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Literature summary for 3.4.21.53 extracted from

  • Vieux, E.F.; Wohlever, M.L.; Chen, J.Z.; Sauer, R.T.; Baker, T.A.
    Distinct quaternary structures of the AAA+ Lon protease control substrate degradation (2013), Proc. Natl. Acad. Sci. USA, 110, E2002-E2008.
    View publication on PubMedView publication on EuropePMC

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
525000
-
hexamer, gel filtration and sedimentation velocity analytical ultracentrifugation Escherichia coli
930000
-
dodecamer, gel filtration and sedimentation velocity analytical ultracentrifugation Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information compared with hexamers, enzyme dodecamers are much less active in degrading large substrates but equally active in degrading small substrates, whcih represents a a unique gating mechanism that allows the repertoire of enzyme substrates to be tuned by its assembly state Escherichia coli ?
-
?

Subunits

Subunits Comment Organism
dodecamer hexamers of Escherichia coli Lon also interact to form a dodecamer at physiological protein concentrations, the dodecamer shows a prolate structure with the protease chambers at the distal ends and a matrix of N domains forming an equatorial hexamer-hexamer interface, with portals of about 45 A providing access to the enzyme lumen Escherichia coli
homohexamer
-
Escherichia coli
More compared with hexamers, enzyme dodecamers are much less active in degrading large substrates but equally active in degrading small substrates Escherichia coli

Synonyms

Synonyms Comment Organism
lon
-
Escherichia coli
lon protease
-
Escherichia coli

General Information

General Information Comment Organism
physiological function Lon is an ATPase associated with cellular activities protease that controls cell division in response to stress and also degrades misfolded and damaged proteins Escherichia coli