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Volumn 41, Issue 6, 2002, Pages 1717-1723
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Arg362 and tyr365 of the botulinum neurotoxin type a light chain are involved in transition state stabilization
a
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Author keywords
[No Author keywords available]
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Indexed keywords
LIGHT CHAIN(LC);
CATALYSIS;
CRYSTALS;
GROUND STATE;
HYDROLYSIS;
LIQUID CHROMATOGRAPHY;
MUTAGENESIS;
X RAYS;
ZINC;
BOTULINUM TOXIN;
GLUZINCIN;
METALLOPROTEINASE;
PROTEINASE;
RECOMBINANT PROTEIN;
SYNAPTOBREVIN;
THERMOLYSIN;
UNCLASSIFIED DRUG;
ZINC ION;
AMINO ACID SEQUENCE;
AMINO ACID SUBSTITUTION;
ARTICLE;
BINDING AFFINITY;
CRYSTAL STRUCTURE;
ENZYME ACTIVE SITE;
ENZYME ACTIVITY;
ENZYME KINETICS;
HYDROLYSIS;
MOLECULAR MODEL;
PRIORITY JOURNAL;
PROTEIN ANALYSIS;
PROTEIN DENATURATION;
PROTEIN SECONDARY STRUCTURE;
PROTEIN STABILITY;
PROTEIN STRUCTURE;
PROTON TRANSPORT;
SITE DIRECTED MUTAGENESIS;
STRUCTURE ANALYSIS;
X RAY CRYSTALLOGRAPHY;
AMINO ACID MOTIFS;
ARGININE;
BASE SEQUENCE;
BINDING SITES;
BOTULINUM TOXIN TYPE A;
CIRCULAR DICHROISM;
DRUG STABILITY;
HYDROLYSIS;
KINETICS;
MEMBRANE PROTEINS;
MODELS, MOLECULAR;
MUTAGENESIS, SITE-DIRECTED;
NERVE TISSUE PROTEINS;
PLASMIDS;
RECOMBINANT PROTEINS;
SYNAPTOSOMAL-ASSOCIATED PROTEIN 25;
TYROSINE;
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EID: 0037065664
PISSN: 00062960
EISSN: None
Source Type: Journal
DOI: 10.1021/bi0157969 Document Type: Article |
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Times cited : (95)
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References (29)
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