BRENDA - Enzyme Database show
show all sequences of 1.1.3.42

Functional analysis of fungal polyketide biosynthesis genes

Fujii, I.; J. Antibiot. 63, 207-218 (2010)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
expression in Aspergillus oryzae under the starch inducible alpha-amylase promoter, expression in Pichia pastoris
Alternaria solani
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
prosolanapyrone II + O2
Alternaria solani
the enzyme is involved in solanapyrone biosynthesis
prosolanapyrone III + H2O2
-
-
?
prosolanapyrone II + O2
Alternaria solani 548
the enzyme is involved in solanapyrone biosynthesis
prosolanapyrone III + H2O2
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Alternaria solani
D7UQ40
-
-
Alternaria solani 548
D7UQ40
-
-
Purification (Commentary)
Commentary
Organism
-
Alternaria solani
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
prosolanapyrone II + O2
the enzyme is involved in solanapyrone biosynthesis
715308
Alternaria solani
prosolanapyrone III + H2O2
-
-
-
?
prosolanapyrone II + O2
the bifunctional enzyme catalyses the oxidation of prosolanapyrone II and the subsequent cycloaddition of the product prosolanapyrone III to (-)-solanapyrone A
715308
Alternaria solani
prosolanapyrone III + H2O2
in an enzyme-catalyzed Diels–Alder reaction the product prosolanapyrone III is isomerized to solanapyrone A (exo Diels-Alder cyclization, [4+2] cycloaddition). Solanapyrone D (endo Diels-Alder cyclization) is formed by a nonenzymatic Diels-Alder cyclization of prosolanopyrone III in polar solvents. The enzyme coverts prosolanapyrone II into solanapyrone A, solanapyrone D and prosolanapyrone III in the ratio 7:1:1
-
-
?
prosolanapyrone II + O2
the enzyme is involved in solanapyrone biosynthesis
715308
Alternaria solani 548
prosolanapyrone III + H2O2
-
-
-
?
prosolanapyrone II + O2
the bifunctional enzyme catalyses the oxidation of prosolanapyrone II and the subsequent cycloaddition of the product prosolanapyrone III to (-)-solanapyrone A
715308
Alternaria solani 548
prosolanapyrone III + H2O2
in an enzyme-catalyzed Diels–Alder reaction the product prosolanapyrone III is isomerized to solanapyrone A (exo Diels-Alder cyclization, [4+2] cycloaddition). Solanapyrone D (endo Diels-Alder cyclization) is formed by a nonenzymatic Diels-Alder cyclization of prosolanopyrone III in polar solvents. The enzyme coverts prosolanapyrone II into solanapyrone A, solanapyrone D and prosolanapyrone III in the ratio 7:1:1
-
-
?
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
30
-
assay at
Alternaria solani
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7
-
assay at
Alternaria solani
Cofactor
Cofactor
Commentary
Organism
Structure
flavin
flavin-dependent oxidase, the enzyme possesses a flavin-binding domain
Alternaria solani
Cloned(Commentary) (protein specific)
Commentary
Organism
expression in Aspergillus oryzae under the starch inducible alpha-amylase promoter, expression in Pichia pastoris
Alternaria solani
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
flavin
flavin-dependent oxidase, the enzyme possesses a flavin-binding domain
Alternaria solani
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
prosolanapyrone II + O2
Alternaria solani
the enzyme is involved in solanapyrone biosynthesis
prosolanapyrone III + H2O2
-
-
?
prosolanapyrone II + O2
Alternaria solani 548
the enzyme is involved in solanapyrone biosynthesis
prosolanapyrone III + H2O2
-
-
?
Purification (Commentary) (protein specific)
Commentary
Organism
-
Alternaria solani
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
prosolanapyrone II + O2
the enzyme is involved in solanapyrone biosynthesis
715308
Alternaria solani
prosolanapyrone III + H2O2
-
-
-
?
prosolanapyrone II + O2
the bifunctional enzyme catalyses the oxidation of prosolanapyrone II and the subsequent cycloaddition of the product prosolanapyrone III to (-)-solanapyrone A
715308
Alternaria solani
prosolanapyrone III + H2O2
in an enzyme-catalyzed Diels–Alder reaction the product prosolanapyrone III is isomerized to solanapyrone A (exo Diels-Alder cyclization, [4+2] cycloaddition). Solanapyrone D (endo Diels-Alder cyclization) is formed by a nonenzymatic Diels-Alder cyclization of prosolanopyrone III in polar solvents. The enzyme coverts prosolanapyrone II into solanapyrone A, solanapyrone D and prosolanapyrone III in the ratio 7:1:1
-
-
?
prosolanapyrone II + O2
the enzyme is involved in solanapyrone biosynthesis
715308
Alternaria solani 548
prosolanapyrone III + H2O2
-
-
-
?
prosolanapyrone II + O2
the bifunctional enzyme catalyses the oxidation of prosolanapyrone II and the subsequent cycloaddition of the product prosolanapyrone III to (-)-solanapyrone A
715308
Alternaria solani 548
prosolanapyrone III + H2O2
in an enzyme-catalyzed Diels–Alder reaction the product prosolanapyrone III is isomerized to solanapyrone A (exo Diels-Alder cyclization, [4+2] cycloaddition). Solanapyrone D (endo Diels-Alder cyclization) is formed by a nonenzymatic Diels-Alder cyclization of prosolanopyrone III in polar solvents. The enzyme coverts prosolanapyrone II into solanapyrone A, solanapyrone D and prosolanapyrone III in the ratio 7:1:1
-
-
?
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
30
-
assay at
Alternaria solani
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7
-
assay at
Alternaria solani
Other publictions for EC 1.1.3.42
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)
741025
Kim
Functional analyses of the Die ...
Alternaria solani, Ascochyta rabiei
Mol. Plant Microbe Interact.
28
482-496
2015
-
-
-
-
-
-
-
-
-
-
-
2
-
2
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
714734
Kasahara
Solanapyrone synthase, a possi ...
Alternaria solani, Alternaria solani 548
ChemBioChem
11
1245-1252
2010
-
-
-
-
-
-
-
-
-
-
-
-
-
6
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
715308
Fujii
Functional analysis of fungal ...
Alternaria solani, Alternaria solani 548
J. Antibiot.
63
207-218
2010
-
-
1
-
-
-
-
-
-
-
-
2
-
5
-
-
1
-
-
-
-
-
4
-
1
-
-
-
1
-
-
1
-
-
-
-
-
1
1
-
-
-
-
-
-
-
-
-
-
2
-
-
-
1
-
-
-
-
4
-
1
-
-
-
1
-
-
-
-
-
-
-
-
-
714520
Katayama
Purification and N-terminal am ...
Alternaria solani
Biosci. Biotechnol. Biochem.
72
604-607
2008
-
-
-
-
-
-
-
-
-
-
2
-
-
2
-
-
1
-
-
-
2
1
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
1
-
-
2
1
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
714292
Katayama
Enzymatic activity and partial ...
Alternaria solani
Biochim. Biophys. Acta
1384
387-395
1998
-
-
-
-
-
1
-
1
-
1
1
-
-
2
-
-
1
-
-
-
2
2
-
-
-
-
-
-
3
-
1
1
-
-
-
-
-
-
1
-
-
1
-
-
-
1
-
1
1
-
-
-
-
1
-
-
2
2
-
-
-
-
-
-
3
-
1
-
-
-
-
-
-
-