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Volumn 41, Issue 30, 2002, Pages 9418-9425
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Kinetic characterization of the peptidase activity of Escherichia coli Lon reveals the mechanistic similarities in ATP-dependent hydrolysis of peptide and protein substrates
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Author keywords
[No Author keywords available]
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Indexed keywords
ISOMECHANISM;
ADENOSINETRIPHOSPHATE;
BIODEGRADATION;
CATALYSIS;
DATA REDUCTION;
ENZYME INHIBITION;
ESCHERICHIA COLI;
HYDROLYSIS;
POLYPEPTIDES;
BIOCHEMISTRY;
ADENOSINE DIPHOSPHATE;
ADENOSINE TRIPHOSPHATE;
ADENOSINE TRIPHOSPHATE DERIVATIVE;
ENDOPEPTIDASE LA;
PEPTIDASE;
PROTEIN;
SERINE PROTEINASE;
UNCLASSIFIED DRUG;
ARTICLE;
CHEMICAL REACTION;
COMPETITIVE INHIBITION;
ENZYME ACTIVITY;
ENZYME KINETICS;
ENZYME MECHANISM;
ENZYME SUBSTRATE;
ESCHERICHIA COLI;
HYDROLYSIS;
NONHUMAN;
PRIORITY JOURNAL;
PROTEIN DEGRADATION;
STEADY STATE;
ADENOSINE DIPHOSPHATE;
ADENOSINE TRIPHOSPHATE;
ATP-DEPENDENT PROTEASES;
CATALYSIS;
ESCHERICHIA COLI PROTEINS;
HEAT-SHOCK PROTEINS;
HYDROLYSIS;
KINETICS;
PEPTIDES;
PROTEASE LA;
PROTEINS;
SERINE ENDOPEPTIDASES;
SUBSTRATE SPECIFICITY;
BACTERIA (MICROORGANISMS);
ESCHERICHIA COLI;
NEGIBACTERIA;
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EID: 0037199423
PISSN: 00062960
EISSN: None
Source Type: Journal
DOI: 10.1021/bi0255470 Document Type: Article |
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Times cited : (39)
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References (30)
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