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| http://www.biopax.org/relea... | |
| http://www.biopax.org/relea... |
Putative ATP-dependent Clp protease proteolytic subunit, mitochondrial
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| http://www.biopax.org/relea... |
CLPP_HUMAN
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| http://www.biopax.org/relea... | |
| http://www.biopax.org/relea... |
3.4.21.92,
Endopeptidase Clp
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| http://www.biopax.org/relea... |
FUNCTION: Clp cleaves peptides in various proteins in a process that requires ATP hydrolysis. Clp may be responsible for a fairly general and central housekeeping function rather than for the degradation of specific substrates. CATALYTIC ACTIVITY: Hydrolysis of proteins to small peptides in the presence of ATP and magnesium. Alpha-casein is the usual test substrate. In the absence of ATP, only oligopeptides shorter than five residues are hydrolyzed (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). SUBUNIT: Tetradecamer that assembles into a two heptameric rings with a central cavity. SUBCELLULAR LOCATION: Mitochondrion matrix. TISSUE SPECIFICITY: Predominantly expressed in skeletal muscle. Intermediate levels in heart, liver and pancreas. Low in brain, placenta, lung and kidney. SIMILARITY: Belongs to the peptidase S14 family. COPYRIGHT: Protein annotation is derived from the UniProt Consortium (http://www.uniprot.org/). Distributed under the Creative Commons Attribution-NoDerivs License.
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