Literature summary for 3.4.21.53 extracted from

Melnikov, E.E.; Andrianova, A.G.; Morozkin, A.D.; Stepnov, A.A.; Makhovskaya, O.V.; Botos, I.; Gustchina, A.; Wlodawer, A.; Rotanova, T.V.
Limited proteolysis of E. coli ATP-dependent protease Lon - a unified view of the subunit architecture and characterization of isolated enzyme fragments (2008), Acta Biochim. Pol., 55, 281-296.

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General Stability

General Stability	Organism
identification of four regions sensitive to chymotryptic digestion	Escherichia coli

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	-	-	-

Subunits

Subunits	Comment	Organism
More	the ATPase fragment isolated after chymotryptic digestion of the protein has no ATPase activity in spite of its ability to bind nucleotides. It is monomeric in solution. The isolated monomeric proteolytic fragment does not display proteolytic activity. The intact ATPase/proteolytic fragment forms dimers and tetramers and exhibits properties of a non-processive protease and show ATPase activity with self-degradation upon ATP hydrolysis	Escherichia coli

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Release 2023.1 (January 2023)