Endopeptidase Clp
Definition:
EC Tree > 3 Hydrolases > 3.4 Acting on peptide bonds (peptidases) > 3.4.21 Serine endopeptidases > 3.4.21.92 Endopeptidase Clp
Endopeptidase Clp (ClpAP/ClpXP) is a bacterial ATP-dependent protease with two subunit types: ClpP, the serine peptidase (type example of family S14), and ClpA, the ATPase; the ClpAP complex, composition (ClpP14ClpA6)2, displays ATP-dependent endopeptidase activity; it hydrolyses proteins to small peptides in the presence of ATP and Mg2+, alpha-casein being the usual test substrate, and in the absence of ATP only oligopeptides shorter than five residues are hydrolysed (e.g. succinyl-Leu-Tyr-NHMec and Leu-Tyr-Leu-Tyr-Trp, with cleavage of Tyr-Leu and Tyr-Trp). By ATP-dependent degradation of misfolded and regulatory proteins it maintains bacterial protein quality control. It appears in viruses and cellular organisms.
Endopeptidase Clp (ClpAP/ClpXP) is a bacterial ATP-dependent protease with two subunit types: ClpP, the serine peptidase (type example of family S14), and ClpA, the ATPase; the ClpAP complex, composition (ClpP14ClpA6)2, displays ATP-dependent endopeptidase activity; it hydrolyses proteins to small peptides in the presence of ATP and Mg2+, alpha-casein being the usual test substrate, and in the absence of ATP only oligopeptides shorter than five residues are hydrolysed (e.g. succinyl-Leu-Tyr-NHMec and Leu-Tyr-Leu-Tyr-Trp, with cleavage of Tyr-Leu and Tyr-Trp). By ATP-dependent degradation of misfolded and regulatory proteins it maintains bacterial protein quality control. It appears in viruses and cellular organisms.
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