Sandbox Reserved 918: Difference between revisions
No edit summary |
No edit summary |
||
| Line 11: | Line 11: | ||
'''Dipeptidyl Peptidase IV''' (commonly abbreviated as '''DPP IV''' or '''CD26''') is a regulatory [http://en.wikipedia.org/wiki/Protease protease] and binding [http://en.wikipedia.org/wiki/Glycoprotein glycoprotein] that carries out numerous functions in humans. DPP IV, discovered by V.K. Hopsu-Havu and G.G. Glenner in homogenized rat liver tissue<ref name="regpeps">PMID: 10588446</ref>, 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 showed that it serves a more generic function as a [http://en.wikipedia.org/wiki/Hydrolase hydrolase] (a serine [http://en.wikipedia.org/wiki/Exopeptidase exopeptidase]), primarily cleaving N-terminal Xaa-Pro bonds, but also capable of cleaving N-terminal Xaa-Ala bonds. DPP IV is the founding member of the DPP-IV and/or structure homologue (DASH) family, who all share this serine protease catalysis of post-proline peptide bonds. <ref> PMID: 16186403</ref> These penultimate [http://en.wikipedia.org/wiki/Proline 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] in their respective proteins, making DPP IV a unique protease for its ability to cleave this site.<ref name="Gorrell"/> | '''Dipeptidyl Peptidase IV''' (commonly abbreviated as '''DPP IV''' or '''CD26''') is a regulatory [http://en.wikipedia.org/wiki/Protease protease] and binding [http://en.wikipedia.org/wiki/Glycoprotein glycoprotein] that carries out numerous functions in humans. DPP IV, discovered by V.K. Hopsu-Havu and G.G. Glenner in homogenized rat liver tissue<ref name="regpeps">PMID: 10588446</ref>, 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 showed that it serves a more generic function as a [http://en.wikipedia.org/wiki/Hydrolase hydrolase] (a serine [http://en.wikipedia.org/wiki/Exopeptidase exopeptidase]), primarily cleaving N-terminal Xaa-Pro bonds, but also capable of cleaving N-terminal Xaa-Ala bonds. DPP IV is the founding member of the DPP-IV and/or structure homologue (DASH) family, who all share this serine protease catalysis of post-proline peptide bonds. <ref> PMID: 16186403</ref> These penultimate [http://en.wikipedia.org/wiki/Proline 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] in their respective proteins, making DPP IV a unique protease for its ability to cleave this site.<ref name="Gorrell"/> | ||
DPP IV also serves as a binding glycoprotein on the membrane of cells, binding ligands such as [http://en.wikipedia.org/wiki/Adenosine_deaminase adenosine deaminase] with high affinity.<ref name="Gorrell"/> Though this interaction currently has no known significance | DPP IV also serves as a binding glycoprotein on the membrane of cells, binding ligands such as [http://en.wikipedia.org/wiki/Adenosine_deaminase adenosine deaminase] with high affinity.<ref name="Gorrell"/> Though this interaction currently has no known significance, DPP IV and its ability to catalyze N-terminal prolines gives it a unique specificity and target for pharmaceutical companies. <ref name="regpeps">PMID: 10588446</ref> | ||
---- | ---- | ||