Article
Catalytic and regulatory sites of yeast plasma membrane H(+)-ATPase studied by directed mutagenesis.
Biochimica et biophysica acta - 25 Jul 1990
Serrano R, Portillo F
Abstract excerpt
More than 35 site-directed mutants of the plasma membrane H(+)-ATPase of the yeast Saccharomyces cerevisiae have been constructed and expressed to investigate the function of N- and C-termini and of conserved amino acids. Conserved motif TGES seems to form part of both the catalytic machinery for the hydrolysis of the phosphorylated intermediate and the vanadate binding site. In addition, it is involved in the...
Topics
- Amino Acid Sequence
- Binding Sites
- Cell Membrane
- Models, Molecular
- Molecular Sequence Data
- Mutation
- Protein Engineering
- Proton-Translocating ATPases
- Saccharomyces cerevisiae