Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

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

Bioorganicheskaia khimiia - 1 Dec 1999

Rotanova T V

Abstract excerpt

Enzymic and structural peculiarities of the ATP-dependent Lon protease from Escherichia coli and its mutant and modified forms were studied. Amino acid residues important for the function of proteolytic and ATPase sites and for the transmission of the interdomain signals of the activity coupling were found. It was shown that the protein substrates are hydrolyzed only by the full-size enzyme, whereas the isolated...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Escherichia coli
Share to Adenosine Triphosphate
Share to Amino Acid Sequence

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to ATP-Dependent Proteases

Share to Escherichia coli Proteins

Share to Heat-Shock Proteins

Share to Protease La

Share to Serine Endopeptidases

Source

Identifiers

PMID: 10734549

Provenance

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.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

[Structural and functional characteristics of ATP-dependent Lon-proteinase from Escherichia coli].PMID 10734549Read ↗

[Synthesis and characterisation of ATP-dependent forms of Lon-proteinase with modified N-terminal domain 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 ↗

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

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

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

[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 ↗

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

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

[A test system based on the lux-regulon from Vibrio fischeri for studying the functional activity of mutant forms of Escherichia coli lon-proteinase].Semantic proximity Read ↗

[Biogenesis and secretion of alkaline phosphatase and its mutants in Escherichia coli. III. Substitution of N-terminal amino acids of alkaline phosphatase affect its biogenesis].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 ↗

⌁Select a neighboring publication to make it the new centre.