Sandbox Reserved 918
From Proteopedia
(Difference between revisions)
| 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=== | ||
Revision as of 20:29, 22 March 2014
| This Sandbox is Reserved from Jan 06, 2014, through Aug 22, 2014 for use by the Biochemistry II class at the Butler University at Indianapolis, IN USA taught by R. Jeremy Johnson. This reservation includes Sandbox Reserved 911 through Sandbox Reserved 922. |
To get started:
More help: Help:Editing |
Contents |
Dipeptidyl Peptidase IV
Image:DPP4 image.png
Ribbon diagram of DPP IV from PDB 1PFQ
Introduction
Dipeptidyl Peptidase IV (commonly abbreviated as DPP IV) is a regulatory protease and binding 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 2-Naphthylamine off of 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. [1]
Structure
Medical Relevancy
References
- ↑ 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
