6IO1

Crystal structure of a novel thermostable (S)-enantioselective omega-transaminase from Thermomicrobium roseum

Summary for 6IO1

• Entry DOI: 10.2210/pdb6io1/pdb
• Descriptor: Aminotransferase, class III, 4'-DEOXY-4'-AMINOPYRIDOXAL-5'-PHOSPHATE (3 entities in total)
• Functional Keywords: enantioselectivity, omega-transaminase, substrate recognition thermomicrobium roseum, transamination, transferase
• Biological source: Thermomicrobium roseum (strain ATCC 27502 / DSM 5159 / P-2)
• Total number of polymer chains: 2
• Total formula weight: 99295.48

Authors

Park, H.H.,Kwon, S. (deposition date: 2018-10-29, release date: 2019-05-22, Last modification date: 2023-11-22)

Primary citation

Kwon, S.,Lee, J.H.,Kim, C.M.,Jang, H.,Yun, H.,Jeon, J.H.,So, I.,Park, H.H.
Structural basis of substrate recognition by a novel thermostable (S)-enantioselective omega-transaminase from Thermomicrobium roseum.
Sci Rep, 9:6958-6958, 2019

PubMed Abstract: Transaminases catalyze the reversible transfer reaction of an amino group between a primary amine and an α-keto acid, utilizing pyridoxal 5'-phosphate as a cofactor. ω-transaminases (ωTAs) recognize an amino group linked to a non-α carbon of amine substrates. Recently, a novel (S)-enantioselective ωTA from Thermomicrobium roseum (Tr-ωTA) 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-ωTA at 1.8 Å resolution to elucidate the mechanism underlying Tr-ωTA substrate (S)-enantioselectivity. A structural analysis of Tr-ωTA 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-ωTA. The present study thus provides structural and functional insights into the (S)-enantioselectivity of Tr-ωTA.

PubMed: 31061438
DOI: 10.1038/s41598-019-43490-2

Experimental method

X-RAY DIFFRACTION (1.803 Å)