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Volumn 184, Issue 19, 2002, Pages 5376-5384
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Purification, substrate range, and metal center of AtzC: The N-isopropylammelide aminohydrolase involved in bacterial atrazine metabolism
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Author keywords
[No Author keywords available]
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Indexed keywords
AMINE;
ATRAZINE;
BACTERIAL PROTEIN;
BENZENE DERIVATIVE;
COBALT;
CYANURIC ACID;
FERROUS ION;
GENE PRODUCT;
HERBICIDE;
HYDROLASE;
ISOPROPYLAMINE;
MANGANESE;
METAL ION;
N ISOPROPYLAMMELIDE AMINOHYDROLASE;
NICKEL;
PROTEIN ATZC;
TRIAZINE;
UNCLASSIFIED DRUG;
ZINC ION;
ABSORPTION;
ANIMAL CELL;
ARTICLE;
ATZC GENE;
BACTERIAL METABOLISM;
CATALYSIS;
COLUMN CHROMATOGRAPHY;
COMPETITIVE INHIBITION;
ELECTRON SPIN RESONANCE;
ENZYME ACTIVE SITE;
ENZYME DEGRADATION;
ENZYME SPECIFICITY;
ENZYME SUBSTRATE;
ENZYME SUBUNIT;
ESCHERICHIA COLI;
HYDROLYSIS;
METAL BINDING;
MOLECULAR CLONING;
MOLECULAR WEIGHT;
NONHUMAN;
PRECIPITATION;
PRIORITY JOURNAL;
PROMOTER REGION;
PROTEIN EXPRESSION;
PROTEIN PURIFICATION;
PSEUDOMONAS;
STOICHIOMETRY;
STRAIN IDENTIFICATION;
TAC GENE;
AMIDOHYDROLASES;
AMINO ACID SEQUENCE;
AMINOHYDROLASES;
ATRAZINE;
BACTERIAL PROTEINS;
BINDING SITES;
ELECTRON SPIN RESONANCE SPECTROSCOPY;
KINETICS;
MOLECULAR SEQUENCE DATA;
PSEUDOMONAS;
SEQUENCE ALIGNMENT;
SPECTRUM ANALYSIS;
SUBSTRATE SPECIFICITY;
ZINC;
ANIMALIA;
BACTERIA (MICROORGANISMS);
ESCHERICHIA COLI;
NEGIBACTERIA;
PROKARYOTA;
PSEUDOMONAS;
PSEUDOMONAS SP.;
PSEUDOMONAS SP. ADP;
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EID: 0036776761
PISSN: 00219193
EISSN: None
Source Type: Journal
DOI: 10.1128/JB.184.19.5376-5384.2002 Document Type: Article |
Times cited : (49)
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References (52)
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