IPR033939
Branched-chain aminotransferase
InterPro entry
Short name | BCAT_family |
Overlapping homologous superfamilies | |
family relationships |
Description
Branched-chain aminotransferase catalyses the transamination of the branched-chain amino acids leucine, isoleucine and valine to their respective alpha-keto acids, alpha-ketoisocaproate, alpha-keto-beta-methylvalerate and alpha-ketoisovalerate. The enzyme requires pyridoxal 5'-phosphate (PLP) as a cofactor to catalyze the reaction. It has been found that mammals have two forms of the enzyme - mitochondrial and cytosolic forms while bacteria contain only one form of the enzyme
[1]. The mitochondrial form plays a significant role in skeletal muscle glutamine and alanine synthesis and in interorgan nitrogen metabolism
[2]. Members of this entry are widely distributed in all three forms of life.
References
1.Human mitochondrial branched chain aminotransferase: structural basis for substrate specificity and role of redox active cysteines. Conway ME, Yennawar N, Wallin R, Poole LB, Hutson SM. Biochim. Biophys. Acta 1647, 61-5, (2003). View articlePMID: 12686109
2.Structure and function of branched chain aminotransferases. Hutson S. Prog. Nucleic Acid Res. Mol. Biol. 70, 175-206, (2001). View articlePMID: 11642362
GO terms
biological process
molecular function
cellular component
- None
Cross References
Contributing Member Database Entry
- CDD:cd01557
Representative structure
1iye: CRYSTAL STRUCTURE OF ESCHELICHIA COLI BRANCHED-CHAIN AMINO ACID AMINOTRANSFERASE