NHMec; and Leu-Tyr-LeuTyr-Trp, in which cleavage of the -TyrLeu- and -TyrTrp bonds also occurs)
Reaction: Hydrolysis of proteins to small peptides in the presence of ATP and Mg2+. α-Casein is the usual test substrate. In the absence of ATP, only oligopeptides shorter than five residues are hydrolysed (such as succinyl-Leu-TyrNHMec; and Leu-Tyr-LeuTyr-Trp, in which cleavage of the -TyrLeu- and -TyrTrp bonds also occurs)
Other names: endopeptidase Ti; caseinolytic protease; protease Ti; ATP-dependent Clp protease; endopeptidase Ti; caseinolytic protease; ClpP; Clp protease
Comments: An enzyme from bacteria that contains subunits of two types, ClpP, with peptidase activity, and ClpA, with ATPase activity. The ClpAP complex, which displays ATP-dependent endopeptidase activity, has the composition (ClpP14ClpA6)2 [4]. ClpP is the type example of peptidase family S14
Links to other databases: BRENDA, EXPASY, KEGG, MEROPS, Metacyc, PDB, CAS registry number: 110910-59-3
References
1. Gottesman, S., Clark, W.P. and Maurizi, M.R. The ATP-dependent Clp protease of Escherichia coli. Sequence of clpA and identification of a Clp-specific substrate. J. Biol. Chem. 265 (1990) 7886-7893 [PMID: 2186030]
2. Maurizi, M.R., Clark, W.P., Katayama, Y., Rudikoff, S., Pumphrey, J., Bowers, B. and Gottesman, S. Sequence and structure of Clp P, the proteolytic component of the ATP-dependent Clp protease of Escherichia coli. J. Biol. Chem. 265 (1990) 12536-12545. [PMID: 2197275]
3. Maurizi, M.R., Thompson, M.W., Singh, S.K. and Kim, S.-H. Endopeptidase Clp: the ATP-dependent Clp protease from Escherichia coli. Methods Enzymol. 244 (1994) 314-331. [PMID: 7845217]
4. Kessel, M., 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 (1995) 587-594. [PMID: 7623377]