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Structural basis of substrate recognition by a novel thermostable (S)-enantioselective omega-transaminase from Thermomicrobium roseum

Cited 2 time in wos
Cited 2 time in scopus
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Title
Structural basis of substrate recognition by a novel thermostable (S)-enantioselective omega-transaminase from Thermomicrobium roseum
Other Titles
호열성 박테리아 (Thermomicrobium roseum) 유래의 transaminase 효소의 구조기반 활성 기작 규명
Authors
Kwon, Sunghark
Lee, Jun Hyuck
Kim, Chang Min
Jang, Hyunseok
Yun, Hyungdon
Jeon, Ju-Hong
So, Insuk
Park, Hyun Ho
Subject
Science & Technology - Other Topics
Issue Date
2019-05
Citation
Sunghark Kwon, et al. 2019. "Structural basis of substrate recognition by a novel thermostable (S)-enantioselective omega-transaminase from Thermomicrobium roseum". SCIENTIFIC REPORTS, 9(6958): 1-12.
Abstract
Transaminases 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 (omega TAs) recognize an amino group linked to a non-alpha carbon of amine substrates. Recently, a novel (S)-enantioselective omega TA from Thermomicrobium roseum (Tr-omega TA) 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-omega TA at 1.8 angstrom resolution to elucidate the mechanism underlying Tr-omega TA substrate (S)-enantioselectivity. A structural analysis of Tr-omega TA 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-omega TA. The present study thus provides structural and functional insights into the (S)-enantioselectivity of Tr-omega TA.
URI
https://repository.kopri.re.kr/handle/201206/10906
DOI
http://dx.doi.org/10.1038/s41598-019-43490-2
Appears in Collections  
2019-2019, Development of potential candidates as antibiotics based on polar genetic resources (19-19) / Lee, Jun Hyuck (PE19210)
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