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[In vitro coupling of ATP hydrolysis to proteolysis of ATP site mutant forms of Lon-proteinase from E.coli].

Bioorganicheskaia khimiia - 1 Apr 1998

Mel'nikov E E, Tsirul'nikov K B, Ginodman L M, Rotanova T V

Abstract excerpt

In order to identify amino acid residues involved in ATP hydrolysis by Escherichia coli protease Lon or participating in the signal transduction from the ATPase domain to the proteolytic one, potentially important residues of the ATPase domain were substituted using site-directed mutagenesis, and the properties of the resulting mutant enzymes were studied. It was found that residues K362, T363 (Walker's motif A),...

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PMID: 9612572

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

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[In vitro coupling of ATP hydrolysis to proteolysis of ATP site mutant forms of Lon-proteinase from E.coli].PMID 9612572Read ↗

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