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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. ...
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 
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