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Article

Site-directed mutagenesis of the conserved beta subunit tyrosine 331 of Escherichia coli ATP synthase yields catalytically active enzymes.

The Journal of biological chemistry - 25 Jun 1990

Wise J G

Abstract excerpt

The ATP synthases of eubacteria and eukaryotes possess a conserved tyrosine (beta 331) that is labeled by ATP analogs and is believed to be at the catalytic site. In this report, this tyrosine was replaced by Phe, Ser, Cys, Gly, and Ala in an attempt to determine its role in catalysis. Each of the beta 331 mutant strains assembled an ATP synthase. Membranes from the beta 331-Ser, -Cys, -Ala, or -Gly strains...

Topics

Alleles
Base Sequence
Cell Membrane
Escherichia coli
Genes, Bacterial
Genotype
Kinetics
Macromolecular Substances
Molecular Sequence Data
Mutation
Oligonucleotide Probes

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Plasmids

Proton-Translocating ATPases

Tyrosine

Source

Identifiers

PMID: 2141332

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-2141332-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

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

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