Endopeptidase Clp
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 | ||||||||
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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.; 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.
- ↑ 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.
- ↑ 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. doi:10.1016/0076-6879(94)44025-5. PMID 7845217.
- ↑ 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 US National Library of Medicine Medical Subject Headings (MeSH)
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