Utilization of positional isotope exchange experiments to evaluate reversibility of ATP hydrolysis catalyzed by Escherichia coli Lon protease

Biochemistry and Cell Biology

Volumn 88, Issue 1, 2010, Pages 119-128

  Thomas, Jennifer ^a   Fishovitz, Jennifer ^b   Lee, Irene ^b  

^a WIL RESEARCH LABORATORIES   (United States)

^b CASE WESTERN RESERVE UNIVERSITY   (United States)

Author keywords

Lon protease; Positional isotope exchange; Reversibility of ATP hydrolysis

Indexed keywords

ATP HYDROLYSIS; ATP-ASE ACTIVITY; ATPASE DOMAIN; ATPASE REACTION; E. COLI; EXPERIMENTAL DATA; INORGANIC PHOSPHATES; ISOTOPE EXCHANGE; KINETIC CHARACTERIZATION; KINETIC MECHANISM; LON PROTEASE; NON-CATALYTIC; O INCORPORATION; PEPTIDASE ACTIVITY; PEPTIDE SUBSTRATES; PROTEIN DEGRADATION; PROTEIN FAMILY; REACTIVITY MODELS; SEQUENCE ALIGNMENTS; SERINE PROTEASE;

ADENOSINETRIPHOSPHATE; AMINO ACIDS; ENZYMES; ESCHERICHIA COLI; HYDROLYSIS; ISOTOPES; PEPTIDES; PHOSPHATASES; SUBSTRATES;

ENZYME ACTIVITY;

ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATASE; BUFFER; ENDOPEPTIDASE LA; ISOTOPE; OXYGEN 18; SERINE PROTEINASE;

BINDING AFFINITY; CHEMICAL REACTION; CONFERENCE PAPER; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME KINETICS; ENZYME SUBSTRATE COMPLEX; ESCHERICHIA COLI; HYDROLYSIS; MASS FRAGMENTOGRAPHY; NONHUMAN; PROTEIN DEGRADATION; PROTEIN HYDROLYSIS; PROTEIN STRUCTURE; SEQUENCE ANALYSIS;

ADENOSINE TRIPHOSPHATASES; ATP-DEPENDENT PROTEASES; ESCHERICHIA COLI; HYDROLYSIS; MODELS, CHEMICAL; PROTEASE LA;

ESCHERICHIA COLI;

EID: 75349083085     PISSN: 08298211     EISSN: 12086002     Source Type: Journal    
DOI: 10.1139/O09-117     Document Type: Conference Paper

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