BRENDA - Enzyme Database
show all sequences of 1.4.3.15

Studies on the metabolism of D-amino acid in microorganisms. Part 4. On the nature of the purified D-glutamic-aspartic oxidase of Aspergillus ustus

Mitzushima, S; J. Gen. Appl. Microbiol. 3, 233-239 (1957)
No PubMed abstract available

Data extracted from this reference:

General Stability
General Stability
Organism
very labile when FAD is removed from the enzyme
Aspergillus ustus
Inhibitors
Inhibitors
Commentary
Organism
Structure
FMN
competes with FAD
Aspergillus ustus
KCN
remarkable inhibition at 1 mM, inhibition is only slight with 2,6-dichlorophenol-indophenol electron acceptor but higher when indophenol is used
Aspergillus ustus
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
D-aspartic acid + H2O + O2
Aspergillus ustus
-
oxaloacetate + NH3 + H2O2
-
-
?
D-glutamic acid + H2O + O2
Aspergillus ustus
-
2-oxoglutarate + NH3 + H2O2
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Aspergillus ustus
-
strain f
-
Purification (Commentary)
Commentary
Organism
90% pure
Aspergillus ustus
Source Tissue
Source Tissue
Commentary
Organism
Textmining
mycelium
-
Aspergillus ustus
-
Storage Stability
Storage Stability
Organism
-20°C, several months
Aspergillus ustus
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
D-aspartic acid + H2O + O2
-
391754
Aspergillus ustus
oxaloacetate + NH3 + H2O2
-
-
-
?
D-aspartic acid + H2O + O2
D-glutamate and D-aspartate are oxidized at the same rate
391754
Aspergillus ustus
oxaloacetate + NH3 + H2O2
-
391754
Aspergillus ustus
?
D-glutamic acid + H2O + O2
-
391754
Aspergillus ustus
2-oxoglutarate + NH3 + H2O2
-
-
-
?
D-glutamic acid + H2O + O2
D-glutamate and D-aspartate are oxidized at the same rate
391754
Aspergillus ustus
2-oxoglutarate + NH3 + H2O2
-
391754
Aspergillus ustus
?
additional information
DL-alpha-aminoadipic acid not deaminated, alpha-aminomalonic acid not deaminated, possible acceptors: oxygen, ferricyanide, 2,6-dichlorophenol-indophenol and methylene blue
391754
Aspergillus ustus
?
-
-
-
-
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
30
-
assay at
Aspergillus ustus
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
0.0833
-
D-glutamate
-
Aspergillus ustus
Cofactor
Cofactor
Commentary
Organism
Structure
FAD
flavoprotein
Aspergillus ustus
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
FAD
flavoprotein
Aspergillus ustus
General Stability (protein specific)
General Stability
Organism
very labile when FAD is removed from the enzyme
Aspergillus ustus
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
FMN
competes with FAD
Aspergillus ustus
KCN
remarkable inhibition at 1 mM, inhibition is only slight with 2,6-dichlorophenol-indophenol electron acceptor but higher when indophenol is used
Aspergillus ustus
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
D-aspartic acid + H2O + O2
Aspergillus ustus
-
oxaloacetate + NH3 + H2O2
-
-
?
D-glutamic acid + H2O + O2
Aspergillus ustus
-
2-oxoglutarate + NH3 + H2O2
-
-
?
Purification (Commentary) (protein specific)
Commentary
Organism
90% pure
Aspergillus ustus
Source Tissue (protein specific)
Source Tissue
Commentary
Organism
Textmining
mycelium
-
Aspergillus ustus
-
Storage Stability (protein specific)
Storage Stability
Organism
-20°C, several months
Aspergillus ustus
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
D-aspartic acid + H2O + O2
-
391754
Aspergillus ustus
oxaloacetate + NH3 + H2O2
-
-
-
?
D-aspartic acid + H2O + O2
D-glutamate and D-aspartate are oxidized at the same rate
391754
Aspergillus ustus
oxaloacetate + NH3 + H2O2
-
391754
Aspergillus ustus
?
D-glutamic acid + H2O + O2
-
391754
Aspergillus ustus
2-oxoglutarate + NH3 + H2O2
-
-
-
?
D-glutamic acid + H2O + O2
D-glutamate and D-aspartate are oxidized at the same rate
391754
Aspergillus ustus
2-oxoglutarate + NH3 + H2O2
-
391754
Aspergillus ustus
?
additional information
DL-alpha-aminoadipic acid not deaminated, alpha-aminomalonic acid not deaminated, possible acceptors: oxygen, ferricyanide, 2,6-dichlorophenol-indophenol and methylene blue
391754
Aspergillus ustus
?
-
-
-
-
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
30
-
assay at
Aspergillus ustus
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
0.0833
-
D-glutamate
-
Aspergillus ustus
Other publictions for EC 1.4.3.15
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)
677271
Takahashi
Physiological role of D-aspart ...
Vanrija humicola
Yeast
22
1203-1212
2005
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4
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391755
Onishi
Mutants of Neurospora deficien ...
Neurospora crassa
J. Biol. Chem.
237
138-142
1962
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391754
Mitzushima
-
Studies on the metabolism of D ...
Aspergillus ustus
J. Gen. Appl. Microbiol.
3
233-239
1957
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