Endopeptidase Clp

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Endopeptidase Clp
ATP-dependent Clp protease (fragment) homo14mer, Streptococcus pneumoniae
EC number
CAS number 110910-59-3
IntEnz IntEnz view
ExPASy NiceZyme view
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum

Endopeptidase Clp (EC, endopeptidase Ti, caseinolytic protease, protease Ti, ATP-dependent Clp protease, ClpP, Clp protease).[1][2][3][4] This enzyme catalyses the following chemical reaction

Hydrolysis of proteins to small peptides in the presence of ATP and Mg2+.

This bacterial enzyme contains subunits of two types, ClpP, with peptidase activity, and ClpA, with ATPase activity.

See also[edit]


  1. ^ Gottesman, S.; Clark, W.P.; Maurizi, M.R. (1990). "The ATP-dependent Clp protease of Escherichia coli. Sequence of clpA and identification of a Clp-specific substrate". J. Biol. Chem. 265: 7886–7893. PMID 2186030. 
  2. ^ Maurizi, M.R.; Clark, W.P.; Katayama, Y.; Rudikoff, S.; Pumphrey, J.; Bowers, B.; Gottesman, S. (1990). "Sequence and structure of Clp P, the proteolytic component of the ATP-dependent Clp protease of Escherichia coli". J. Biol. Chem. 265: 12536–12545. PMID 2197275. 
  3. ^ Maurizi, M.R.; Thompson, M.W.; Singh, S.K.; Kim, S.-H. (1994). "Endopeptidase Clp: the ATP-dependent Clp protease from Escherichia coli". Methods Enzymol. 244: 314–331. PMID 7845217. doi:10.1016/0076-6879(94)44025-5. 
  4. ^ Kessel, M. (1995). ", Maurizi,M.R., Kim, B., Kocsis, E., Trus, B., Singh, S.K. and Steven, A.C. Homology in structural organization between E. coli ClpAP protease and the eukaryotic 26 S proteasome". J. Mol. Biol. 250: 587–594. PMID 7623377. doi:10.1006/jmbi.1995.0400. 

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