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 WP, Maurizi MR (May 1990). "The ATP-dependent Clp protease of Escherichia coli. Sequence of clpA and identification of a Clp-specific substrate". The Journal of Biological Chemistry. 265 (14): 7886–93. PMID 2186030.
  2. ^ Maurizi MR, Clark WP, Katayama Y, Rudikoff S, Pumphrey J, Bowers B, Gottesman S (July 1990). "Sequence and structure of Clp P, the proteolytic component of the ATP-dependent Clp protease of Escherichia coli". The Journal of Biological Chemistry. 265 (21): 12536–45. PMID 2197275.
  3. ^ Maurizi MR, Thompson MW, Singh SK, Kim SH (1994). "Endopeptidase Clp: ATP-dependent Clp protease from Escherichia coli". Methods in Enzymology. 244: 314–31. doi:10.1016/0076-6879(94)44025-5. PMID 7845217.
  4. ^ Kessel M, Maurizi MR, Kim B, Kocsis E, Trus BL, Singh SK, Steven AC (July 1995). "Homology in structural organization between E. coli ClpAP protease and the eukaryotic 26 S proteasome". Journal of Molecular Biology. 250 (5): 587–94. doi:10.1006/jmbi.1995.0400. PMID 7623377.

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