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

• Main Authors: Lee, Chang, Wanki Yoo, Sun-Ha Park, Le, Ly, Chang-Sook Jeong, Ryu, Bum, Shin, Seung, Han-Woo Kim, Park, Hyun, Kim, Kyeong, T. Kim, Lee, Jun
• Format: Article in Journal/Newspaper
• Language: unknown
• Published: figshare 2019
• Subjects: Biophysics; Biochemistry; Microbiology; FOS Biological sciences; Genetics; 39999 Chemical Sciences not elsewhere classified; FOS Chemical sciences; Science Policy; Computational Biology; Antarctic; Triton; Antarc*
• Online Access: https://dx.doi.org/10.6084/m9.figshare.c.4634534.v1; https://springernature.figshare.com/collections/Structural_and_functional_characterization_of_a_novel_cold-active_S-formylglutathione_hydrolase_SfSFGH_homolog_from_Shewanella_frigidimarina_a_psychrophilic_bacterium/4634534/1

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...