Site-directed mutagenesis of Asp-376, the catalytic phosphorylation site, and Lys-507, the putative ATP-binding site, of the alpha-subunit of Torpedo californica Na+/K(+)-ATPase.

doi:10.1016/0005-2736(90)90028-m

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Article

Site-directed mutagenesis of Asp-376, the catalytic phosphorylation site, and Lys-507, the putative ATP-binding site, of the alpha-subunit of Torpedo californica Na+/K(+)-ATPase.

Biochimica et biophysica acta - 29 Jan 1990

Ohtsubo M, Noguchi S, Takeda K, Morohashi M, Kawamura M

Abstract excerpt

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...

Topics

Adenosine Triphosphate
Animals
Aspartic Acid
Base Sequence
Binding Sites
Female
Gene Expression
Kinetics
Lysine
Macromolecular Substances
Molecular Sequence Data

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Mutation

Oligodeoxyribonucleotides

Oocytes

Phosphorylation

Restriction Mapping

Sodium-Potassium-Exchanging ATPase

Torpedo

Source

Open in PubMed

Identifiers

PMID: 2154258
DOI: 10.1016/0005-2736(90)90028-m

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-2154258-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 29 Aug 2026.

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