Homotropic allosteric control in clostridial glutamate dehydrogenase: Different mechanisms for glutamate and NAD+?

FEBS Letters

Volumn 582, Issue 13, 2008, Pages 1816-1820

  Hamza, Muaawia A ^a   Engel, Paul C ^a  

^a UNIVERSITY COLLEGE DUBLIN   (Ireland)

Author keywords

Allosteric mechanism; Glutamate dehydrogenase; Hill coefficients; Homotropic interaction; Negative cooperativity; Site directed mutagenesis; Trp Phe mutants

Indexed keywords

GLUTAMATE DEHYDROGENASE; GLUTAMIC ACID; NICOTINAMIDE ADENINE DINUCLEOTIDE; PHENYLALANINE; TRYPSIN;

ALLOSTERISM; ARTICLE; COENZYME; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; MICHAELIS MENTEN KINETICS; NONHUMAN; PH MEASUREMENT; PRIORITY JOURNAL;

ALLOSTERIC REGULATION; BACTERIAL PROTEINS; CLOSTRIDIUM SYMBIOSUM; GLUTAMATE DEHYDROGENASE; GLUTAMATES; MUTATION; NAD; PHENYLALANINE; TRYPTOPHAN;

EID: 44449112803     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.febslet.2008.04.049     Document Type: Article

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