EC |
2.6.1.42 |
Accepted name: |
branched-chain-amino-acid transaminase |
Reaction: |
L-leucine + 2-oxoglutarate = 4-methyl-2-oxopentanoate + L-glutamate |
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For diagram of reaction, click here, of leucine biosynthesis click here, of isoleucine and valine biosynthesis, click here, of coenzyme-A biosynthesis, click here and for diagram of mechanism, click here |
Other name(s): |
transaminase B; branched-chain amino acid aminotransferase; branched-chain amino acid-glutamate transaminase; branched-chain aminotransferase; L-branched chain amino acid aminotransferase; glutamate-branched-chain amino acid transaminase |
Systematic name: |
branched-chain-amino-acid:2-oxoglutarate aminotransferase |
Comments: |
Also acts on L-isoleucine and L-valine, and thereby differs from EC 2.6.1.6, leucine transaminase, which does not. It also differs from EC 2.6.1.66, valine—pyruvate transaminase. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9054-65-3 |
References: |
1. |
Aki, K., Ogawa, K. and Ichihara, A. Transaminases of branched chain amino acids. IV. Purification and properties of two enzymes from rat liver. Biochim. Biophys. Acta 159 (1968) 276–284. [DOI] [PMID: 4968655] |
2. |
Aki, K., Yokojima, A. and Ichihara, A. Transaminase of branched chain amino acids. VI. Purification and properties of the hog brain enzyme. J. Biochem. (Tokyo) 65 (1969) 539–544. [PMID: 4979711] |
3. |
Ichihara, A. and Koyama, E. Transaminase of branched chain amino acids. I. Branched chain amino acids-α-ketoglutarate transaminase. J. Biochem. (Tokyo) 59 (1966) 160–169. [PMID: 5943594] |
4. |
Taylor, R.T. and Jenkins, W.T. Leucine aminotransferase. II. Purification and characterization. J. Biol. Chem. 241 (1966) 4396–4405. [PMID: 5922965] |
5. |
Rudman, D. and Meister, A. Transamination in Escherichia coli. J. Biol. Chem. 200 (1953) 591–604. [PMID: 13034817] |
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[EC 2.6.1.42 created 1972] |
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