Penicillopepsin
From Proteopedia
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| - | + | <StructureSection load='1ppm' size='400' side='right' scene='' caption='Glycosylated penicillopepsin complex with peptide analog and sulfate, [[1ppm]]'> | |
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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. | ||
| + | == Structural highlights == | ||
| + | </StructureSection> | ||
==3D structures of penicillopepsin== | ==3D structures of penicillopepsin== | ||
Revision as of 08:42, 28 August 2017
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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
