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Crystal structure of a novel thermostable (S)-enantioselective omega-transaminase from Thermomicrobium roseumCrystal structure of a novel thermostable (S)-enantioselective omega-transaminase from Thermomicrobium roseum
Structural highlights
FunctionPublication Abstract from PubMedTransaminases catalyze the reversible transfer reaction of an amino group between a primary amine and an alpha-keto acid, utilizing pyridoxal 5'-phosphate as a cofactor. omega-transaminases (omegaTAs) recognize an amino group linked to a non-alpha carbon of amine substrates. Recently, a novel (S)-enantioselective omegaTA from Thermomicrobium roseum (Tr-omegaTA) was identified and its enzymatic activity reported. However, the detailed mechanism of (S)-enantioselective substrate recognition remained unclear. In this study, we determined the crystal structure of Tr-omegaTA at 1.8 A resolution to elucidate the mechanism underlying Tr-omegaTA substrate (S)-enantioselectivity. A structural analysis of Tr-omegaTA along with molecular docking simulations revealed that two pockets at the active site tightly restrict the size and orientation of functional groups of substrate candidates. Based on the structural information and docking simulation results, we propose a comprehensive catalytic mechanism of Tr-omegaTA. The present study thus provides structural and functional insights into the (S)-enantioselectivity of Tr-omegaTA. Structural basis of substrate recognition by a novel thermostable (S)-enantioselective omega-transaminase from Thermomicrobium roseum.,Kwon S, Lee JH, Kim CM, Jang H, Yun H, Jeon JH, So I, Park HH Sci Rep. 2019 May 6;9(1):6958. doi: 10.1038/s41598-019-43490-2. PMID:31061438[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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