(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
Search PMC articles PubMed articles NCBI proteins

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 ${\displaystyle \rightleftharpoons }$ 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

• 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.