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Volumn 7, Issue 4-5, 2002, Pages 490-499
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Three high-resolution crystal structures of cadmium-substituted carboxypeptidase a provide insight into the enzymatic function
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Author keywords
Cadmium substitution; Carboxypeptidase A; Reaction mechanism; Sequence alignment; Water flow
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Indexed keywords
CADMIUM;
CARBOXYPEPTIDASE A;
CHLORIDE;
ARTICLE;
BINDING SITE;
CATALYSIS;
CONCENTRATION RESPONSE;
CRYSTAL STRUCTURE;
ENZYME ACTIVITY;
IONIC STRENGTH;
NONHUMAN;
PH;
PRIORITY JOURNAL;
REACTION ANALYSIS;
SEQUENCE ANALYSIS;
STRUCTURE ANALYSIS;
X RAY DIFFRACTION;
AMINO ACID SEQUENCE;
CADMIUM;
CARBOXYPEPTIDASES;
CARBOXYPEPTIDASES A;
CATALYTIC DOMAIN;
CONSERVED SEQUENCE;
CRYSTALLOGRAPHY, X-RAY;
HYDROGEN-ION CONCENTRATION;
MODELS, MOLECULAR;
MOLECULAR SEQUENCE DATA;
OSMOLAR CONCENTRATION;
PROTEIN CONFORMATION;
ZINC;
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EID: 0036933841
PISSN: 09498257
EISSN: None
Source Type: Journal
DOI: 10.1007/s00775-001-0324-0 Document Type: Article |
Times cited : (12)
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References (38)
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