(S)-3-amino-2-methylpropionate transaminase
| (S)-3-amino-2-methylpropionate transaminase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 2.6.1.22 | ||||||||
| CAS no. | 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 | ||||||||
| |||||||||
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 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
[edit]- Kakimoto Y, Kanazawa A, Taniguchi K, Sano I (1968). "Beta-aminoisobutyrate-alpha-ketoglutarate transaminase in relation to beta-aminoisobutyric aciduria". Biochim. Biophys. Acta. 156 (2): 374–80. doi:10.1016/0304-4165(68)90267-5. PMID 5641913.
- Tamaki N, Sakata SF, Matsuda K (2000). "Purification, Properties, and Sequencing of Aminoisobutyrate Aminotransferases from Rat Liver". Branched-Chain Amino Acids, Part B. Methods in Enzymology. Vol. 324. pp. 376–89. doi:10.1016/S0076-6879(00)24247-X. ISBN 978-0-12-182225-5. PMID 10989446.
