Three of the six possible intersubunit stabilizing interactions involving Glu-239 are sufficient for restoration of the homotropic and heterotropic properties of Escherichia coli aspartate transcarbamoylase

Journal of Biological Chemistry

Volumn 275, Issue 2, 2000, Pages 752-758

  Sakash, Jessica B ^a   Chan, Robin S ^a   Tsuruta, Hiro ^b   Kantrowitz, Evan R ^a  

^a BOSTON COLLEGE   (United States)

^b SLAC NATIONAL ACCELERATOR LABORATORY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ASPARTATE CARBAMOYLTRANSFERASE; GLUTAMIC ACID; HOLOENZYME;

ALLOSTERISM; ANION EXCHANGE CHROMATOGRAPHY; ARTICLE; ENZYME ANALYSIS; ENZYME ISOLATION; ENZYME STABILITY; ENZYME SUBUNIT; ESCHERICHIA COLI; MOLECULAR INTERACTION; NONHUMAN; PRIORITY JOURNAL;

ADENOSINE TRIPHOSPHATE; AMINO ACID SUBSTITUTION; ASPARTATE CARBAMOYLTRANSFERASE; CATALYTIC DOMAIN; CYTIDINE TRIPHOSPHATE; ENZYME STABILITY; ESCHERICHIA COLI; GLUTAMIC ACID; KINETICS; MACROMOLECULAR SUBSTANCES; MODELS, MOLECULAR; MUTAGENESIS, SITE-DIRECTED; PROTEIN HYBRIDIZATION; PROTEIN STRUCTURE, QUATERNARY; PROTEIN STRUCTURE, SECONDARY; RECOMBINANT PROTEINS; X-RAY DIFFRACTION;

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI; NEGIBACTERIA;

EID: 0033978887     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.275.2.752     Document Type: Article

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