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branched chain amino acid transaminase 2

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Target not currently curated in GtoImmuPdb

Target id: 2893

Nomenclature: branched chain amino acid transaminase 2

Family: Branched-chain-amino-acid transaminase

Gene and Protein Information Click here for help
Species TM AA Chromosomal Location Gene Symbol Gene Name Reference
Human - 392 19q13.33 BCAT2 branched chain amino acid transaminase 2 1
Mouse - 393 7 29.36 cM Bcat2 branched chain aminotransferase 2, mitochondrial
Rat - 393 1q22 Bcat2 branched chain amino acid transaminase 2 1
Gene and Protein Information Comments
For the human gene and protein we provide details for the longest form, isoform a (from transcript variant a) also known as PP18a. Isoforms b and c (PP18b, PP18c) are shorter at 300 and 352 amino acids (aa) respectively. Two mouse isoforms are produced from 3 transcript variants. Isoform 1 is the longest (details in the table), with isoform 2 having a shorter N-terminus (353 aa).
Previous and Unofficial Names Click here for help
branched-chain-amino-acid aminotransferase, mitochondrial | BCATm | BCAM | BCT2 | Eca40 (Mm) | Bcat-2 | mBcat | branched chain aminotransferase 2, mitochondrial | branched chain aminotransferase 2
Database Links Click here for help
ChEMBL Target
Ensembl Gene
Entrez Gene
Human Protein Atlas
KEGG Enzyme
RefSeq Nucleotide
RefSeq Protein
Selected 3D Structures Click here for help
Image of receptor 3D structure from RCSB PDB
Description:  X-ray crystal structure at 1.65A resolution of human mitochondrial branched chain aminotransferase (BCATm) complexed with a thiazole compound and pmp cofactor.
PDB Id:  5I5X
Ligand:  compound 27 [PMID: 26938474]
Resolution:  1.65Å
Species:  Human
References:  2
Enzyme Reaction Click here for help
EC Number:
Description Reaction Reference
L-leucine + 2-oxoglutarate <=> 4-methyl-2-oxopentanoate + L-glutamate
L-isoleucine + 2-oxoglutarate <=> (S)-3-methyl-2-oxopentanoate + L-glutamate
L-valine + 2-oxoglutarate <=> 3-methyl-2-oxobutanoate + L-glutamate

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Key to terms and symbols View all chemical structures Click column headers to sort
Ligand Sp. Action Value Parameter Reference
BAY-069 Small molecule or natural product Click here for species-specific activity table Hs Inhibition 6.8 pIC50 3
pIC50 6.8 (IC50 1.53x10-7 M) [3]
compound 27 [PMID: 26938474] Small molecule or natural product Ligand has a PDB structure Hs Inhibition 6.7 pIC50 2
pIC50 6.7 (IC50 1.99x10-7 M) [2]
compound 42 [PMID: 26938474] Small molecule or natural product Hs Inhibition 5.8 pIC50 2
pIC50 5.8 (IC50 1.585x10-6 M) [2]
Immuno Process Associations
Immuno Process:  Cytokine production & signalling
Tissue Distribution Comments
In mammals, BCAT2 (BCATm) is expressed in most tissues [4]. In comparison, expression of the cytosilic isozyme BCAT1 (BCATc; UniProt P54687) is restricted to the CNS.
Physiological Consequences of Altering Gene Expression Click here for help
Bcat2 knockout mice are resistant to high-fat diet induced obesity and diabetes
Species:  Mouse
Technique:  Gene knockout
References:  5
General Comments
BCAT2 is a mitochondrial protein that catalyses the first step in the production of the branched chain amino acids leucine, isoleucine, and valine.
HGNC places this protein in the minor histocompatibility antigen (MHA) family. MHAs are known to induce an immunological response in some organ transplants, albeit to a much lesser degree than the major histocompatibility complex (MHC) antigens. Amino acid differences in MHAs can cause slow rejection of transplanted organs even when MHCs are comprehensively matched between donor and recipient.


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1. Bledsoe RK, Dawson PA, Hutson SM. (1997) Cloning of the rat and human mitochondrial branched chain aminotransferases (BCATm). Biochim Biophys Acta, 1339 (1): 9-13. [PMID:9165094]

2. Borthwick JA, Ancellin N, Bertrand SM, Bingham RP, Carter PS, Chung CW, Churcher I, Dodic N, Fournier C, Francis PL et al.. (2016) Structurally Diverse Mitochondrial Branched Chain Aminotransferase (BCATm) Leads with Varying Binding Modes Identified by Fragment Screening. J Med Chem, 59 (6): 2452-67. [PMID:26938474]

3. Günther J, Hillig RC, Zimmermann K, Kaulfuss S, Lemos C, Nguyen D, Rehwinkel H, Habgood M, Lechner C, Neuhaus R et al.. (2022) BAY-069, a Novel (Trifluoromethyl)pyrimidinedione-Based BCAT1/2 Inhibitor and Chemical Probe. J Med Chem, 65 (21): 14366-14390. [PMID:36261130]

4. Hutson S. (2001) Structure and function of branched chain aminotransferases. Prog Nucleic Acid Res Mol Biol, 70: 175-206. [PMID:11642362]

5. She P, Reid TM, Bronson SK, Vary TC, Hajnal A, Lynch CJ, Hutson SM. (2007) Disruption of BCATm in mice leads to increased energy expenditure associated with the activation of a futile protein turnover cycle. Cell Metab, 6 (3): 181-94. [PMID:17767905]

How to cite this page Branched-chain-amino-acid transaminase: branched chain amino acid transaminase 2. Last modified on 31/10/2022. Accessed on 14/06/2024. IUPHAR/BPS Guide to PHARMACOLOGY,