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Volumn 48, Issue 3, 2009, Pages 511-513
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In vitro kinetic analysis of substrate specificity in enterobactin biosynthetic lower pathway enzymes provides insight into the biochemical function of the hot dog-fold thioesterase EntH
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Author keywords
[No Author keywords available]
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Indexed keywords
BIOCHEMICAL FUNCTIONS;
DIHYDROXYBENZOATE;
ENTEROBACTIN;
IN-VITRO;
KINETIC ANALYSIS;
L SERINES;
NONRIBOSOMAL PEPTIDE SYNTHETASES;
SIDEROPHORE;
SUBSTRATE SPECIFICITIES;
THIOESTERASE;
AMINES;
ESCHERICHIA COLI;
AMINO ACIDS;
2,3 DIHYDROXYBENZOIC ACID;
ENTEROCHELIN;
PEPTIDE SYNTHASE;
PROTEIN ENTB;
PROTEIN ENTF;
PROTEIN ENTH;
SERINE;
THIOL ESTER HYDROLASE;
UNCLASSIFIED DRUG;
2,4-DIHYDROXYBENZOPHENONE;
ACYL COENZYME A;
BENZOPHENONE DERIVATIVE;
BENZORESORCINOL;
ESCHERICHIA COLI PROTEIN;
HOLOENZYME;
YBDB PROTEIN, E COLI;
ACYLATION;
ARTICLE;
ENZYME ACTIVITY;
ENZYME KINETICS;
ENZYME SPECIFICITY;
ESCHERICHIA COLI;
IN VITRO STUDY;
NONHUMAN;
PRIORITY JOURNAL;
PROTEIN ASSEMBLY;
BIOSYNTHESIS;
CATALYSIS;
CHEMISTRY;
ELECTROSPRAY MASS SPECTROMETRY;
ENZYMOLOGY;
HYDROLYSIS;
KINETICS;
METABOLISM;
PH;
PROTEIN SECONDARY STRUCTURE;
TEMPERATURE;
TIME;
CANIS FAMILIARIS;
ESCHERICHIA COLI;
ACYL COENZYME A;
BENZOPHENONES;
CATALYSIS;
ENTEROBACTIN;
ESCHERICHIA COLI;
ESCHERICHIA COLI PROTEINS;
HOLOENZYMES;
HYDROGEN-ION CONCENTRATION;
HYDROLYSIS;
KINETICS;
PROTEIN STRUCTURE, SECONDARY;
SPECTROMETRY, MASS, ELECTROSPRAY IONIZATION;
SUBSTRATE SPECIFICITY;
TEMPERATURE;
THIOLESTER HYDROLASES;
TIME FACTORS;
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EID: 59249107241
PISSN: 00062960
EISSN: None
Source Type: Journal
DOI: 10.1021/bi802207t Document Type: Article |
Times cited : (22)
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References (9)
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