Transient kinetic experiments demonstrate the existence of a unique catalytic enzyme form in the peptide-stimulated ATPase mechanism of Escherichia coli Lon protease

Biochemistry

Volumn 45, Issue 38, 2006, Pages 11432-11443

  Vineyard, Diana ^a   Zhang, Xuemei ^a   Lee, Irene ^a  

^a CASE WESTERN RESERVE UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINETRIPHOSPHATE; CATALYSIS; CATALYST ACTIVITY; CONFORMATIONS; ENZYME KINETICS; ESCHERICHIA COLI; HYDROLYSIS;

ATPASE; KINETIC MODEL; TRANSIENT KINETICS;

ENZYMES;

ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATASE; BACTERIAL ENZYME; CASEIN; ENDOPEPTIDASE LA; PEPTIDE DERIVATIVE;

ARTICLE; CATALYSIS; CONFORMATIONAL TRANSITION; ENZYME ACTIVITY; ENZYME ANALYSIS; ENZYME BINDING; ENZYME CONFORMATION; ENZYME KINETICS; ENZYME MECHANISM; ENZYME STRUCTURE; ENZYME SUBSTRATE; ESCHERICHIA COLI; NONHUMAN; PRIORITY JOURNAL; STEADY STATE; STRUCTURE ANALYSIS;

ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATASES; ADENOSINE TRIPHOSPHATE; ANTHRANILIC ACIDS; CATALYSIS; ESCHERICHIA COLI; FLUORESCENCE; HYDROLYSIS; KINETICS; PEPTIDES; PROTEASE LA; PROTEIN BINDING; PROTEIN CONFORMATION; TRYPSIN;

ESCHERICHIA COLI;

EID: 33749013872     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi060809+     Document Type: Article

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