Summary
Structures of the branched-chain amino acid aminotransferase fromE. coliand its complexes with substrate analogues have been solved by X-ray crystallographic method. BCAT is in a hexameric form, and catalyzes the transamination of branched-chain amino acids. The hexamer can be regarded as the assembly of three dimer units around a 3-fold axis. On binding of the substrate analogue, the flexible loop, which is disordered in the unliganded enzyme, moves toward the active-site entrance and shields the substrate from the solvent region. a-Carboxylate of the substrate directly interacts with an OH group of Tyr and two NH groups of β-turn and indirectly with Arg. The side chain of the branched-chain amino acid is in the cavity formed by aromatic rings and an isopropyl group of the active site residues.
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Hirotsu, K., Goto, M., Miyahara, I., Hayashi, H., Kagamiyama, H., Okada, K. (2000). Structure, Induced Fit and Substrate Recognition of E. coli Branched-Chain Amino Acid Aminotransferase. In: Iriarte, A., Martinez-Carrion, M., Kagan, H.M. (eds) Biochemistry and Molecular Biology of Vitamin B6 and PQQ-dependent Proteins. Birkhäuser, Basel. https://doi.org/10.1007/978-3-0348-8397-9_31
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DOI: https://doi.org/10.1007/978-3-0348-8397-9_31
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