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3.4.21.92: Endopeptidase Clp

This is an abbreviated version!
For detailed information about Endopeptidase Clp, go to the full flat file.

Word Map on EC 3.4.21.92

Reaction

Hydrolysis of proteins to small peptides in the presence of ATP and Mg2+. alpha-Casein is the usual test substrate. In the absence of ATP, only oligopeptides shorter than five residues are hydrolysed (such as succinyl-Leu-Tyr-/-NHMec, and Leu-Tyr-Leu-/-Tyr-Trp, in which cleavage of the -Tyr-/-Leu- and -Tyr-/-Trp bonds also occurs) =

Synonyms

ATP-dependent caseinolytic protease, ATP-dependent Clp protease, ATP-dependent Clp protease proteolytic subunit 1, ATP-dependent Clp protease proteolytic subunit 2, BsClpP, Caseinolytic protease, CLP, Clp protease, Clp proteolytic subunit, ClpA, ClpAP, ClpAP protease, ClpB, ClpC, ClpC ATPase, ClpC1, ClpCP protease, ClpCP3/R protease, ClpE, ClpP, ClpP Peptidase, ClpP Protease, ClpP protease complex, ClpP1, ClpP1 protease, ClpP1P2, ClpP2, ClpP2 protease, ClpP3, ClpP3/R complex, ClpQ, ClpR, ClpS1, ClpX, ClpX2, ClpXP, ClpXP protease, ClpY, CplC, endopeptidase Clp, endopeptidase Ti, Heat shock protein F21.5, heat-shock protease ClpP, nClpP7, nClpP8, PfClpP, Protease Ti, stress protein G7

ECTree

     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.21 Serine endopeptidases
                3.4.21.92 Endopeptidase Clp

Molecular Weight

Molecular Weight on EC 3.4.21.92 - Endopeptidase Clp

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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
12620
-
ClpA, analytical ultracentrifugation
12640
-
ClpB, analytical ultracentrifugation
13940
-
ClpX, analytical ultracentrifugation
140000
14230
-
ClpY, analytical ultracentrifugation
150000
-
gel filtration, enzyme treated with inhibitor diisopropyl fluorophosphate, 1-[4-(4-ethynylbenzoyl)-1,1-dioxido-1,2-thiazetidin-2-yl]undec-10-en-1-one, or beta-lactone (4R)-3-(4-methoxyphenyl)-4-(pent-4-yn-1-yl)oxetan-2-one
180000
-
n * 230000, n * 180000, ClpP1, ClpP3, clpP4, ClpP5, clpP6, clpR1, clpR2, ClpR3, cClR4, ClpS1
21000
-
1 * 230000, subunit ClpP (12 * 21000, amino acid sequence, subunit of ClpP)
22000
-
ClpP1(pClpP), MALDI-TOF, ClpS1(nClpC like), MALDI-TOF, ClpP5 (nClpP1), MALDI-TOF, ClpP6 (nClpP6), MALDI-TOF
23000
23000 - 25000
-
ClpP2 (nClpP7), MALDI-TOF
230000
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
25000
Western blot
26000
-
ClpR2 (nClpP2), MALDI-TOF, 6,13,21 ClpP4 (nClpP4), MALDI-TOF
26000 - 29000
-
2 isoenzymes, immunoblot analysis, antibody against plastid-encoded rice ClpP
27000
-
ClpR3 (nClpP8), MALDI-TOF
270000
28000
-
ClpR1 (nClpP5), MALDI-TOF
29000
-
ClpP3 (nClpP3), MALDI-TOF
300000
304000
-
gel filtration, native enzyme
335000
-
wild type, native Page, decreased by 80% in clpP6 antisense mutants, ClpP6 is necessary for the formation of the Clp proteolytic core complex
340000
-
E. coli
346000
-
sedimentation velocity analytical ultracentrifugation, tetradecamer
350000
-
ClpP protease complex, gel filtration
43000
calculated from cDNA, unprocessed protein
46000
-
x * 46000, ClpX, SDS-PAGE
46300
-
x * 46300, ClpX, calculation from amino acid sequence
700000
-
E. coli, complex of subunits ClpA with ClpP in presence of ATP
80000
-
x * 80000 (ClpA, SDS-PAGE, behaves as a dimer of MW 140000 Da on gel filtration) + x * 23000 (ClpP, SDS-PAGE, behaves as a complex of 10-12 subunits, MW 260000 Da)
81000
-
x * 81000, ClpA, SDS-PAGE
83000
-
x * 120000-140000, subunit ClpA, gel filtration, x * 83000, subunit ClpA, amino acid sequence