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Volumn 361, Issue 3, 2002, Pages 613-619
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S′2 substrate specificity and the role of His110 and his111 in the exopeptidase activity of human cathepsin B
a a a a a |
Author keywords
Cysteine protease; Dipeptidase; Enzyme kinetics; Occluding loop; Quenched fluorescence substrates
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Indexed keywords
ENZYMES;
FLUORESCENCE;
MUTAGENESIS;
QUENCHING;
PEPTIDES;
BIOCHEMICAL ENGINEERING;
AROMATIC COMPOUND;
ASPARTIC ACID;
CATHEPSIN B;
CYSTEINE PROTEINASE;
DIPEPTIDYL CARBOXYPEPTIDASE;
EXOPEPTIDASE;
GLUTAMIC ACID;
HISTIDINE;
AMIDASE;
CARBOXYTOLBUTAMIDE;
DRUG DERIVATIVE;
ION;
RECOMBINANT PROTEIN;
TOLBUTAMIDE;
ARTICLE;
CARBOXY TERMINAL SEQUENCE;
ELECTRICITY;
ENZYME ACTIVITY;
ENZYME SPECIFICITY;
FLUORESCENCE;
HUMAN;
LYSOSOME;
MOLECULAR INTERACTION;
PRIORITY JOURNAL;
SITE DIRECTED MUTAGENESIS;
BINDING SITE;
CHEMICAL STRUCTURE;
CHEMISTRY;
ENZYMOLOGY;
GENETICS;
KINETICS;
METABOLISM;
MUTATION;
PROTEIN BINDING;
PROTEIN TERTIARY STRUCTURE;
AMIDOHYDROLASES;
ASPARTIC ACID;
BINDING SITES;
CATHEPSIN B;
EXOPEPTIDASES;
GLUTAMIC ACID;
HISTIDINE;
HUMANS;
IONS;
KINETICS;
LYSOSOMES;
MODELS, MOLECULAR;
MUTAGENESIS, SITE-DIRECTED;
MUTATION;
PROTEIN BINDING;
PROTEIN STRUCTURE, TERTIARY;
RECOMBINANT PROTEINS;
SUBSTRATE SPECIFICITY;
TOLBUTAMIDE;
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EID: 0036462513
PISSN: 02646021
EISSN: None
Source Type: Journal
DOI: 10.1042/0264-6021:3610613 Document Type: Article |
Times cited : (67)
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References (46)
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