Pepsin: Difference between revisions
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==Protein Function== | ==Protein Function== | ||
Pepsin is one of three proteolytic, or protein degrading enzymes in the digestive system. It resides in the alimentary canal, and is produced by mucosal cells, as an inactive precursor pepsinogen. Once it is secreted into the acidic conditions of the stomachs lumen, the propart peptide is cleaved, yielding the active pepsin. Pepsin degrades peptides, and is optimally active at low pHs <ref name="Xray">PMID: 2115088</ref>. Pepsin is an aspartic proteinase, more specifically a eukaryotic aspartic protease enzyme. Pepsin was among the first enzymes to be isolated in crystalline form <ref name="flexible">PMID: 2217165</ref>. Aspartic proteinases are widespread in nature, and pepsin in particular has been known to be medically important <ref name="native">The prosegment catalyzed pepsin folding to a kinetically trapped native state. Biochemistry 49:365-371</ref>. | Pepsin is one of three proteolytic, or protein degrading enzymes in the digestive system. It resides in the alimentary canal, and is produced by mucosal cells, as an inactive precursor pepsinogen. Once it is secreted into the acidic conditions of the stomachs lumen, the propart peptide is cleaved, yielding the active pepsin. Pepsin degrades peptides, and is optimally active at low pHs <ref name="Xray">PMID: 2115088</ref>. Pepsin is an aspartic proteinase, more specifically a eukaryotic aspartic protease enzyme. Pepsin was among the first enzymes to be isolated in crystalline form <ref name="flexible">PMID: 2217165</ref>. Aspartic proteinases are widespread in nature, and pepsin in particular has been known to be medically important <ref name="native">The prosegment catalyzed pepsin folding to a kinetically trapped native state. Biochemistry 49:365-371</ref>. '''Endothiapepsin''' (ETPep) hydrolyzes proteins with preference to hydrophobic residues at P1 and P1' positions. | ||
==Overall Structure== | ==Overall Structure== | ||
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==3D structures of pepsin== | ==3D structures of pepsin== | ||
''Updated | ''Updated June 2012'' | ||
===Pepsin=== | ===Pepsin=== | ||
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[[2vs2]], [[1gkt]] - CpPep + inhibitor - neutron | [[2vs2]], [[1gkt]] - CpPep + inhibitor - neutron | ||
==Endothiapepsin=== | |||
[[1er8]], [[3er3]], [[4er1]], [[4ape]], [[1ent]] – CpPep – ''Cryphonectria parasitica''<br /> | |||
[[3lzy]], [[1oew]] – CpPep residues 90-419<br /> | |||
[[3urj]] - ETPep – ''Endothia parasitica''<br /> | |||
[[3pb5]], [[3pbd]], [[3pbz]], [[3pcw]], [[3pgi]], [[3pi0]], [[3pld]], [[3pll]], [[3pm4]], [[3pmu]], [[3pmy]] – CpETPep + fragment chemotype<br /> | |||
[[3pcz]] – CpETPep + benzamidine<br /> | |||
[[3prs]], [[3pww]] – CpETPep + antiviral drug<br /> | |||
[[3psy]] – CpETPep + inhibitor<br /> | |||
[[3q6y]]- CpETPep + pyrrolidine derivative<br /> | |||
[[3uri]], [[3url]] - CpETPep + polypeptide | |||
