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EC Tree
IUBMB Comments Also acts on beta-alanine and other omega-amino acids having carbon chains between 2 and 5. The two enantiomers of the 2-methyl-3-oxopropanoate formed by the enzyme interconvert by enolization, so that this enzyme, together with EC 2.6.1.40, (R)-3-amino-2-methylpropionate---pyruvate transaminase, provide a route for interconversion of the enantiomers of 3-amino-2-methylpropanoate.
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Synonyms
aminotransferase, L-3-aminoisobutyrate, beta-aminobutyric transaminase, L-3-aminoisobutyrate transaminase, L-3-aminoisobutyric aminotransferase,
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aminotransferase, L-3-aminoisobutyrate
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beta-aminobutyric transaminase
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L-3-aminoisobutyrate transaminase
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L-3-aminoisobutyric aminotransferase
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(S)-3-amino-2-methylpropanoate + 2-oxoglutarate = 2-methyl-3-oxopropanoate + L-glutamate
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amino group transfer
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(S)-3-amino-2-methylpropanoate:2-oxoglutarate aminotransferase
Also acts on beta-alanine and other omega-amino acids having carbon chains between 2 and 5. The two enantiomers of the 2-methyl-3-oxopropanoate formed by the enzyme interconvert by enolization, so that this enzyme, together with EC 2.6.1.40, (R)-3-amino-2-methylpropionate---pyruvate transaminase, provide a route for interconversion of the enantiomers of 3-amino-2-methylpropanoate.
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(S)-3-amino-2-methylpropanoate + 2-oxoglutarate
2-methyl-3-oxopropanoate + L-glutamate
(S)-3-amino-2-methylpropanoate + pyruvate
D-methylmalonate semialdehyde + L-alanine
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r
4-aminobutanoate + 2-oxoglutarate
succinic semialdehyde + L-glutamate
5-aminopentanoate + 2-oxoglutarate
5-oxopentanoate + L-glutamate
beta-alanine + 2-oxoglutarate
malonic semialdehyde + L-glutamate
additional information
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(S)-3-amino-2-methylpropanoate + 2-oxoglutarate
2-methyl-3-oxopropanoate + L-glutamate
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i.e. L-beta-aminoisobutyrate, not D-isomer
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?
(S)-3-amino-2-methylpropanoate + 2-oxoglutarate
2-methyl-3-oxopropanoate + L-glutamate
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involved in omega-amino acid metabolism in mammals
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?
(S)-3-amino-2-methylpropanoate + 2-oxoglutarate
2-methyl-3-oxopropanoate + L-glutamate
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i.e. L-beta-aminoisobutyrate, not D-isomer
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r
4-aminobutanoate + 2-oxoglutarate
succinic semialdehyde + L-glutamate
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transamination at 150% the rate of (S)-3-amino-2-methylpropanoate
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r
4-aminobutanoate + 2-oxoglutarate
succinic semialdehyde + L-glutamate
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transamination at 92% the rate of (S)-3-amino-2-methylpropanoate
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5-aminopentanoate + 2-oxoglutarate
5-oxopentanoate + L-glutamate
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transamination at 145% the rate of (S)-3-amino-2-methylpropanoate
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r
5-aminopentanoate + 2-oxoglutarate
5-oxopentanoate + L-glutamate
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transamination at 33% the rate of (S)-3-amino-2-methylpropanoate
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beta-alanine + 2-oxoglutarate
malonic semialdehyde + L-glutamate
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as good as (S)-3-amino-2-methylpropanoate
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beta-alanine + 2-oxoglutarate
malonic semialdehyde + L-glutamate
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as good as (S)-3-amino-2-methylpropanoate
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r
beta-alanine + 2-oxoglutarate
malonic semialdehyde + L-glutamate
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as good as (S)-3-amino-2-methylpropanoate
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additional information
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no substrates are glyoxylate, pyruvate, oxalacetate, phenylpyruvate
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additional information
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no substrates are 3-aminobutanoate, 2-ethyl-beta-alanine, glycine, L-alpha-alanine, 2-aminoisobutanoate, lysine, taurine, O-phosphoethanolamine, homocarnosine. Poor substrates are 6-aminohexanoate or ornithine, no substrates are pyruvate, oxaloacetate or glyoxylate
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(S)-3-amino-2-methylpropanoate + 2-oxoglutarate
2-methyl-3-oxopropanoate + L-glutamate
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involved in omega-amino acid metabolism in mammals
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?
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pyridoxal 5'-phosphate
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pyridoxal 5'-phosphate
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activates at low concentrations, inhibits at high concentrations
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(S)-3-amino-2-methylpropanoate
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beta-alanine as substrate, not (R)-isomer
2-oxoglutarate
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in excess, substrate inhibition
Antiserum against beta-alanine:2-oxoglutarate aminotransferase
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pyridoxal 5'-phosphate
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inhibits at high concentrations, activates at low concentrations
additional information
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not inhibitory: 6-azauridine, 6-azauridine 5-phosphate
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2.7
(S)-3-amino-2-methylpropanoate
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pH 8.8, 37°C
1.1
beta-Alanine
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pH 8.8, 37°C
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2.7
(S)-3-amino-2-methylpropanoate
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pH 8.8, 37°C
0.7
6-Azauracil
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pH 8.8, 37°C
0.0071
gabaculine
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pH 8.8, 37°C
1.8
5-fluorouracil
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uncompetitive against 2-oxoglutarate, pH 8.8, 37°C
1.9
5-fluorouracil
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competitive to beta-alanine, pH 8.8, 37°C
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0.047
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kidney enzyme, pH 8.8, 37°C
0.096
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brain enzyme, pH 8.8, 37°C
0.133
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liver enzyme, pH 8.8, 37°C
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8.5 - 9.5
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about half-maximal activity at pH 8.5 and 9.5
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37
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assay at
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brenda
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male Sprague Dawley
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brenda
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brenda
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brenda
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brenda
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brenda
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dimer
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2 x 56000, SDS-PAGE
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-20°C, in 0.05 M phosphate buffer, pH 7.5, at least 3 weeks
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-25°C, in 0.1 M phosphate buffer, pH 7.0, 1mM EDTA, 2 mM 2-mercaptoethanol, 0.04 mM pyridoxal-5'-phosphate, few days, 50% loss of activity
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4°C, in 0.1 M phosphate buffer, pH 7.0, 1mM EDTA, 2 mM 2-mercaptoethanol, 0.04 mM pyridoxal-5'-phosphate, 1 week, no loss of activity
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Kakimoto, Y.; Kanazawa, A.; Taniguchi, K.; Sano, I.
beta-Aminoisobutyrate-alpha-ketoglutarate transaminase in relation to beta-aminoisobutyric aciduria
Biochim. Biophys. Acta
156
374-380
1968
Sus scrofa
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Tamaki, N.; Fujimoto, S.; Mizota, C.; Kikugawa, M.
Identity of beta-alanine-oxo-glutarate aminotransferase and L-beta-aminoisobutyrate aminotransferase in rat liver
Biochim. Biophys. Acta
925
238-240
1987
Rattus norvegicus
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Tamaki, N.; Sakata, S.F.; Matsuda, K.
Purification, properties, and sequencing of aminoisobutyrate aminotransferases from rat liver
Methods Enzymol.
324
376-389
2000
Rattus norvegicus
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