Penicillopepsin

From Proteopedia

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Template:STRUCTURE 1ppm

Contents 1 Function 2 Relevance 3 3D structures of penicillopepsin 4 References

Function

Penicillopepsin (PP) is a proteinase with a broad spectrum of substrates. PP prefers hydrophobic residues at P1 and P1’ sites. PP is a member of the aspartic proteinase family. Its extended binding site cleft can bind at least 7 amino acids^[1].

Relevance

PP causes clotting in milk and activates trypsinogen.

3D structures of penicillopepsin

3app – PjPP – Penicillium janthinellum
1ppl, 1ppm, 1ppk – PjPP + peptide analog
1apt, 1apu, 1apv, 1apw - PjPP + pepstatin analog
2wea, 2web, 2wec, 2wed, 1bxo, 1bxq - PjPP + peptidyl inhibitor

References

1. ↑ Takahashi M, Hofmann T. Acyl intermediates in penicillopepsin-catalysed reactions and a discussion of the mechanism of action of pepsins. Biochem J. 1975 Jun;147(3):549-63. PMID:1172664