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Volumn 268, Issue 14, 2001, Pages 3950-3957
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The conserved Asn49 of maize glutathione S-transferase I modulates substrate binding, catalysis and intersubunit communication
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Author keywords
Cooperativity; Glutathione S transferase; Herbicide detoxification; Protein engineering
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Indexed keywords
1 CHLORO 2,4 DINITROBENZENE;
1 HYDROXYL 2,4 DINITROBENZENE;
ALANINE;
AMINO ACID;
ASPARAGINE;
BENZENE DERIVATIVE;
ENZYME;
GLUTATHIONE;
GLUTATHIONE TRANSFERASE;
MONOMER;
PHENYLALANINE;
TRYPSIN;
UNCLASSIFIED DRUG;
ALPHA HELIX;
AMINO ACID SUBSTITUTION;
AMINO TERMINAL SEQUENCE;
ARTICLE;
BINDING SITE;
CATALYSIS;
CONTROLLED STUDY;
ENZYME SUBSTRATE COMPLEX;
ENZYME SUBUNIT;
HYDROGEN BOND;
KINETICS;
MAIZE;
NONHUMAN;
PRIORITY JOURNAL;
PROTEIN DEGRADATION;
PROTEIN INTERACTION;
PROTEIN STRUCTURE;
SITE DIRECTED MUTAGENESIS;
THERMOSTABILITY;
ULTRAVIOLET SPECTROSCOPY;
VISCOSITY;
ALANINE;
AMINO ACID SEQUENCE;
ASPARAGINE;
CATALYSIS;
CONSERVED SEQUENCE;
ENZYME STABILITY;
GLUTATHIONE TRANSFERASE;
HEAT;
HERBICIDES;
KINETICS;
MODELS, MOLECULAR;
MUTAGENESIS, SITE-DIRECTED;
PLANT PROTEINS;
PROTEIN SUBUNITS;
SUBSTRATE SPECIFICITY;
TRYPSIN;
VISCOSITY;
ZEA MAYS;
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EID: 0034832887
PISSN: 00142956
EISSN: None
Source Type: Journal
DOI: 10.1046/j.1432-1327.2001.02307.x Document Type: Article |
Times cited : (27)
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References (45)
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