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Literature summary for 3.4.21.92 extracted from
- Control of peptide product sizes by the energy-dependent protease ClpAP (2005), Biochemistry, 44, 13921-13931.
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Escherichia coli | - |
- |
- |
Reaction
| Reaction | Comment | Organism | Reaction ID |
|---|---|---|---|
| Hydrolysis of proteins to small peptides in the presence of ATP and Mg2+. alpha-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) | dual mechanism in which translocation alternates with proteolysis, allowing peptides of more or less unifirm length to be cleaved processively from a translocating substrate | Escherichia coli |
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