Article
ATPase kinetics for wild-type Saccharomyces cerevisiae F1-ATPase and F1-ATPase with the beta-subunit Thr197-->Ser mutation.
European journal of biochemistry - 15 Jun 1994
Mueller D M, Indyk V, McGill L
Abstract excerpt
Unisite ATPase kinetic constants were measured for wild-type yeast Saccharomyces cerevisiae F1-ATPase and F1-ATPase with the Thr197-->Ser mutation in the beta subunit. Under unisite conditions, the concentration of ATP is greater than that of the enzyme, ATP hydrolysis is slow and the affinity of...
Topics
- Adenosine Diphosphate
- Adenosine Triphosphate
- Amino Acid Sequence
- Azides
- Binding Sites
- Kinetics
- Molecular Sequence Data
- Mutation
- Proton-Translocating ATPases
- Saccharomyces cerevisiae
- Sodium Azide
- Sulfites
