The active site cysteine of ubiquitin-conjugating enzymes has a significantly elevated pKa: Functional implications

Biochemistry

Volumn 44, Issue 50, 2005, Pages 16385-16391

  Tolbert, Blanton S ^a   Tajc, Stephen G ^a   Webb, Helen ^b   Snyder, Jessica ^a   Nielsen, Jens E ^b   Miller, Benjamin L ^a   Basavappa, Ravi ^a  

^a UNIVERSITY OF ROCHESTER SCHOOL OF MEDICINE AND DENTISTRY   (United States)

^b UNIVERSITY COLLEGE DUBLIN   (Ireland)

Author keywords

[No Author keywords available]

Indexed keywords

ELECTROSTATICS; ENZYMES; ESTERS; MOLECULAR STRUCTURE; PROTEINS;

CYSTEINE; PROTEIN CHEMISTRY; TARGET PROTEIN; UBIQUITIN-CONJUGATING ENZYMES;

AMINO ACIDS;

CYSTEINE; PROTEIN; THIOESTER; UBIQUITIN; UBIQUITIN CONJUGATING ENZYME;

AFFINITY CHROMATOGRAPHY; ARTICLE; CARBOXY TERMINAL SEQUENCE; ENZYME ACTIVE SITE; HUMAN; HUMAN CELL; ISOTHERMAL TITRATION CALORIMETRY; LIGHT ABSORPTION; PH; PKA; POLYACRYLAMIDE GEL ELECTROPHORESIS; PRIORITY JOURNAL; UBIQUITINATION;

AMINO ACID SEQUENCE; BINDING SITES; CALORIMETRY; CYSTEINE; HYDROGEN-ION CONCENTRATION; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PROTEIN CONFORMATION; SEQUENCE HOMOLOGY, AMINO ACID; UBIQUITIN-CONJUGATING ENZYMES;

EID: 29244464347     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi0514459     Document Type: Article

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