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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

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Saccharomyces cerevisiae expresses a 67.8 kDa homodimeric serine thioesterase, S-formylglutathione hydrolase (SFGH), that is 39.9% identical with human esterase D. ...
physiology genetics metabolism enzymology chemistry 
Cholinesterase Inhibitors Crystallography, X-Ray Paraoxon Protein Structure, Tertiary Saccharomyces cerevisiae Proteins Amino Acid Substitution Humans Thiolester Hydrolases Hydrolysis Saccharomyces cerevisiae Phosphorylation Binding Sites Carboxylesterase Sequence Homology, Amino Acid Drug Resistance, Fungal Mutation, Missense 
18707125  
10.1021/bi8010016  
15 (Last update: 05/23/2018 7:54:45pm)  
1PV1  
structure