Apparent negative co-operativity and substrate inhibition in overexpressed glutamate dehydrogenase from Escherichia coli

FEMS Microbiology Letters

Volumn 281, Issue 2, 2008, Pages 132-139

  Sharkey, Michael A ^a   Engel, Paul C ^a  

^a UNIVERSITY COLLEGE DUBLIN   (Ireland)

Author keywords

Enzyme purification; Escherichia coli; Glutamate dehydrogenase; Negative co operativity; Overexpression; Substrate inhibition

Indexed keywords

2 OXOGLUTARIC ACID; AMMONIA; GLUTAMATE DEHYDROGENASE; GLUTAMIC ACID; NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE;

ARTICLE; CONTROLLED STUDY; DEAMINATION; ENZYME KINETICS; ENZYME SUBSTRATE COMPLEX; ESCHERICHIA COLI; MICHAELIS CONSTANT; NONHUMAN; OXIDATION; PH MEASUREMENT; PRIORITY JOURNAL; PROTEIN EXPRESSION; PROTEIN PURIFICATION; REDUCTION;

CLONING, MOLECULAR; COENZYMES; ENZYME STABILITY; ESCHERICHIA COLI; GLUTAMATE DEHYDROGENASE; HYDROGEN-ION CONCENTRATION; KINETICS; RECOMBINANT PROTEINS; SUBSTRATE SPECIFICITY;

ESCHERICHIA COLI;

EID: 41049099764     PISSN: 03781097     EISSN: 15746968     Source Type: Journal    
DOI: 10.1111/j.1574-6968.2008.01086.x     Document Type: Article

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