http://52.214.119.220/wiki/index.php?action=history&feed=atom&title=Sandbox_78Sandbox 78 - Revision history2026-04-07T12:16:32ZRevision history for this page on the wikiMediaWiki 1.11.2http://52.214.119.220/wiki/index.php?title=Sandbox_78&diff=2587956&oldid=prevMegan M. Roy at 18:52, 20 April 20162016-04-20T18:52:40Z<p></p>
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<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>== Structural highlights ==</div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>== Structural highlights ==</div></td></tr>
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<tr><td class='diff-marker'>-</td><td style="background: #ffa; color:black; font-size: smaller;"><div>HGL, a dimeric [[hydrolase]] enzyme consisting of two 379 amino acid residue-long subunits, possesses a <scene name='72/728060/Catalytic_elbow/3'>Catalytic Arm</scene> that contains residues Ser-153, His-353, and Asp-324. This structure is essential to the breakdown of lipids, coordinated with an <scene name='72/728060/Arm_and_hole/1'>Oxyanion Hole</scene> at Leu-67 and Gln-154 <ref name="dogs">PMID:20965171</ref>, that serves to stabilize the transition state. Structurally, the human gastric lipase exhibits a complex <scene name='72/728060/Secondary_structure/1'>Secondary Structure</scene> (beta sheets shown in yellow, alpha helices shown in orange, coiled coils shown in green, and amino acid side chains shown as purple). The <scene name='72/728060/1hlg_lid/5'>"Lid"</scene> of <del style="color: red; font-weight: bold; text-decoration: none;">the lipase </del>at residues 215-244 <ref name="dogs">PMID:20965171</ref> gives way to the <scene name='72/728060/Hydrophobic_regions/1'>Hydrophobic Areas</scene> (hydrophobic regions noted in red) both surrounding the active site and interfacing the lid. These areas are thought to draw lipids and promote docking <ref name="roussel" />. </div></td><td class='diff-marker'>+</td><td style="background: #cfc; color:black; font-size: smaller;"><div>HGL, a dimeric [[hydrolase]] enzyme consisting of two 379 amino acid residue-long subunits, possesses a <scene name='72/728060/Catalytic_elbow/3'>Catalytic Arm</scene> that contains residues Ser-153, His-353, and Asp-324. This structure is essential to the breakdown of lipids, coordinated with an <scene name='72/728060/Arm_and_hole/1'>Oxyanion Hole</scene> at Leu-67 and Gln-154 <ref name="dogs">PMID:20965171</ref>, that serves to stabilize the transition state. Structurally, the human gastric lipase exhibits a complex <scene name='72/728060/Secondary_structure/1'>Secondary Structure</scene> (beta sheets shown in yellow, alpha helices shown in orange, coiled coils shown in green, and amino acid side chains shown as purple). The <scene name='72/728060/1hlg_lid/5'>"Lid"</scene> of <ins style="color: red; font-weight: bold; text-decoration: none;">HGL </ins>at residues 215-244 <ref name="dogs">PMID:20965171</ref> gives way to the <scene name='72/728060/Hydrophobic_regions/1'>Hydrophobic Areas</scene> (hydrophobic regions noted in red) both surrounding the active site and interfacing the lid. These areas are thought to draw lipids and promote docking <ref name="roussel" />. </div></td></tr>
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<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>== Function ==</div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>== Function ==</div></td></tr>
</table>Megan M. Royhttp://52.214.119.220/wiki/index.php?title=Sandbox_78&diff=2587955&oldid=prevMegan M. Roy at 18:51, 20 April 20162016-04-20T18:51:32Z<p></p>
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<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>== Introduction ==</div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>== Introduction ==</div></td></tr>
