3won: Difference between revisions

Line 9:

</table>

== Function ==

[https://www.uniprot.org/uniprot/DAPB2_PSEMX DAPB2_PSEMX] Exopeptidase that catalyzes the removal of dipeptide units (NH2-P2-P1-) from the free amino termini of oligopeptides and small proteins (PubMed:24598890, PubMed:~~8892831~~, PubMed:~~24827749~~). Peptide digestion is sequential and substrate recognition is non-specific, with the exception that Pro is not suitable as a P1 residue (PubMed:24827749). Removes many residues of bioactive oligopeptides such as angiotensin I and neuromedin N and cleaves also oxidized insulin B chain. Able to hydrolyze an X-Pro bond, an imido bond. No endopeptidase activity (PubMed:8892831). May play a physiological role in feeding (PubMed:24598890).<ref>PMID:24598890</ref> <ref>PMID:24827749</ref> <ref>PMID:8892831</ref>

[https://www.uniprot.org/uniprot/DAPB2_PSEMX DAPB2_PSEMX] Exopeptidase that catalyzes the removal of dipeptide units (NH2-P2-P1-) from the free amino termini of oligopeptides and small proteins (PubMed:24598890, PubMed:24827749, PubMed:8892831). Peptide digestion is sequential and substrate recognition is non-specific, with the exception that Pro is not suitable as a P1 residue (PubMed:24827749). Removes many residues of bioactive oligopeptides such as angiotensin I and neuromedin N and cleaves also oxidized insulin B chain. Able to hydrolyze an X-Pro bond, an imido bond. No endopeptidase activity (PubMed:8892831). May play a physiological role in feeding (PubMed:24598890).<ref>PMID:24598890</ref> <ref>PMID:24827749</ref> <ref>PMID:8892831</ref>

== Publication Abstract from PubMed ==

Navigation menu

Page actions

Page actions

Personal tools

Navigation

Search

Tools

@@ Line 9: / Line 9: @@
 </table>
 == Function ==
-[https://www.uniprot.org/uniprot/DAPB2_PSEMX DAPB2_PSEMX] Exopeptidase that catalyzes the removal of dipeptide units (NH2-P2-P1-) from the free amino termini of oligopeptides and small proteins (PubMed:24598890, PubMed:8892831, PubMed:24827749). Peptide digestion is sequential and substrate recognition is non-specific, with the exception that Pro is not suitable as a P1 residue (PubMed:24827749). Removes many residues of bioactive oligopeptides such as angiotensin I and neuromedin N and cleaves also oxidized insulin B chain. Able to hydrolyze an X-Pro bond, an imido bond. No endopeptidase activity (PubMed:8892831). May play a physiological role in feeding (PubMed:24598890).<ref>PMID:24598890</ref> <ref>PMID:24827749</ref> <ref>PMID:8892831</ref>
+[https://www.uniprot.org/uniprot/DAPB2_PSEMX DAPB2_PSEMX] Exopeptidase that catalyzes the removal of dipeptide units (NH2-P2-P1-) from the free amino termini of oligopeptides and small proteins (PubMed:24598890, PubMed:24827749, PubMed:8892831). Peptide digestion is sequential and substrate recognition is non-specific, with the exception that Pro is not suitable as a P1 residue (PubMed:24827749). Removes many residues of bioactive oligopeptides such as angiotensin I and neuromedin N and cleaves also oxidized insulin B chain. Able to hydrolyze an X-Pro bond, an imido bond. No endopeptidase activity (PubMed:8892831). May play a physiological role in feeding (PubMed:24598890).<ref>PMID:24598890</ref> <ref>PMID:24827749</ref> <ref>PMID:8892831</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==