Biology:(S)-3-amino-2-methylpropionate transaminase
| (S)-3-amino-2-methylpropionate transaminase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 2.6.1.22 | ||||||||
| CAS number | 9031-95-2 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
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In enzymology, a (S)-3-amino-2-methylpropionate transaminase (EC 2.6.1.22) is an enzyme that catalyzes the chemical reaction
- (S)-3-amino-2-methylpropanoate + 2-oxoglutarate [math]\displaystyle{ \rightleftharpoons }[/math] 2-methyl-3-oxopropanoate + L-glutamate
Thus, the two substrates of this enzyme are (S)-3-amino-2-methylpropanoate and 2-oxoglutarate, whereas its two products are 2-methyl-3-oxopropanoate and L-glutamate.
This enzyme belongs to the family of transferases, specifically the transaminases, which transfer nitrogenous groups. The systematic name of this enzyme class is (S)-3-amino-2-methylpropanoate:2-oxoglutarate aminotransferase. Other names in common use include L-3-aminoisobutyrate transaminase, beta-aminobutyric transaminase, L-3-aminoisobutyric aminotransferase, and beta-aminoisobutyrate-alpha-ketoglutarate transaminase. This enzyme participates in valine, leucine and isoleucine degradation.
References
- "Beta-aminoisobutyrate-alpha-ketoglutarate transaminase in relation to beta-aminoisobutyric aciduria". Biochim. Biophys. Acta 156 (2): 374–80. 1968. doi:10.1016/0304-4165(68)90267-5. PMID 5641913.
- "Purification, properties, and sequencing of aminoisobutyrate aminotransferases from rat liver". Methods Enzymol.. Methods in Enzymology 324: 376–89. 2000. doi:10.1016/S0076-6879(00)24247-X. ISBN 978-0-12-182225-5. PMID 10989446.
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