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

• Published in: Microbial Cell Factories
• Main Authors: Lee, Chang Woo, Yoo, Wanki, Park, Sun-Ha, Le, Ly Thi Huong Luu, Jeong, Chang-Sook, Ryu, Bum Han, Shin, Seung Chul, Kim, Han-Woo, Park, Hyun, Kim, Kyeong Kyu, Kim, T. Doohun, Lee, Jun Hyuck
• Format: Text
• Language: English
• Published: BioMed Central 2019
• Subjects: Research; Antarctic; Triton; Antarc*
• Online Access: http://www.ncbi.nlm.nih.gov/pmc/articles/PMC6699074/; http://www.ncbi.nlm.nih.gov/pubmed/31426813; https://doi.org/10.1186/s12934-019-1190-1

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 triad at th...