Kinetic study of the enzymatic cycling reaction conducted with 3α-hydroxysteroid dehydrogenase in the presence of excessive thio-NAD + and NADH

Analytical Biochemistry

Volumn 332, Issue 1, 2004, Pages 84-89

  Ueda, Shigeru ^a   Oda, Masayuki ^b   Imamura, Shigeyuki ^a   Ohnishi, Masatake ^b  

^a ASAHI KASEI PHARMA CORPORATION   (Japan)

^b KYOTO PREFECTURAL UNIVERSITY   (Japan)

Author keywords

3 Hydroxysteroid dehydrogenase; Enzymatic cycling; Nucleotide cofactor; Steady state kinetics

Indexed keywords

CATALYSIS; CATALYTIC OXIDATION; DISSOCIATION; ENZYMES; ISOMERS; KINETIC PARAMETERS; NUCLEOTIDES; RATE CONSTANTS;

CATALYTIC FUNCTIONS; COFACTORS; DISSOCIATION CONSTANT; ENZYMATIC CYCLING; HYDROXYSTEROID DEHYDROGENASE; INITIAL CONCENTRATION; REACTION MECHANISM; STEADY-STATE KINETICS;

KINETIC THEORY;

3ALPHA HYDROXYSTEROID DEHYDROGENASE; NICOTINAMIDE ADENINE DINUCLEOTIDE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE;

ARTICLE; CATALYSIS; CATALYST; CHEMICAL REACTION; COMPLEX FORMATION; CONCENTRATION (PARAMETERS); DISSOCIATION CONSTANT; ENZYME ACTIVITY; KINETICS; MOLECULAR MODEL; OXIDATION KINETICS; PRIORITY JOURNAL; STEADY STATE;

PSEUDOMONAS; PSEUDOMONAS SP.;

EID: 4143141013     PISSN: 00032697     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.ab.2004.04.035     Document Type: Article

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