HslVU ATP-dependent protease utilizes maximally six among twelve threonine active sites during proteolysis

Journal of Biological Chemistry

Volumn 284, Issue 48, 2009, Pages 33475-33484

  Lee, Jung Wook ^a   Park, Eunyong ^a   Jeong, Min Sun ^a   Jeon, Young Joo ^a   Eom, Soo Hyun ^b   Seol, Jae Hong ^a   Chung, Chin Ha ^a  

^a Seoul National University   (South Korea)

^b Gwangju Institute of Science and Technology (GIST)   (South Korea)

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVE SITE; ACTIVE SITE RESIDUES; ATP HYDROLYSIS; ATP-ASE ACTIVITY; ATP-DEPENDENT PROTEASE; CATALYTIC ACTIVITY; N-TERMINALS; PROTEASOME INHIBITORS; PROTEASOMES; PROTEOLYTIC ACTIVITIES; RESTING STATE; SUBSTRATE-BOUND;

DEGRADATION; MATHEMATICAL MODELS; PROTEOLYSIS;

SUBSTRATES;

ADENOSINE TRIPHOSPHATE; ADENOSINE TRIPHOSPHATE DEPENDENT PROTEINASE; BACTERIAL ENZYME; PROTEASOME; PROTEASOME INHIBITOR; PROTEIN HSIVU; THREONINE; UNCLASSIFIED DRUG;

ARTICLE; CATALYSIS; CONTROLLED STUDY; ENZYME ACTIVATION; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME MECHANISM; ENZYME STABILITY; ENZYME SUBSTRATE; MATHEMATICAL MODEL; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN HYDROLYSIS; PROTEIN PROTEIN INTERACTION;

ADENOSINE TRIPHOSPHATE; ALANINE; AMINO ACID SUBSTITUTION; BINDING SITES; CATALYSIS; ELECTROPHORESIS, POLYACRYLAMIDE GEL; ENDOPEPTIDASE CLP; ENZYME ASSAYS; ESCHERICHIA COLI PROTEINS; HYDROLYSIS; KINETICS; MODELS, BIOLOGICAL; MUTATION; PEPTIDES; PROTEIN BINDING; PROTEIN SUBUNITS; SPECTROMETRY, FLUORESCENCE; SUBSTRATE SPECIFICITY; THREONINE;

BACTERIA (MICROORGANISMS); EUKARYOTA;

EID: 70450235042     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M109.045807     Document Type: Article

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