Penicillopepsin

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Current revision (08:56, 18 July 2024) (edit) (undo)
 
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{{STRUCTURE_1ppm| PDB=1ppm | SIZE=400| SCENE= |right| CAPTION=Glycosylated penicillopepsin complex with peptide analog and sulfate, [[1ppm]] }}
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<StructureSection load='1ppm' size='400' side='right' scene='49/493723/Cv/1' caption='Glycosylated penicillopepsin complex with peptide analog and sulfate, [[1ppm]]' pspeed='8'>
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== Function ==
== 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<ref>PMID:1172664</ref>.
'''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<ref>PMID:1172664</ref>.
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PP causes clotting in milk and activates trypsinogen.
PP causes clotting in milk and activates trypsinogen.
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== Structural highlights ==
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*<scene name='49/493723/Cv/3'>Binding site</scene>.
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*<scene name='49/493723/Cv/4'>Binding site cleft</scene>.
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</StructureSection>
==3D structures of penicillopepsin==
==3D structures of penicillopepsin==
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Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
[[3app]] – PjPP – ''Penicillium janthinellum''<br />
[[3app]] – PjPP – ''Penicillium janthinellum''<br />

Current revision

Glycosylated penicillopepsin complex with peptide analog and sulfate, 1ppm

Drag the structure with the mouse to rotate

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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