Mutational analysis of conserved glycine residues 142, 143 and 146 reveals Gly142 is critical for tetramerization of CTP synthase from Escherichia coli

Biochemical Journal

Volumn 412, Issue 1, 2008, Pages 113-121

  Lunn, Faylene A ^a   MacLeod, Travis J ^a   Bearne, Stephen L ^a  

^a DALHOUSIE UNIVERSITY   (Canada)

Author keywords

Amidotransferase; CTP; Glycine; Mutagenesis; Proteolysis; Synthase; Tetramerization; UTP

Indexed keywords

ADENOSINETRIPHOSPHATE; ENZYME ACTIVITY; ESCHERICHIA COLI; MUTAGENESIS; OLIGOMERIZATION;

CYTOTOXIC PYRIMIDINE; MUTATIONAL ANALYSIS; TETRAMERIZATION;

AMINO ACIDS;

CYTIDINE TRIPHOSPHATE SYNTHASE; GLUTAMINASE; GLYCINE;

ARTICLE; BINDING AFFINITY; BINDING SITE; ENZYME ACTIVITY; ESCHERICHIA COLI; GEL FILTRATION; HIGH PERFORMANCE LIQUID CHROMATOGRAPHY; HYDROLYSIS; KINETICS; MUTAGENESIS; MUTATIONAL ANALYSIS; NONHUMAN; OLIGOMERIZATION; PRIORITY JOURNAL; SPECTROSCOPY;

ALANINE; AMINO ACID SUBSTITUTION; AMMONIA; CARBON-NITROGEN LIGASES; CONSERVED SEQUENCE; CYTIDINE TRIPHOSPHATE; DIMERIZATION; DNA MUTATIONAL ANALYSIS; ESCHERICHIA COLI; GLYCINE; KINETICS; MODELS, MOLECULAR; MUTAGENESIS, SITE-DIRECTED; MUTANT PROTEINS;

ESCHERICHIA COLI;

EID: 43549117268     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/BJ20071163     Document Type: Article

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