Kinetic behaviour of NADP-glutamate dehydrogenase from an extreme halophile Haloferax mediterranei in halophilic conditions (3 M KCL) and in glycerol

Biocatalysis and Biotransformation

Volumn 19, Issue 3, 2001, Pages 235-249

  Ferrer, J ^a   Pire, C ^a   Bonete, M J ^a  

^a UNIVERSITY OF ALICANTE   (Spain)

Author keywords

Haloferax mediterranei; Halophilic enzyme; Kinetic mechanism; NADP glutamate dehydrogenase

Indexed keywords

AMINATION; BIOREACTORS; ENZYME INHIBITION; GLYCEROL; SODIUM CHLORIDE; SUBSTRATES;

HALOPHILIC CONDITIONS;

ENZYME KINETICS;

2 OXOGLUTARIC ACID; AMMONIA; GLUTAMATE DEHYDROGENASE (NADP); GLYCEROL; POTASSIUM CHLORIDE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE; SODIUM CHLORIDE;

AMINATION; ARTICLE; BACTERIAL GROWTH; BIOREACTOR; CHEMICAL ANALYSIS; CONCENTRATION RESPONSE; ENZYME BINDING; ENZYME INHIBITION; ENZYME KINETICS; ENZYME STABILITY; ENZYME SUBSTRATE; HALOFERAX MEDITERRANEI; HALOPHILIC BACTERIUM; MEASUREMENT; NONHUMAN; STEADY STATE; VELOCITY;

ARCHAEA; BACTERIA (MICROORGANISMS); HALOFERAX MEDITERRANEI; HALOPHILIC ARCHAEON;

EID: 0034926467     PISSN: 10242422     EISSN: None     Source Type: Journal    
DOI: 10.3109/10242420109105266     Document Type: Article

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