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<tr><td class='diff-marker'>-</td><td style="background: #ffa; color:black; font-size: smaller;"><div>Human gastric lipase (HGL, E.C. 3.1.1.3) (PBD ID: 1hlg) is the [[lipase]] that is responsible for initiating the digestion of dietary fats in the stomach <ref name="armand">PMID:7598069</ref>. This acid-stable enzyme <ref name="gastritis">PMID:23899880</ref> is secreted by the fundic chief cells of the human stomach and catalyzes 10-20% of total lipolytic processes (i.e., those involving fat breakdown) in healthy adults <ref name="armand" />. HGL specifically catalyzes the hydrolysis of triacylglycerol in order to produce diacylglycerol and a carboxylate byproduct <ref name="roussel">PMID:10358049</ref>, a process that facilitates subsequent fat breakdown by pancreatic lipase <ref name="dogs">PMID:20965171</ref>. In terms of disease implications, there is evidence to suggest that HGL secretion is altered in individuals with gastritis <ref name="gastritis" />.</div></td><td class='diff-marker'>+</td><td style="background: #cfc; color:black; font-size: smaller;"><div>Human gastric lipase (HGL, E.C. 3.1.1.3) (PBD ID: 1hlg) is the [[lipase]] that is responsible for initiating the digestion of dietary fats in the stomach <ref name="armand">PMID:7598069</ref>. This acid-stable enzyme <ref name="gastritis">PMID:23899880</ref> is secreted by the fundic chief cells of the human stomach and catalyzes 10-20% of total lipolytic processes (i.e., those involving fat breakdown) in healthy adults <ref name="armand" />. HGL specifically catalyzes the hydrolysis of triacylglycerol in order to produce diacylglycerol and a carboxylate byproduct <ref name="roussel">PMID:10358049</ref>, a process that facilitates subsequent fat breakdown by pancreatic lipase <ref name="dogs">PMID:20965171</ref>. In terms of disease implications, there is evidence to suggest that HGL secretion is altered in individuals with gastritis <ins style="color: red; font-weight: bold; text-decoration: none;">(the most common gastric condition, in which the stomach lining is inflamed) </ins><ref name="gastritis" />.</div></td></tr>
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<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>== Structural highlights ==</div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>== Structural highlights ==</div></td></tr>
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<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>== Relevance to Human Health & Disease ==</div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>== Relevance to Human Health & Disease ==</div></td></tr>
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<tr><td class='diff-marker'>-</td><td style="background: #ffa; color:black; font-size: smaller;"><div>Tomasik et al. (2013) <ref name="gastritis" /> investigated the hormonal regulation of HGL secretion in children and adolescents with gastritis <del style="color: red; font-weight: bold; text-decoration: none;">(the most common gastric condition, in which the stomach lining is inflamed)</del>. HGL activity was compared across three groups: one experimental group consisting of adolescents diagnosed with Helicobacter pylori gastritis (n = 10), another experimental group consisting of adolescents with a non-H. pylori induced form of gastritis (n = 10), and one control group of healthy adolescents (n = 14). HGL activity, in addition to plasma concentrations of glucagon-like peptide-1, cholecystokinin, and glucose-dependent insulinotropic peptide, were observed through analysis of gastric juice samples that had been collected via endoscopic measurements from each patient.</div></td><td class='diff-marker'>+</td><td style="background: #cfc; color:black; font-size: smaller;"><div>Tomasik et al. (2013) <ref name="gastritis" /> investigated the hormonal regulation of HGL secretion in children and adolescents with gastritis. HGL activity was compared across three groups: one experimental group consisting of adolescents diagnosed with <ins style="color: red; font-weight: bold; text-decoration: none;">''</ins>Helicobacter pylori<ins style="color: red; font-weight: bold; text-decoration: none;">'' </ins>gastritis (<ins style="color: red; font-weight: bold; text-decoration: none;">''</ins>n<ins style="color: red; font-weight: bold; text-decoration: none;">'' </ins>= 