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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

Purification

Purification on EC 3.4.21.92 - Endopeptidase Clp

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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
a subcomplex of ClpP can be produced by dissociation, comprising ClpP1 and ClpR1, 2, 3 and 4, similar to the ClpR-ring described in land plants. Purified ClpP preparation also contains two ClpT subunits, ClpT3 and ClpT4, which like the land plant ClpT1 and ClpT2 show 2 Clp-N domains
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by anion exchange and gel filtration
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by immunoprecipitation
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ClpA, ClpAP, Clp-SC
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ClpP-His6, ClpA and ClpPDELTAN
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ClpP3/R complex purified on Ni2+ affinity column and by gel filtration, purification of ClpC and ClpS1
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glutathione-sepharose 4B bead column chromatography
of the recombinant proteins by Ni2+-NTA chromatography and gel filtration, untagged protein by phenyl sepharose and Sephacryl 16/60 S-300 column chromatography
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SSD domains of the ATPase activity
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using Ni-NTA chromatography