Literature summary for 3.4.21.53 extracted from

Vasilyeva, O.V.; Martynova, N.Y.; Potapenko, N.A.; Ovchinnikova, T.V.
Isolation and characterization of fragments of the ATP-dependent protease Lon from Escherichia coli obtained by limited proteolysis (2004), Russ. J. Bioorg. Chem., 30, 306-314.

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Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	-	-	-

Subunits

Subunits	Comment	Organism
More	isolated proteolytic domain LonP, obtained by limited proteolysis, exhibits both peptidase and proteolytic activity, but cleaves large protein substrates at a significantly lower rate than the full size protease. LonAP fragment, containing both the ATPase and the proteolytic domains, retains almost all of the enzymawtic properties of the full-size protein. both LonP and LonAP predominantly form dimers unlike the native protease Lon functioning as a tetramer	Escherichia coli

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Release 2023.1 (January 2023)