3.4.21.92: Endopeptidase Clp
This is an abbreviated version!
For detailed information about Endopeptidase Clp, go to the full flat file.
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)
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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
Application
Application on EC 3.4.21.92 - Endopeptidase Clp
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analysis
development of a ClpXP protein degradation systemusing purified ClpXP in a cell-free transcription-translation system
drug development
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synthetic beta-lactones as novel inhibitors for specific and selective targeting of the key virulence regulator ClpP
medicine
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C. jejuni is the principal cause of bacterial food-borne gastroenteritis in humans. ClpP may be a suitable target of new intervention strategies aimed at reducing C. jejuni in poultry production. The growth of the ClpP mutant is impaired at high temperature and at conditions that are known to increase the level of misfolded proteins
medicine
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ClpP as antibacterial drug target
medicine
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ClpP as antibacterial drug target
medicine
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ClpP as antibacterial drug target
medicine
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ClpP as antibacterial drug target
medicine
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ClpP proteolytic activity is strongly involved in the pathogenicity of S. aureus and adaptation of the pathogen to several stresses
medicine
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induction of Bacillus subtilis genes controlled by the extracytoplasmic function alternative sigma factor W is strongly impaired in a strain deleted for the ClpP peptidase gene
medicine
ClpP is expressed in vivo during mild and paucibacillary paratuberculosis infection in sheep
medicine
correlative effect of Lon and ClpP upregulation on loss of mitochondrial Fe-S proteins during the progression of Friedreich ataxia suggesting that Fe-S proteins are potential targets of Lon and ClpP proteases in Friedreich ataxia
medicine
immunizing mice intranasally with a mixture of ClpP and CbpA (choline binding protein A) elicites better protection than that of immunizing either single ClpP or CbpA
medicine
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protective efficacy of mucosal immunization with ClpP as a promising pneumococcal protein antigen
medicine
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ClpP activation is an effective means of controlling the replication of Mycobacterium tuberculosis
medicine
ATP-dependent Clp protease proteolytic subunit 2 displays potent immunogenicity. In tuberculosis patients, both the levels of ClpP2 antigen and antibody are increased. ClpP2 antigens may be used as a biomarker in tuberculosis pathogenesis
medicine
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treatment with ClpP inhibits cell growth and induces apoptosis in SK-N-SH neuroblastoma cells. Treatment results in hypodiploid DNA contents, increased Bax/Bcl-2 ratio and induction of reactive oxygen species production. The release of cytochrome c from mitochondria into the cytosol, is not observed in ClpP-treated cells. Pretreatment with Z-Val-Ala-Asp-fluoromethylketone, a broad spectrum caspase inhibitor, cannot rescue apoptotic cells from ClpP toxicity. Caspase-3 and -8 activation and cleavage of PARP are not detected. Caspase independent apoptosis-inducing factor is released from mitochondria and translocated to the nucleus in response to ClpP. ClpP treatment results in the increase of p53 activity, and cytoplasmic p53 levels are increased by ClpP
medicine
reducing the levels of mitochondrial ClpP or ClpX renders human cancer cells more sensitive to cisplatin. ClpP levels are elevated in cervical carcinoma cells (KB-CP20) and hepatoma cells (BEL-7404-CP20) independently selected for cisplatin resistance
medicine
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C. jejuni is the principal cause of bacterial food-borne gastroenteritis in humans. ClpP may be a suitable target of new intervention strategies aimed at reducing C. jejuni in poultry production. The growth of the ClpP mutant is impaired at high temperature and at conditions that are known to increase the level of misfolded proteins
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medicine
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ATP-dependent Clp protease proteolytic subunit 2 displays potent immunogenicity. In tuberculosis patients, both the levels of ClpP2 antigen and antibody are increased. ClpP2 antigens may be used as a biomarker in tuberculosis pathogenesis
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