10), another experimental group consisting of adolescents with a non-<ins style="color: red; font-weight: bold; text-decoration: none;">''</ins>H. pylori<ins style="color: red; font-weight: bold; text-decoration: none;">'' </ins>induced form of gastritis (<ins style="color: red; font-weight: bold; text-decoration: none;">''</ins>n<ins style="color: red; font-weight: bold; text-decoration: none;">'' </ins>= 10), and one control group of healthy adolescents (<ins style="color: red; font-weight: bold; text-decoration: none;">''</ins>n<ins style="color: red; font-weight: bold; text-decoration: none;">'' </ins>= 14). HGL activity, in addition to plasma concentrations of glucagon-like peptide-1, cholecystokinin, and glucose-dependent insulinotropic peptide, were observed through analysis of gastric juice samples that had been collected via endoscopic measurements from each patient.</div></td></tr>
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<tr><td class='diff-marker'>-</td><td style="background: #ffa; color:black; font-size: smaller;"><div>Patients whose superficial gastritis was induced by pathogens other than H. pylori exhibited lower levels of HGL activity compared to both healthy adolescents (p < .005) and those who were diagnosed with H. pylori gastritis (p < .005). Mean plasma concentrations of glucose-dependent insulinotropic peptide were lower in healthy patients (p < 0.005) than in those with non-H. pylori gastritis (p < .003) and those with H. pylori gastritis (p < 0.01). Regulation of HGL secretion by glucagon-like peptide-1 and cholecystokinin was therefore found to be altered in adolescents with gastritis. In addition, glucose-dependent insulinotropic peptide was found to be a powerful activator of human gastric lipase activity in all experimental and control groups <ref name="gastritis" />.</div></td><td class='diff-marker'>+</td><td style="background: #cfc; color:black; font-size: smaller;"><div>Patients whose superficial gastritis was induced by pathogens other than <ins style="color: red; font-weight: bold; text-decoration: none;">''</ins>H. pylori<ins style="color: red; font-weight: bold; text-decoration: none;">'' </ins>exhibited lower levels of HGL activity compared to both healthy adolescents (<ins style="color: red; font-weight: bold; text-decoration: none;">''</ins>p<ins style="color: red; font-weight: bold; text-decoration: none;">'' </ins>< .005) and those who were diagnosed with <ins style="color: red; font-weight: bold; text-decoration: none;">''</ins>H. pylori<ins style="color: red; font-weight: bold; text-decoration: none;">'' </ins>gastritis (<ins style="color: red; font-weight: bold; text-decoration: none;">''</ins>p<ins style="color: red; font-weight: bold; text-decoration: none;">'' </ins>< .005). Mean plasma concentrations of glucose-dependent insulinotropic peptide were lower in healthy patients (<ins style="color: red; font-weight: bold; text-decoration: none;">''</ins>p<ins style="color: red; font-weight: bold; text-decoration: none;">'' </ins>< 0.005) than in those with non-<ins style="color: red; font-weight: bold; text-decoration: none;">''</ins>H. pylori<ins style="color: red; font-weight: bold; text-decoration: none;">'' </ins>gastritis (<ins style="color: red; font-weight: bold; text-decoration: none;">''</ins>p<ins style="color: red; font-weight: bold; text-decoration: none;">'' </ins>< .003) and those with <ins style="color: red; font-weight: bold; text-decoration: none;">''</ins>H. pylori<ins style="color: red; font-weight: bold; text-decoration: none;">'' </ins>gastritis (<ins style="color: red; font-weight: bold; text-decoration: none;">''</ins>p<ins style="color: red; font-weight: bold; text-decoration: none;">'' </ins>< 0.01). Regulation of HGL secretion by glucagon-like peptide-1 and cholecystokinin was therefore found to be altered in adolescents with gastritis. In addition, glucose-dependent insulinotropic peptide was found to be a powerful activator of human gastric lipase activity in all experimental and control groups <ref name="gastritis" />.</div></td></tr>
