6IO1

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

6IO1 の概要

• エントリーDOI: 10.2210/pdb6io1/pdb
• 分子名称: Aminotransferase, class III, 4'-DEOXY-4'-AMINOPYRIDOXAL-5'-PHOSPHATE (3 entities in total)
• 機能のキーワード: enantioselectivity, omega-transaminase, substrate recognition thermomicrobium roseum, transamination, transferase
• 由来する生物種: Thermomicrobium roseum (strain ATCC 27502 / DSM 5159 / P-2)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 99295.48

構造登録者

Park, H.H.,Kwon, S. (登録日: 2018-10-29, 公開日: 2019-05-22, 最終更新日: 2023-11-22)

主引用文献

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

実験手法

X-RAY DIFFRACTION (1.803 Å)