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Literature summary for 3.4.22.15 extracted from

  • Zhu, S.; Wei, L.; Yamasaki, K.; Gallo, R.L.
    Activation of cathepsin L by the cathelin-like domain of protegrin-3 (2008), Mol. Immunol., 45, 2531-2536.
    View publication on PubMedView publication on EuropePMC

Activating Compound

Activating Compound Comment Organism Structure
protegrin-3 a porcine cathelicidin, molecular weight 11.7 kDa. The cathelin-like domain efficiently activates human cathepsin L. Partial deletion of the L2 loop of cathelin-like domain, a structurally equivalent region important ininteraction of cystatins with proteases, significantly decreases its activating effect on cathepsin L. Proposal of a complex model based on this functional loop, with the cathelin-like domain fitting into the active cleft of the enzyme in an analogous way as cystatin B does Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens
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Source Tissue

Source Tissue Comment Organism Textmining
commercial preparation isolated from liver Homo sapiens
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liver commercial production Homo sapiens
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