BRENDA - Enzyme Database show
show all sequences of 2.6.1.31

Pyridoxamine-oxaloacetic transaminase of rat kidney

Wu, H.L.C.; Mason, M.; J. Biol. Chem. 239, 1492-1497 (1964)

Data extracted from this reference:

Activating Compound
Activating Compound
Commentary
Organism
Structure
arsenate
activation, less effective than phosphate
Rattus norvegicus
D-Aspartate
increases activity
Rattus norvegicus
diphosphate
activation, less effective than phosphate
Rattus norvegicus
phosphate
essential, activation in absence of diethylstilbestrol and pyridoxal 5'-phosphate
Rattus norvegicus
Inhibitors
Inhibitors
Commentary
Organism
Structure
2-oxoglutarate
inhibition at pH 7.0 is higher than at pH 8.5, 3.33 mM in presence of equimolar concentrations of oxaloacetate
Rattus norvegicus
2-Oxomalonate
inhibition at pH 7.0 is higher than at pH 8.5, 0.4 mM in presence of equimolar concentrations of oxaloacetate
Rattus norvegicus
3,3-Dimethylglutamic acid
not at pH 7.0, weak at pH 8.0
Rattus norvegicus
3-oxoadipate
inhibition at pH 7.0 is higher than at pH 8.5, 3.33 mM in presence of equimolar concentrations of oxaloacetate
Rattus norvegicus
adipic acid
not at pH 7.0, weak at pH 8.0
Rattus norvegicus
Benzylmalonic acid
not at pH 7.0, weak at pH 8.0
Rattus norvegicus
Diethylstilbestrol diphosphate
-
Rattus norvegicus
L-aspartate
-
Rattus norvegicus
L-glutamate
-
Rattus norvegicus
pyridoxal 5'-phosphate
-
Rattus norvegicus
pyridoxamine phosphate
-
Rattus norvegicus
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.012
-
oxaloacetate
somewhat higher at very high levels of pyridoxamine, 14 mM
Rattus norvegicus
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
pyridoxamine + oxaloacetate
Rattus norvegicus
-
pyridoxal + L-aspartate
-
-
r
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Rattus norvegicus
-
-
-
Purification (Commentary)
Commentary
Organism
979fold
Rattus norvegicus
Source Tissue
Source Tissue
Commentary
Organism
Textmining
kidney
-
Rattus norvegicus
-
Specific Activity [micromol/min/mg]
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
0.066
-
purified enzyme
Rattus norvegicus
Storage Stability
Storage Stability
Organism
frozen, 20% loss of activity after 2 months
Rattus norvegicus
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
pyridoxamine + oxaloacetate
-
639962
Rattus norvegicus
pyridoxal + L-aspartate
-
-
-
r
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
8.5
-
-
Rattus norvegicus
pH Range
pH Minimum
pH Maximum
Commentary
Organism
7.5
9.5
about 50% of activity maximum at pH 7.5 and pH 9.5
Rattus norvegicus
Activating Compound (protein specific)
Activating Compound
Commentary
Organism
Structure
arsenate
activation, less effective than phosphate
Rattus norvegicus
D-Aspartate
increases activity
Rattus norvegicus
diphosphate
activation, less effective than phosphate
Rattus norvegicus
phosphate
essential, activation in absence of diethylstilbestrol and pyridoxal 5'-phosphate
Rattus norvegicus
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
2-oxoglutarate
inhibition at pH 7.0 is higher than at pH 8.5, 3.33 mM in presence of equimolar concentrations of oxaloacetate
Rattus norvegicus
2-Oxomalonate
inhibition at pH 7.0 is higher than at pH 8.5, 0.4 mM in presence of equimolar concentrations of oxaloacetate
Rattus norvegicus
3,3-Dimethylglutamic acid
not at pH 7.0, weak at pH 8.0
Rattus norvegicus
3-oxoadipate
inhibition at pH 7.0 is higher than at pH 8.5, 3.33 mM in presence of equimolar concentrations of oxaloacetate
Rattus norvegicus
adipic acid
not at pH 7.0, weak at pH 8.0
Rattus norvegicus
Benzylmalonic acid
not at pH 7.0, weak at pH 8.0
Rattus norvegicus
Diethylstilbestrol diphosphate
-
Rattus norvegicus
L-aspartate
-
Rattus norvegicus
L-glutamate
-
Rattus norvegicus
pyridoxal 5'-phosphate
-
Rattus norvegicus
pyridoxamine phosphate
-
Rattus norvegicus
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.012
-
oxaloacetate
somewhat higher at very high levels of pyridoxamine, 14 mM
Rattus norvegicus
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
pyridoxamine + oxaloacetate
Rattus norvegicus
-
pyridoxal + L-aspartate
-
-
r
Purification (Commentary) (protein specific)
Commentary
Organism
979fold
Rattus norvegicus
Source Tissue (protein specific)
Source Tissue
Commentary
Organism
Textmining
kidney
-
Rattus norvegicus
-
Specific Activity [micromol/min/mg] (protein specific)
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
0.066
-
purified enzyme
Rattus norvegicus
Storage Stability (protein specific)
Storage Stability
Organism
frozen, 20% loss of activity after 2 months
Rattus norvegicus
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
pyridoxamine + oxaloacetate
-
639962
Rattus norvegicus
pyridoxal + L-aspartate
-
-
-
r
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
8.5
-
-
Rattus norvegicus
pH Range (protein specific)
pH Minimum
pH Maximum
Commentary
Organism
7.5
9.5
about 50% of activity maximum at pH 7.5 and pH 9.5
Rattus norvegicus
Other publictions for EC 2.6.1.31
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)
639962
Wu
Pyridoxamine-oxaloacetic trans ...
Rattus norvegicus
J. Biol. Chem.
239
1492-1497
1964
4
-
-
-
-
-
11
1
-
-
-
1
-
1
-
-
1
-
-
1
1
1
1
-
-
-
-
-
1
1
-
-
-
-
-
4
-
-
-
-
-
-
-
11
-
1
-
-
-
1
-
-
-
1
-
1
1
1
1
-
-
-
-
-
1
1
-
-
-
-
-
-
-
-
639961
Wada
Enzymatic transamination of py ...
Escherichia coli, Oryctolagus cuniculus
J. Biol. Chem.
237
127-132
1962
-
-
-
-
-
-
10
4
-
-
-
2
-
2
-
-
2
-
-
1
4
-
4
-
2
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
10
-
4
-
-
-
2
-
-
-
2
-
1
4
-
4
-
2
-
-
-
2
-
-
-
-
-
-
-
-
-