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Article

Tryptophan-free Escherichia coli F1-ATPase.

Archives of biochemistry and biophysics - 1 Mar 1994

Wilke-Mounts S, Weber J, Grell E, Senior A E

Abstract excerpt

We have engineered a mutant form of Escherichia coli F1-ATPase which is tryptophan-free and contains five mutations, namely delta W28L/alpha W513F/gamma W108Y/gamma W206Y/beta W107F. A strain carrying all five mutations grew normally by oxidative phosphorylation. Purified mutant F1-ATPase showed Vmax and Km both 65% higher than wild-type, resulting in kcat/Km the same as wild-type. The pH dependence of ATPase...

Topics

Adenosine Diphosphate
Adenosine Triphosphate
Aurovertins
Azides
Base Sequence
Dicyclohexylcarbodiimide
Escherichia coli
Hydrogen-Ion Concentration
Molecular Sequence Data
Mutagenesis, Site-Directed
Mutation

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Oxidative Phosphorylation

Proton-Translocating ATPases

Spectrometry, Fluorescence

Tryptophan

Source

Identifiers

PMID: 8135549
DOI: 10.1006/abbi.1994.1125

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-8135549-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

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

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