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

Keyphrases

• Structural Characterization 100%
• Functional Characterization 100%
• Psychrophilic Bacteria 100%
• S-formylglutathione Hydrolase 100%
• Cold-active 100%
• Shewanella Frigidimarina 100%
• Active Sites 60%
• Esterase 40%
• Catalytic Triad 40%
• Protein Engineering 40%
• Molecular Mass 20%
• Ethanol 20%
• Thiols 20%
• Enzymatic Activity 20%
• Amino Acids 20%
• Steric Effect 20%
• Short-chain Ester 20%
• Glutathione 20%
• Triton X-100 (TX-100) 20%
• P-nitrophenyl Acetate 20%
• Hexanoate 20%
• Urea 20%
• Activity Analysis 20%
• Butyrate 20%
• Binding Residues 20%
• Industrial Use 20%
• Industrial Application 20%
• Alkaline pH 20%
• Family Members 20%
• Optimum pH 20%
• Lipolytic Enzymes 20%
• Broad Substrate Specificity 20%
• Sequence Analysis 20%
• Structure Function 20%
• Formate 20%
• Substrate-binding Pocket 20%
• Substrate Binding 20%
• Engineering Strategies 20%
• Pentapeptide 20%
• Gatekeeper Residue 20%
• Octanoate 20%
• Esterase D 20%
• Site Configuration 20%

Biochemistry, Genetics and Molecular Biology

• Hydrolase 100%
• Shewanella 100%
• Psychrophilic Bacterium 100%
• Active Site 60%
• Catalytic Triad 40%
• Esterase 40%
• Protein Engineering 40%
• Enzyme 20%
• Molecular Weight 20%
• Amino Acids 20%
• Wild Type 20%
• Crystal Structure 20%
• Enzyme Activity 20%
• Enzyme Specificity 20%
• Protein Sequencing 20%
• Carboxylesterase 20%
• Butyrate 20%
• Caprylic Acid 20%
• Alkalinity 20%
• Thiol 20%
• Glutathione 20%
• Hexanoic Acid 20%