Sandbox Reserved 918: Difference between revisions

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===Introduction===

'''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/Glycoprotein glycoprotein] 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 [http://en.wikipedia.org/wiki/Exopeptidase exopeptidase]), breaking N-terminal Xaa-Pro bonds (though it can also catalyze alanine 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] 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 name="regpeps">PMID: 10588446</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/Glycoprotein glycoprotein] 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 [http://en.wikipedia.org/wiki/Exopeptidase exopeptidase]), breaking N-terminal Xaa-Pro bonds (though it can also catalyze alanine 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] of their respective proteins. Also, DPP IV 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 has no known significance as of yet, DPP IV and its ability to catalyze N-terminal prolines gives it a unique specificity and target for pharmaceutical companies to take advantage of. <ref name="regpeps">PMID: 10588446</ref>

----

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|} <ref name="Gorrell"/>

These substrates, along with many others, are cleaved by DPP IV at its active site containing a catalytic triad composed of <scene name='57/573132/1x70_catalytictriad/1'>Ser630, His740, and Asp708.</scene>.

These substrates, along with many others, are cleaved by DPP IV at its active site containing a catalytic triad composed of <scene name='57/573132/1x70_catalytictriad/1'>Ser630, His740, and Asp708</scene>.

</StructureSection>

Sandbox Reserved 918: Difference between revisions

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@@ Line 9: / Line 9: @@
 ===Introduction===
-'''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/Glycoprotein glycoprotein] 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 [http://en.wikipedia.org/wiki/Exopeptidase exopeptidase]), breaking  N-terminal Xaa-Pro bonds (though it can also catalyze alanine 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] 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 name="regpeps">PMID: 10588446</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/Glycoprotein glycoprotein] 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 [http://en.wikipedia.org/wiki/Exopeptidase exopeptidase]), breaking  N-terminal Xaa-Pro bonds (though it can also catalyze alanine 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] of their respective proteins. Also, DPP IV 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 has no known significance as of yet, DPP IV and its ability to catalyze N-terminal prolines gives it a unique specificity and target for pharmaceutical companies to take advantage of. <ref name="regpeps">PMID: 10588446</ref>
+----
 <StructureSection load='1X70' size='350' frame='true' align='right' caption='Biological Dimer of DPP IV' scene='57/573132/1x70_basic_dimer/1'>
@@ Line 38: / Line 42: @@
 |} <ref name="Gorrell"/>
-These substrates, along with many others, are cleaved by DPP IV at its active site containing a catalytic triad composed of <scene name='57/573132/1x70_catalytictriad/1'>Ser630, His740, and Asp708.</scene>.
+These substrates, along with many others, are cleaved by DPP IV at its active site containing a catalytic triad composed of <scene name='57/573132/1x70_catalytictriad/1'>Ser630, His740, and Asp708</scene>.
 </StructureSection>