Site-directed mutagenesis of Asp-376, the catalytic phosphorylation site, and Lys-507, the putative ATP-binding site, of the α-subunit of Torpedo californica
| Autor: | Shunsuke Noguchi, Kazuo Takeda, Michihiro Ohtsubo, Masaru Kawamura, Michiaki Morohashi |
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| Rok vydání: | 1990 |
| Předmět: |
Macromolecular Substances
Xenopus Sodium-Potassium-Exchanging ATPase ATPase Protein subunit Molecular Sequence Data Restriction Mapping Biophysics Gene Expression Biology Torpedo Biochemistry law.invention chemistry.chemical_compound Adenosine Triphosphate law Animals Phosphorylation Binding site Na+/K+-ATPase Site-directed mutagenesis Aspartic Acid Binding Sites Base Sequence Lysine Cell Biology Molecular biology Kinetics Oligodeoxyribonucleotides chemistry Mutation Oocytes biology.protein Female Adenosine triphosphate |
| Zdroj: | Biochimica et Biophysica Acta (BBA) - Biomembranes. 1021:157-160 |
| ISSN: | 0005-2736 |
| DOI: | 10.1016/0005-2736(90)90028-m |
| Popis: | Point mutations of Asp-376 of the alpha-subunit of Torpedo californica Na+/K(+)-ATPase (the site of phosphorylation during the catalytic cycle) to Asn, Glu or Thr led to virtual abolishment of Na+/K(+)-ATPase activity and ouabain-binding capacity. Replacement of Lys-507 of the same subunit (the putative ATP-binding site) by Met resulted in decreases in Na+/K(+)-ATPase activity and ouabain-binding capacity. These results are in agreement with those reported for rabbit sarcoplasmic reticulum Ca2(+)-ATPase (Maruyama, K. and MacLennan, D.H. (1988) Proc. Natl. Acad. Sci. USA 85, 3314-3318). |
| Databáze: | OpenAIRE |
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