Endopeptidase Clp

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Endopeptidase Clp
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ATP-dependent Clp protease (fragment) homo14mer, Streptococcus pneumoniae
Identifiers
EC number 3.4.21.92
CAS number 110910-59-3
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum

Endopeptidase Clp (EC 3.4.21.92, 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]

References[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. 

External links[edit]