The C-terminal domain of biotin protein ligase from E. coli is required for catalytic activity

Protein Science

Volumn 10, Issue 12, 2001, Pages 2608-2617

  Chapman Smith, Anne ^a   Mulhern, Terrence D ^b   Whelan, Fiona ^a   Cronan Jr , John E ^c   Wallace, John C ^a  

^a UNIVERSITY OF ADELAIDE   (Australia)

^b UNIVERSITY OF MELBOURNE   (Australia)

^c UNIVERSITY OF ILLINOIS AT URBANA CHAMPAIGN   (United States)

Author keywords

ATP binding; Biotin holoenzyme synthetase; Biotin protein ligase; Posttranslational modification; Protein protein interactions

Indexed keywords

ADENOSINE TRIPHOSPHATE; BACTERIAL ENZYME; BIOTIN; BIOTIN SYNTHASE; HOLOENZYME; LIGASE; MUTANT PROTEIN;

AMINO ACID SUBSTITUTION; ARTICLE; BINDING AFFINITY; BINDING SITE; CARBOXY TERMINAL SEQUENCE; CATALYSIS; ENZYME ACTIVITY; ENZYME KINETICS; ENZYME STRUCTURE; ESCHERICHIA COLI; NONHUMAN; PRIORITY JOURNAL; PROTEIN PROCESSING; PROTEIN PROTEIN INTERACTION; SITE DIRECTED MUTAGENESIS; STRUCTURE ACTIVITY RELATION;

ADENOSINE TRIPHOSPHATE; AMINO ACID MOTIFS; AMINO ACID SEQUENCE; BACTERIAL PROTEINS; BINDING SITES; BIOTIN; BIOTINYLATION; CARBON-NITROGEN LIGASES; CATALYSIS; CATALYTIC DOMAIN; DNA MUTATIONAL ANALYSIS; ELECTROPHORESIS, POLYACRYLAMIDE GEL; ESCHERICHIA COLI; ESCHERICHIA COLI PROTEINS; KINETICS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; MUTATION; PROTEIN CONFORMATION; PROTEIN STRUCTURE, TERTIARY; REPRESSOR PROTEINS; SEQUENCE HOMOLOGY, AMINO ACID; TIME FACTORS; TRANSCRIPTION FACTORS;

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI;

EID: 0035188539     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.ps.22401     Document Type: Article

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