View publication

Structural characterization and reversal of the natural organophosphate resistance of a D-type esterase, Saccharomyces cerevisiae S-formylglutathione hydrolase.

Legler PM, Kumaran D, Swaminathan S, Studier FW, Millard CB,
Biochemistry (2008) 47:9592-601 PublishedPSI:Phase 2  
New York Structural Genomics Research Consortium

(click to unfold)
Saccharomyces cerevisiae expresses a 67.8 kDa homodimeric serine thioesterase, S-formylglutathione hydrolase (SFGH), that is 39.9% identical with human esterase D. ...
metabolism chemistry genetics enzymology physiology 
Binding Sites Crystallography, X-Ray Humans Protein Structure, Tertiary Sequence Homology, Amino Acid Phosphorylation Hydrolysis Amino Acid Substitution Saccharomyces cerevisiae Proteins Saccharomyces cerevisiae Mutation, Missense Carboxylesterase Cholinesterase Inhibitors Drug Resistance, Fungal Paraoxon Thiolester Hydrolases 
18707125  
10.1021/bi8010016  
15 (Last update: 10/13/2018 5:43:22pm)  
1PV1  
structure