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Volumn 430, Issue 2, 2004, Pages 185-190
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Kinetic studies and site-directed mutagenesis of Escherichia coli agmatinase. a role for Glu274 in binding and correct positioning of the substrate guanidinium group
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Author keywords
Agmatinase; E. coli; Glu274; Kinetic mechanism; Site directed mutagenesis
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Indexed keywords
AGMATINE;
AMINO ACID DERIVATIVE;
BACTERIAL ENZYME;
GUANIDINE;
HYDROLASE;
PUTRESCINE;
TRYPTOPHAN;
AMINO ACID SEQUENCE;
CATALYSIS;
CIRCULAR DICHROISM;
CONFERENCE PAPER;
CONTROLLED STUDY;
ENZYME BINDING;
ESCHERICHIA COLI;
LINEAR SYSTEM;
NONHUMAN;
PRIORITY JOURNAL;
SITE DIRECTED MUTAGENESIS;
STATISTICAL SIGNIFICANCE;
STRUCTURE ANALYSIS;
WILD TYPE;
BINDING SITES;
CATALYSIS;
ESCHERICHIA COLI;
GLUTAMINE;
GUANIDINE;
KINETICS;
MODELS, MOLECULAR;
MUTAGENESIS, SITE-DIRECTED;
MUTATION;
STRUCTURE-ACTIVITY RELATIONSHIP;
SUBSTRATE SPECIFICITY;
UREOHYDROLASES;
VARIATION (GENETICS);
ESCHERICHIA COLI;
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EID: 4444281756
PISSN: 00039861
EISSN: None
Source Type: Journal
DOI: 10.1016/j.abb.2004.07.005 Document Type: Conference Paper |
Times cited : (14)
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References (22)
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