| EC |
2.6.1.22 |
| Accepted name: |
(S)-3-amino-2-methylpropionate transaminase |
| Reaction: |
(S)-3-amino-2-methylpropanoate + 2-oxoglutarate = 2-methyl-3-oxopropanoate + L-glutamate |
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For diagram of reaction, click here |
| Other name(s): |
L-3-aminoisobutyrate transaminase; β-aminobutyric transaminase; L-3-aminoisobutyric aminotransferase; β-aminoisobutyrate-α-ketoglutarate transaminase |
| Systematic name: |
(S)-3-amino-2-methylpropanoate:2-oxoglutarate aminotransferase |
| Comments: |
Also acts on β-alanine and other ω-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. |
| Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9031-95-2 |
| References: |
| 1. |
Kakimoto, Y., Kanazawa, A., Taniguchi, K. and Sano, I. β-Aminoisobutyrate-α-ketoglutarate transaminase in relation to β-aminoisobutyric aciduria. Biochim. Biophys. Acta 156 (1968) 374–380. [DOI] [PMID: 5641913] |
| 2. |
Tamaki, N., Sakata, S.F. and Matsuda, K. Purification, properties, and sequencing of aminoisobutyrate aminotransferases from rat liver. Methods Enzymol. 324 (2000) 376–389. [DOI] [PMID: 10989446] |
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| [EC 2.6.1.22 created 1972, modified 1982, modified 2004] |
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