Three-Dimensional Structure of Branched-Chain Amino Acid Transaminase from Thermoproteus uzoniensis in Complex with L-Norvaline

• Published in: Crystallography reports Vol. 65; no. 5; pp. 740 - 743
• Main Authors: Boyko, K. M., Nikolaeva, A. Yu, Timofeev, V. I., Popov, V. O., Bezsudnova, E. Yu
• Format: Journal Article
• Language: English
• Published: Moscow Pleiades Publishing 2020; Springer Nature B.V
• Subjects: Amines; Amino acids; Binding; Chain branching; Chains; Crystal structure; Crystallography and Scattering Methods; Enzymes; Physics; Physics and Astronomy; Structure of Macromolecular Compounds; Substrates; Thermal stability; Transaminases
• ISSN: 1063-7745; 1562-689X
• DOI: 10.1134/S1063774520040045

Transaminases (aminotransferases) are stereospecific enzymes catalyzing the reversible amino group transfer from various substrates. Transaminases are key enzymes in amino acid metabolism in all organisms, and they show promise for fine organic synthesis. Among a diversity of transaminases, as-yet poorly characterized pyridoxal 5′-phosphate-dependent fold type IV transaminases have attracted great interest. This transaminase family shows specificity for both D- and L-amino acids and (R)-amines. The crystal structure of thermally stable fold type IV branched-chain amino acid transaminase from the archaeon Thermoproteus uzoniensis in complex with the non-natural substrate L-norvaline was established. The mechanism of substrate binding is considered. The key amino acids involved in the substrate binding are described.