Endopeptidase Clp
 | It has been suggested that this article be merged with ATP-dependent Clp protease proteolytic subunit. (Discuss) Proposed since June 2015. |
| Endopeptidase Clp | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 3.4.21.92 | ||||||||
| CAS no. | 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
References
- ^ Gottesman, S., Clark, W.P. and 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.
{{cite journal}}: CS1 maint: multiple names: authors list (link) - ^ Maurizi, M.R., Clark, W.P., Katayama, Y., Rudikoff, S., Pumphrey, J., Bowers, B. and 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.
{{cite journal}}: CS1 maint: multiple names: authors list (link) - ^ Maurizi, M.R., Thompson, M.W., Singh, S.K. and Kim, S.-H. (1994). "Endopeptidase Clp: the ATP-dependent Clp protease from Escherichia coli". Methods Enzymol. 244: 314–331. doi:10.1016/0076-6879(94)44025-5. PMID 7845217.
{{cite journal}}: CS1 maint: multiple names: authors list (link) - ^ 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. doi:10.1006/jmbi.1995.0400. PMID 7623377.
External links
- Endopeptidase+Clp at the U.S. National Library of Medicine Medical Subject Headings (MeSH)