Candida utilis NAD+ kinase: Kinetic and inhibition studies with ADP
Copyright policy )Candida utilis NAD+ kinase: Kinetic and inhibition studies with ADP
1. Initial velocity and product inhibition studies using ADP were carried out on cytoplasmic NAD+ kinase (ATP:NAD 2' phosphotransferase, EC 2.7.1.23) purified from Candida utilis. Initial velocity studies were also carried out on a sample of chicken liver NAD+ kinase. 2. The data indicate both enzymes followed a sequential mechanism of reactant binding. 3. Product inhibition studies on C. utilis NAD+ kinase suggest the mechanism of NAD+, ATP addition is best described as rapid equilibrium random with multiple binding of ADP to the free enzyme and the E X ATP and E X NAD+ complexes. 4. The characteristics of this enzyme, prepared from several sources, are briefly summarized.
- Seton Hill University United States
Binding Sites, Phosphotransferases, NAD, Adenosine Diphosphate, Kinetics, Phosphotransferases (Alcohol Group Acceptor), Adenosine Triphosphate, Liver, Animals, Chickens, Candida
Binding Sites, Phosphotransferases, NAD, Adenosine Diphosphate, Kinetics, Phosphotransferases (Alcohol Group Acceptor), Adenosine Triphosphate, Liver, Animals, Chickens, Candida
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