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Literature summary for 3.4.21.92 extracted from

  • Maurizi, M.R.; Clark, W.P.; Katayama, Y.; Rudikoff, S.; Pumphrey, J.; Bowers, B.; Gottesman, S.
    Sequence and structure of Clp P, the proteolytic component of the ATP-dependent Clp protease of Escherichia coli (1990), J. Biol. Chem., 265, 12536-12545.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
of the subunit ClpP containing the proteolytic active site Escherichia coli

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
23000
-
240000 (ClpP with the subunit structure 12 * 23000, SDS-PAGE), gel filtration in presence of more than or at 0.1 M KCl, in absence of KCl, native ClpP appears to dimerize giving a structure with a MW of 500000 Escherichia coli
240000
-
240000 (ClpP with the subunit structure 12 * 23000, SDS-PAGE), gel filtration in presence of more than or at 0.1 M KCl, in absence of KCl, native ClpP appears to dimerize giving a structure with a MW of 500000 Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Purification (Commentary)

Purification (Comment) Organism
ClpP Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
casein + H2O
-
Escherichia coli small peptides derived from casein
-
?

Subunits

Subunits Comment Organism
? 240000 (ClpP with the subunit structure 12 * 23000, SDS-PAGE), gel filtration in presence of more than or at 0.1 M KCl, in absence of KCl, native ClpP appears to dimerize giving a structure with a MW of 500000 Escherichia coli
More enzyme consists of two components: ClpP and ClpA or ClpX Escherichia coli
More ClpP is synthesized with a 14-amino acid leader which is rapidly cleaved in vivo yielding the in vitro active protein of 193 amino acids Escherichia coli

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
additional information
-
pI: 6.0 (in presence of 8.0 M urea) Escherichia coli