The Enzyme Database

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EC 3.4.21.92     
Accepted name: endopeptidase Clp
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-Tyr┼NHMec; and Leu-Tyr-Leu┼Tyr-Trp, in which cleavage of the -Tyr┼Leu- and -Tyr┼Trp bonds also occurs)
Other name(s): 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, MetaCyc, MEROPS, 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]
[EC 3.4.21.92 created 1996]
 
 


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