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Article

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

Bioorganicheskaia khimiia - 1 Jan 2000

Kudzhaev A M, Andrianova A G, Serova O V, Arkhipova V A, Dubovtseva E S, Rotanova T V

Abstract excerpt

ATP-Dependent protease LonA from E. coli (Ec-Lon), belonging to the superfamily of AAA+ proteins, is a key member of the protein quality control system in bacterial cells. Ec-Lon functions as homohexamer and degrades abnormal and defective polypeptides as well as a number of regulatory proteins by the processive mechanism. Ec-Lon subunit includes--the both ATPase and proteolytic components (AAA+ module and P...

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Identifiers

PMID: 26762095
DOI: 10.1134/s1068162015050076

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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.

Related research

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[The Effect of Mutations in the Inserted Domain of ATP-Dependent Lon Protease from E. coli on the Enzyme Function].PMID 26762095Read ↗

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

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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 ↗

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