BRENDA - Enzyme Database show
show all sequences of 1.14.99.34

FAD-dependent epoxidase as a key enzyme in fungal metabolism of prenylated flavonoids

Tanaka, M.; Tahara, S.; Phytochemistry 46, 433-439 (1997)
No PubMed abstract available

Data extracted from this reference:

Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
7-O-methylluteone + NADPH + O2
Botrytis cinerea
key enzyme in metabolism of prenylated flavonoids. Enzyme is induced by the substrate analogue 6-prenylnaringenin
dihydrofurano derivative of 7-O-methylluteone + NADP+ + H2O
-
Botrytis cinerea
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Botrytis cinerea
-
-
-
Source Tissue
Source Tissue
Commentary
Organism
Textmining
mycelium
-
Botrytis cinerea
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
2'-hydroxylupalbigenin + NADPH + O2
-
285469
Botrytis cinerea
?
-
-
-
?
2,3-dihydrokievitone + NADPH + O2
-
285469
Botrytis cinerea
?
-
-
-
?
7-O-methyl-2,3-dehydrokievitone + NADPH + O2
-
285469
Botrytis cinerea
?
-
-
-
?
7-O-methylluteone + NADH + O2
-
285469
Botrytis cinerea
dihydrofurano derivative of 7-O-methylluteone + NAD+ + H2O
-
285469
Botrytis cinerea
?
7-O-methylluteone + NADPH + O2
-
285469
Botrytis cinerea
dihydrofurano derivative of 7-O-methylluteone + NADP+ + H2O
-
285469
Botrytis cinerea
?
7-O-methylluteone + NADPH + O2
key enzyme in metabolism of prenylated flavonoids. Enzyme is induced by the substrate analogue 6-prenylnaringenin
285469
Botrytis cinerea
dihydrofurano derivative of 7-O-methylluteone + NADP+ + H2O
-
285469
Botrytis cinerea
?
licoisoflavone A + NADPH + O2
-
285469
Botrytis cinerea
?
-
-
-
?
luteone + NADPH + O2
-
285469
Botrytis cinerea
?
-
-
-
?
wighteone + NADPH + O2
-
285469
Botrytis cinerea
?
-
-
-
?
Cofactor
Cofactor
Commentary
Organism
Structure
FAD
required for maximal activity
Botrytis cinerea
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
FAD
required for maximal activity
Botrytis cinerea
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
7-O-methylluteone + NADPH + O2
Botrytis cinerea
key enzyme in metabolism of prenylated flavonoids. Enzyme is induced by the substrate analogue 6-prenylnaringenin
dihydrofurano derivative of 7-O-methylluteone + NADP+ + H2O
-
Botrytis cinerea
?
Source Tissue (protein specific)
Source Tissue
Commentary
Organism
Textmining
mycelium
-
Botrytis cinerea
-
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
2'-hydroxylupalbigenin + NADPH + O2
-
285469
Botrytis cinerea
?
-
-
-
?
2,3-dihydrokievitone + NADPH + O2
-
285469
Botrytis cinerea
?
-
-
-
?
7-O-methyl-2,3-dehydrokievitone + NADPH + O2
-
285469
Botrytis cinerea
?
-
-
-
?
7-O-methylluteone + NADH + O2
-
285469
Botrytis cinerea
dihydrofurano derivative of 7-O-methylluteone + NAD+ + H2O
-
285469
Botrytis cinerea
?
7-O-methylluteone + NADPH + O2
-
285469
Botrytis cinerea
dihydrofurano derivative of 7-O-methylluteone + NADP+ + H2O
-
285469
Botrytis cinerea
?
7-O-methylluteone + NADPH + O2
key enzyme in metabolism of prenylated flavonoids. Enzyme is induced by the substrate analogue 6-prenylnaringenin
285469
Botrytis cinerea
dihydrofurano derivative of 7-O-methylluteone + NADP+ + H2O
-
285469
Botrytis cinerea
?
licoisoflavone A + NADPH + O2
-
285469
Botrytis cinerea
?
-
-
-
?
luteone + NADPH + O2
-
285469
Botrytis cinerea
?
-
-
-
?
wighteone + NADPH + O2
-
285469
Botrytis cinerea
?
-
-
-
?
Other publictions for EC 1.14.99.34
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)
285469
Tanaka
-
FAD-dependent epoxidase as a k ...
Botrytis cinerea
Phytochemistry
46
433-439
1997
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