Detailed Information

Cited 0 time in webofscience Cited 0 time in scopus
Metadata Downloads

Structural basis for the substrate specificity of an S-formylglutathione hydrolase derived from Variovorax sp. PAMC 28711

Authors
Hwang, J.Kim, B.Lee, M.J.Nam, Y.Youn, U.J.Lee, C.S.Oh, T.-J.Park, H.H.Do, H.Lee, J.H.
Issue Date
Nov-2022
Publisher
Elsevier B.V.
Keywords
Crystal structure; S-Formylglutathione hydrolase; Substrate specificity; Variovorax sp. PAMC 28711; X-ray crystallography
Citation
Biochemical and Biophysical Research Communications, v.629, pp 159 - 164
Pages
6
Journal Title
Biochemical and Biophysical Research Communications
Volume
629
Start Page
159
End Page
164
URI
https://scholarworks.bwise.kr/cau/handle/2019.sw.cau/59102
DOI
10.1016/j.bbrc.2022.09.008
ISSN
0006-291X
1090-2104
Abstract
S-Formylglutathione hydrolase was originally known to catalyze the hydrolysis of S-formylglutathione to formate and glutathione. However, this enzyme has a broader esterase activity toward substrates containing thioester and ester bonds. In a previous study, we identified a new S-formylglutathione hydrolase (VaSFGH) gene in the Antarctic bacterium Variovorax sp. PAMC 28711, and recombinant VaSFGH protein was purified and characterized. Previous enzyme activity assays showed that VaSFGH has high activity, especially toward short-chain p-nitrophenyl esters (C2–C4). In this study, we determined the crystal structure of substrate-free VaSFGH at a resolution of 2.38 Å. In addition, p-nitrophenyl ester-bound VaSFGH structure models were generated by molecular docking simulations to obtain structural evidence of its substrate specificity. Comparative structural analysis of the apo-form and p-nitrophenyl ester-bound VaSFGH model structures revealed that large substrates could not bind inside the hydrophobic substrate-binding pocket because of the intrinsically static and relatively small substrate-binding pocket size of VaSFGH. This study provides useful information for further protein engineering of SFGHs for industrial use. © 2022 Elsevier Inc.
Files in This Item
There are no files associated with this item.
Appears in
Collections
ETC > 1. Journal Articles

qrcode

Items in ScholarWorks are protected by copyright, with all rights reserved, unless otherwise indicated.

Related Researcher

Researcher Park, Hyun Ho photo

Park, Hyun Ho
대학원 (글로벌혁신신약학과)
Read more

Altmetrics

Total Views & Downloads

BROWSE