4y06

Structural highlights

Function

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).^{[1] [2] [3]}

References

1. ↑ Suzuki Y, Sakamoto Y, Tanaka N, Okada H, Morikawa Y, Ogasawara W. Identification of the catalytic triad of family S46 exopeptidases, closely related to clan PA endopeptidases. Sci Rep. 2014 Mar 6;4:4292. PMID:24598890 doi:10.1038/srep04292
2. ↑ Sakamoto Y, Suzuki Y, Iizuka I, Tateoka C, Roppongi S, Fujimoto M, Inaka K, Tanaka H, Masaki M, Ohta K, Okada H, Nonaka T, Morikawa Y, Nakamura KT, Ogasawara W, Tanaka N. S46 peptidases are the first exopeptidases to be members of clan PA. Sci Rep. 2014 May 15;4:4977. doi: 10.1038/srep04977. PMID:24827749 doi:http://dx.doi.org/10.1038/srep04977
3. ↑ Ogasawara W, Kobayashi G, Okada H, Morikawa Y. Two types of novel dipeptidyl aminopeptidases from Pseudomonas sp. strain WO24. J Bacteriol. 1996 Nov;178(21):6288-95. PMID:8892831 doi:10.1128/jb.178.21.6288-6295.1996
4. ↑ Sakamoto Y, Suzuki Y, Iizuka I, Tateoka C, Roppongi S, Fujimoto M, Inaka K, Tanaka H, Yamada M, Ohta K, Gouda H, Nonaka T, Ogasawara W, Tanaka N. Structural and mutational analyses of dipeptidyl peptidase 11 from Porphyromonas gingivalis reveal the molecular basis for strict substrate specificity. Sci Rep. 2015 Jun 9;5:11151. doi: 10.1038/srep11151. PMID:26057589 doi:http://dx.doi.org/10.1038/srep11151