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[Proteolysis coupled with ATP. Regulation of activity of proteolytic centers of Escherichia coli lon protease].

Bioorganicheskaia khimiia - 1 Jan 2000

Tsirul'nikov K B, Mel'nikov E E, Rotanova T V

Abstract excerpt

Regulation of activity of the proteolytic sites of Lon protease was studied. It was found that ATP-Mg has the properties of a noncompetitive activator of peptidase sites. The processive mechanism of the hydrolysis of protein substrates by Lon protease was experimentally confirmed under the conditions of ATP hydrolysis. It was shown that the oligomeric state of the enzyme is the necessary prerequisite for the...

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Identifiers

PMID: 14601403
DOI: 10.1023/a:1026049525351

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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[Proteolysis coupled with ATP. Regulation of activity of proteolytic centers of Escherichia coli lon protease].PMID 14601403Read ↗

[Coupling of proteolysis and hydrolysis of ATP upon functioning of Lon proteinase of Escherichia coli. II. Hydrolysis of ATP and activity of peptide hydrolase sites of the enzyme].Semantic proximity Read ↗

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

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[Synthesis and characterisation of ATP-dependent forms of Lon-proteinase with modified N-terminal domain from Escherichia coli].Semantic proximity Read ↗

[ATP-dependent proteinase La from Escherichia coli].Semantic proximity Read ↗

Processive degradation of unstructured protein by Escherichia coli Lon occurs via the slow, sequential delivery of multiple scissile sites followed by rapid and synchronized peptide bond cleavage events.Semantic proximity Read ↗

Mutations to a glycine loop in the catalytic site of human Lon changes its protease, peptidase and ATPase activities.Semantic proximity Read ↗

Effects of inorganic polyphosphate on the proteolytic and DNA-binding activities of Lon in Escherichia coli.Semantic proximity Read ↗

Lon and Clp-like ATP-dependent proteases of Lactococcus lactis.Semantic proximity Read ↗

LonR9 carrying a single Glu614 to Lys mutation inhibits the ATP-dependent protease La (Lon) by forming mixed oligomeric complexes.Semantic proximity Read ↗

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