Activity of NADH oxidase from Thermus thermophilus in water/alcohol binary mixtures is limited by the stability of quaternary structure

Journal of Molecular Catalysis B: Enzymatic

Volumn 64, Issue 1-2, 2010, Pages 60-67

  Tóth, Kamil ^a   Sedlák, Erik ^a,b   Musatov, Andrej ^b   Žoldák, Gabriel ^c  

^a P J AFÁRIK UNIVERSITY   (Slovakia)

^b UNIVERSITY OF TEXAS HEALTH SCIENCE CENTER AT SAN ANTONIO   (United States)

^c UNIVERSITY OF BAYREUTH   (Germany)

Author keywords

Active site; Alcohols; Flavoenzyme; Michaelis constants; NADH oxidase

Indexed keywords

ACTIVE SITE; ALCOHOL CONCENTRATIONS; CATALYTIC CONSTANTS; CATALYTIC EFFICIENCIES; EFFECT OF WATER; ENZYME CONCENTRATIONS; FLAVIN COFACTOR; FLAVIN REDUCTASE; FLAVOENZYMES; ISO-PROPANOLS; MICHAELIS CONSTANTS; NADH OXIDASE; NATIVE STRUCTURES; NITROREDUCTASES; OPTIMUM ACTIVITY; QUATERNARY STRUCTURE; THEORETICAL SIMULATION; THERMOPHILIC ENZYMES; THERMUS THERMOPHILUS; TIME CONSTANTS; TIME DEPENDENT;

BINARY MIXTURES; CONCENTRATION (PROCESS); DISSOCIATION; ENZYMES; ETHANOL; METHANOL; PROPANOL;

ENZYME ACTIVITY;

2 PROPANOL; ALCOHOL; FLAVOPROTEIN; METHANOL; PROPANOL; QUERCETIN; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE DEHYDROGENASE; WATER;

ARTICLE; CONCENTRATION (PARAMETERS); CONTROLLED STUDY; DIMERIZATION; DISSOCIATION; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME CONFORMATION; ENZYME INACTIVATION; ENZYME MECHANISM; ENZYME REACTIVATION; ENZYME STABILITY; INCUBATION TIME; MICHAELIS CONSTANT; MISCIBILITY; NONHUMAN; PROTEIN DENATURATION; PROTEIN QUATERNARY STRUCTURE; PROTEIN STABILITY; THERMUS THERMOPHILUS;

THERMUS THERMOPHILUS;

EID: 77951498568     PISSN: 13811177     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.molcatb.2010.02.002     Document Type: Article

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