(R)-3-amino-2-methylpropionate—pyruvate transaminase
| (R)-3-amino-2-methylpropionate-pyruvate transaminase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 2.6.1.40 | ||||||||
| CAS no. | 37279-00-8 | ||||||||
| 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 (R)-3-amino-2-methylpropionate—pyruvate transaminase (EC 2.6.1.40) is an enzyme that catalyzes the chemical reaction
- (R)-3-amino-2-methylpropanoate + pyruvate 2-methyl-3-oxopropanoate + L-alanine
Thus, the two substrates of this enzyme are (R)-3-amino-2-methylpropanoate and pyruvate, whereas its two products are 2-methyl-3-oxopropanoate and L-alanine.
This enzyme belongs to the family of transferases, specifically the transaminases, which transfer nitrogenous groups. The systematic name of this enzyme class is (R)-3-amino-2-methylpropanoate:pyruvate aminotransferase. Other names in common use include D-3-aminoisobutyrate-pyruvate transaminase, beta-aminoisobutyrate-pyruvate aminotransferase, D-3-aminoisobutyrate-pyruvate aminotransferase, D-3-aminoisobutyrate-pyruvate transaminase, (R)-3-amino-2-methylpropionate transaminase, and D-beta-aminoisobutyrate:pyruvate aminotransferase. But some additional information is that this enzyme catalyzed it transamination with L isomer, but D isomer in natural form, inactive as substrate. Also other names of enzymes similar to this contains, L-3-aminoisobutyrate transaminase, beta-aminobutyric transaminase, L-3-aminoisobutyric aminotransferase, and beta-aminoisobutyrate-alpha-ketoglutarate transaminase.[1]
References
[edit]- ^ "Kakimoto Y, Kanazawa A, Taniguchi K, Sano I (1968), and Tamaki N, Sakata SF, Matsuda K (2000)
- Kakimoto Y, Taniguchi K, Sano I (1969). "D-beta-aminoisobutyrate:pyruvate aminotransferase in mammalian liver and excretion of beta-aminoisobutyrate by man". J. Biol. Chem. 244 (2): 335–40. doi:10.1016/S0021-9258(18)94435-2. PMID 5773299.
- 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 9780121822255. PMID 10989446.
