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Article

Kinetic properties of Mg, Ca ATPase from various Escherichia coli mutants.

Zeitschrift fur Naturforschung. Section C, Biosciences - 1 Jan 2000

Ahlers J, Günther T, Schrandt I

Abstract excerpt

The ATPase is not lacking in the ATPase mutants DL 54 and AN 120 but has very different kinetic properties including a higher Cl- optimum and higher Km values for MgATP. In AN 120, the ATPase activity also has a higher Mg2+ optimum.

Topics

Adenosine Triphosphatases
Azides
Chlorides
Enzyme Activation
Escherichia coli
Kinetics
Magnesium
Mutation

Source

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Identifiers

PMID: 134563
DOI: 10.1515/znc-1976-3-422

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-134563-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

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

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