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Volumn 39, Issue 34, 2000, Pages 10385-10396
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The crystal structure of Bacillus cereus phosphonoacetaldehyde hydrolase: Insight into catalysis of phosphorus bond cleavage and catalytic diversification within the had enzyme superfamily
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Author keywords
[No Author keywords available]
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Indexed keywords
ACETALDEHYDE;
BACTERIAL ENZYME;
CARBONYL DERIVATIVE;
LYSINE;
MAGNESIUM ION;
PHOSPHATASE;
PHOSPHATE;
PHOSPHONOACETALDEHYDE HYDROLASE;
TRYPTAMINE;
TYROSINE;
UNCLASSIFIED DRUG;
ARTICLE;
BACILLUS CEREUS;
CATALYSIS;
CONTROLLED STUDY;
ENZYME ACTIVE SITE;
ENZYME ACTIVITY;
ENZYME DEGRADATION;
HYDROGEN BOND;
HYDROLYSIS;
NONHUMAN;
NUCLEOTIDE SEQUENCE;
PRIORITY JOURNAL;
PROTEIN BINDING;
PROTEIN DOMAIN;
AMINO ACID SEQUENCE;
BACILLUS CEREUS;
CATALYSIS;
CATALYTIC DOMAIN;
CONSERVED SEQUENCE;
CRYSTALLOGRAPHY, X-RAY;
ELECTROSTATICS;
ENZYME INHIBITORS;
HYDROLASES;
MODELS, MOLECULAR;
MOLECULAR SEQUENCE DATA;
MUTAGENESIS, SITE-DIRECTED;
PROTEIN STRUCTURE, QUATERNARY;
PROTEIN STRUCTURE, TERTIARY;
RECOMBINANT PROTEINS;
SEQUENCE HOMOLOGY, AMINO ACID;
TUNGSTEN COMPOUNDS;
BACILLUS CEREUS;
BACTERIA (MICROORGANISMS);
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EID: 0034730072
PISSN: 00062960
EISSN: None
Source Type: Journal
DOI: 10.1021/bi001171j Document Type: Article |
Times cited : (134)
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References (54)
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