Allosteric effects of carbamoyl phosphate synthetase from Escherichia coli are entropy-driven

Biochemistry

Volumn 35, Issue 36, 1996, Pages 11918-11924

  Braxton, B L ^a   Mullins, Leisha S ^b   Raushel, Frank M ^b   Reinhart, Gregory D ^b  

^a UNIVERSITY OF WISCONSIN LA CROSSE   (United States)

^b TEXAS A AND M UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATE MAGNESIUM; BACTERIAL ENZYME; CARBAMOYL PHOSPHATE SYNTHASE;

ALLOSTERISM; ARTICLE; BINDING AFFINITY; ENTROPY; ENZYME ACTIVITY; ESCHERICHIA COLI; NONHUMAN; PRIORITY JOURNAL; TEMPERATURE SENSITIVITY; THERMODYNAMICS;

ADENOSINE DIPHOSPHATE; ALLOSTERIC REGULATION; ALLOSTERIC SITE; CARBAMOYL-PHOSPHATE SYNTHASE (GLUTAMINE-HYDROLYZING); ENZYME ACTIVATION; ESCHERICHIA COLI; INOSINE MONOPHOSPHATE; KINETICS; LIGANDS; ORNITHINE; PROTEIN BINDING; TEMPERATURE; THERMODYNAMICS; URIDINE MONOPHOSPHATE;

EID: 0029808058     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi961305m     Document Type: Article

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