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Article

[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 condit...

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Identifiers

PMID: 14601403
DOI: 10.1023/a:1026049525351

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 1 Sept 2026. Prepared record publication-14601403-2026-09-01.1. Manifest publication-graph-cohort-2026-09-01.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 1 Sept 2026.

Related research

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Research trail→

Click a neighbor to travelStep 1 · 12 closest

[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 ↗

[Structural and functional characteristics of ATP-dependent Lon-proteinase from Escherichia coli].Semantic proximity Read ↗

[The Effect of Mutations in the Inserted Domain of ATP-Dependent Lon Protease from E. coli on the Enzyme Function].Semantic proximity Read ↗

[Isolation and characterization of fragments of ATP-dependent protease Lon from Escherichia coli obtained by limited proteolysis].Semantic proximity Read ↗

[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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