Structural and functional characterization of a novel cold-active S-formylglutathione hydrolase (SfSFGH) homolog from Shewanella frigidimarina, a psychrophilic bacterium

Structural and functional characterization of a novel cold-active S-formylglutathione hydrolase (SfSFGH) homolog from Shewanella frigidimarina, a psychrophilic bacterium

Abstract Background S-Formylglutathione is hydrolyzed to glutathione and formate by an S-formylglutathione hydrolase (SFGH) (3.1.2.12). This thiol esterase belongs to the esterase family and is also known as esterase D. SFGHs contain highly conserved active residues of Ser-Asp-His as a catalytic tri...

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Main Authors: Chang Woo Lee, Wanki Yoo, Sun-Ha Park, Ly Thi Huong Luu Le, Chang-Sook Jeong, Bum Han Ryu, Seung Chul Shin, Han-Woo Kim, Hyun Park, Kyeong Kyu Kim, T. Doohun Kim, Jun Hyuck Lee
Format: Article
Language:English
Published: BMC 2019-08-01
Series:Microbial Cell Factories
Subjects:
Crystal structure
S-Formylglutathione hydrolase
Substrate specificity
Shewanella frigidimarina
Mutagenesis
Online Access:http://link.springer.com/article/10.1186/s12934-019-1190-1

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http://link.springer.com/article/10.1186/s12934-019-1190-1

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