Sandbox Reserved 918: Difference between revisions
From Proteopedia
Jump to navigationJump to search
No edit summary |
No edit summary |
||
| Line 6: | Line 6: | ||
==Dipeptidyl Peptidase IV== | ==Dipeptidyl Peptidase IV== | ||
[[Image:DPP4_image.png|300px|right|thumb|<font size="3.5"><div style="text-align: center;"> [ | [[Image:DPP4_image.png|300px|right|thumb|<font size="3.5"><div style="text-align: center;"> [http://en.wikipedia.org/wiki/Ribbon_diagram Ribbon diagram] of DPP IV from PDB [http://www.rcsb.org/pdb/explore/explore.do?structureId=1PFQ 1PFQ] </div></font>]] | ||
===Introduction=== | ===Introduction=== | ||
'''Dipeptidyl Peptidase IV''' (commonly abbreviated as '''DPP IV''') is a regulatory protease and binding [http://en.wikipedia.org/wiki/Protein protein] that carries out numerous functions in humans making it a prime candidate for medicinal and pharmaceutical research. DPP IV, discovered by V.K. Hopsu-Havu and G.G. Glenner in homogenized rat liver tissue, was originally believed to serve a specific role in breaking [http://en.wikipedia.org/wiki/2-Naphthylamine 2-Naphthylamine] off of [http://brenda-enzymes.org/php/ligand_flatfile.php4?brenda_ligand_id=228740 Gly-Pro-2-napthylamide], hence its original name glycylproline napthylamidase. However, further research into the specificity of DPP IV eventually showed that it serves a more generic function as a hydrolase (a serine exopeptidase), breaking N-terminal Xaa-Pro bonds. These penultimate prolines of the N-terminus are known for their ability to resist attacks from most proteases and also induce a conformational change of their respective proteins. Therefore, DPP IV and its ability to catalyze said prolines gives it a unique specificity and target for pharmaceutical companies to take advantage of. <ref> Mentlein, R. (1999). Dipeptidyl-peptidase IV (CD26)--role in the inactivation of regulatory peptides. Regulatory Peptides, 85(1), 9–24. http://www.sciencedirect.com/science/article/pii/S0167011599000890 </ref> | '''Dipeptidyl Peptidase IV''' (commonly abbreviated as '''DPP IV''') is a regulatory [http://en.wikipedia.org/wiki/Protease protease] and binding [http://en.wikipedia.org/wiki/Protein protein] that carries out numerous functions in humans making it a prime candidate for medicinal and pharmaceutical research. DPP IV, discovered by V.K. Hopsu-Havu and G.G. Glenner in homogenized rat liver tissue, was originally believed to serve a specific role in breaking [http://en.wikipedia.org/wiki/2-Naphthylamine 2-Naphthylamine] off of [http://brenda-enzymes.org/php/ligand_flatfile.php4?brenda_ligand_id=228740 Gly-Pro-2-napthylamide], hence its original name glycylproline napthylamidase. However, further research into the specificity of DPP IV eventually showed that it serves a more generic function as a [http://en.wikipedia.org/wiki/Hydrolase hydrolase] (a serine exopeptidase), breaking N-terminal Xaa-Pro bonds. These penultimate prolines of the [http://en.wikipedia.org/wiki/N-terminus N-terminus] are known for their ability to resist attacks from most proteases and also induce a [http://en.wikipedia.org/wiki/Conformational_change conformational change] of their respective proteins. Therefore, DPP IV and its ability to catalyze said prolines gives it a unique specificity and target for pharmaceutical companies to take advantage of. <ref> Mentlein, R. (1999). Dipeptidyl-peptidase IV (CD26)--role in the inactivation of regulatory peptides. Regulatory Peptides, 85(1), 9–24. http://www.sciencedirect.com/science/article/pii/S0167011599000890 </ref> | ||
===Structure=== | ===Structure=== | ||
