Penicillopepsin

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Revision as of 09:04, 28 August 2017

spinqualitylabelsall models Glycosylated penicillopepsin complex with peptide analog and sulfate, 1ppm Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image 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 . .

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