ. Microbiol.
64
4834-4841
1998
-
-
1
-
3
-
-
-
-
-
-
4
-
2
-
-
-
-
-
1
-
-
4
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
3
-
-
-
-
-
-
-
-
4
-
-
-
-
-
1
-
-
4
-
-
-
-
-
-
-
-
-
-
1
1
-
-
-
721574
Bhatnagar
Enzymological evidence for sep ...
Aspergillus flavus, Aspergillus flavus SRRC 141, Aspergillus parasiticus, Aspergillus parasiticus SRRC 163
Biochemistry
30
4343-4350
1991
-
-
-
-
-
-
-
2
-
-
-
8
-
4
-
-
2
-
-
-
2
-
8
-
2
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
2
-
-
-
8
-
-
-
2
-
-
2
-
8
-
2
-
-
-
2
-
-
-
-
-
-
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-