Penicillopepsin

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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.

Structural highlights

  • Binding site.
  • Binding site cleft.

Glycosylated penicillopepsin complex with peptide analog and sulfate, 1ppm

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3D structures of penicillopepsin

Updated on 18-July-2024

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

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Michal Harel, Alexander Berchansky

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