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Volumn 71, Issue 1, 2008, Pages 16-23
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Cysteine 10 is critical for the activity of Ochrobactrum anthropi glutathione transferase and its mutation to alanine causes the preferential binding of glutathione to the H-site
a
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Author keywords
Bacterial GST; G site; H site; Ochrobactrum anthropi; Stability
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Indexed keywords
ALANINE;
BACTERIAL ENZYME;
CYSTEINE;
GLUTATHIONE;
GLUTATHIONE TRANSFERASE;
THIOTRANSFERASE;
UNCLASSIFIED DRUG;
AMINO ACID SEQUENCE;
AMINO ACID SUBSTITUTION;
ARTICLE;
BINDING SITE;
CRYSTALLIZATION;
ENZYME ACTIVITY;
ENZYME ANALYSIS;
ENZYME BINDING;
ENZYME STABILITY;
ENZYME SUBSTRATE;
HYDROPHOBICITY;
MUTATION;
NUCLEOTIDE SEQUENCE;
OCHROBACTRUM ANTHROPI;
PRIORITY JOURNAL;
PROTEIN BINDING;
PROTEIN FUNCTION;
SITE DIRECTED MUTAGENESIS;
STRUCTURE ANALYSIS;
THERMOSTABILITY;
ALANINE;
BACTERIAL PROTEINS;
BINDING SITES;
CYSTEINE;
GLUTATHIONE;
GLUTATHIONE TRANSFERASE;
MUTATION, MISSENSE;
OCHROBACTRUM ANTHROPI;
BACTERIA (MICROORGANISMS);
OCHROBACTRUM ANTHROPI;
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EID: 40549133470
PISSN: 08873585
EISSN: 10970134
Source Type: Journal
DOI: 10.1002/prot.21835 Document Type: Article |
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Times cited : (16)
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References (30)
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