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<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>== References ==</div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>== References ==</div></td></tr>
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<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div><references/></div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div><references/></div></td></tr>
</table>Megan M. Royhttp://52.214.119.220/wiki/index.php?title=Sandbox_78&diff=2587954&oldid=prevMegan M. Roy at 18:46, 20 April 20162016-04-20T18:46:08Z<p></p>
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<tr><td class='diff-marker'>-</td><td style="background: #ffa; color:black; font-size: smaller;"><div>HGL, a dimeric [[hydrolase]] enzyme consisting of two 379 amino acid residue-long subunits, possesses a <scene name='72/728060/Catalytic_elbow/3'>Catalytic Arm</scene> <del style="color: red; font-weight: bold; text-decoration: none;">consisting of </del>residues Ser-153, His-353, and Asp-324 essential to the breakdown of lipids, coordinated with an <scene name='72/728060/Arm_and_hole/1'>Oxyanion Hole</scene> at Leu-67 and Gln-154 <ref name="dogs">PMID:20965171</ref>, that serves to stabilize the transition state. Structurally, the human gastric lipase exhibits a complex <scene name='72/728060/Secondary_structure/1'>Secondary Structure</scene> (beta sheets shown in yellow, alpha helices shown in orange, coiled coils shown in green, and amino acid side chains shown as purple). The <scene name='72/728060/1hlg_lid/5'>"Lid"</scene> of the lipase at residues 215-244 <ref name="dogs">PMID:20965171</ref> gives way to the <scene name='72/728060/Hydrophobic_regions/1'>Hydrophobic Areas</scene> (hydrophobic regions noted in red) both surrounding the active site and interfacing the lid. These areas are thought to draw lipids and promote docking <ref name="roussel" />. </div></td><td class='diff-marker'>+</td><td style="background: #cfc; color:black; font-size: smaller;"><div>HGL, a dimeric [[hydrolase]] enzyme consisting of two 379 amino acid residue-long subunits, possesses a <scene name='72/728060/Catalytic_elbow/3'>Catalytic Arm</scene> <ins style="color: red; font-weight: bold; text-decoration: none;">that contains </ins>residues Ser-153, His-353, and Asp-324<ins style="color: red; font-weight: bold; text-decoration: none;">. This structure is </ins>essential to the breakdown of lipids, coordinated with an <scene name='72/728060/Arm_and_hole/1'>Oxyanion Hole</scene> at Leu-67 and Gln-154 <ref name="dogs">PMID:20965171</ref>, that serves to stabilize the transition state. Structurally, the human gastric lipase exhibits a complex <scene name='72/728060/Secondary_structure/1'>Secondary Structure</scene> (beta sheets shown in yellow, alpha helices shown in orange, coiled coils shown in green, and amino acid side chains shown as purple). The <scene name='72/728060/1hlg_lid/5'>"Lid"</scene> of the lipase at residues 215-244 <ref name="dogs">PMID:20965171</ref> gives way to the <scene name='72/728060/Hydrophobic_regions/1'>Hydrophobic Areas</scene> (hydrophobic regions noted in red) both surrounding the active site and interfacing the lid. These areas are thought to draw lipids and promote docking <ref name="roussel" />. </div></td></tr>
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<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>== Function ==</div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>== Function ==</div></td></tr>
</table>Megan M. Royhttp://52.214.119.220/wiki/index.php?title=Sandbox_78&diff=2587953&oldid=prevMegan M. Roy at 18:43, 20 April 20162016-04-20T18:43:09Z<p></p>
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<tr><td class='diff-marker'>-</td><td style="background: #ffa; color:black; font-size: smaller;"><div>HGL, a dimeric enzyme consisting of two 379 amino acid residue-long subunits, possesses a <scene name='72/728060/Catalytic_elbow/3'>Catalytic Arm</scene> consisting of residues Ser-153, His-353, and Asp-324 essential to the breakdown of lipids, coordinated with an <scene name='72/728060/Arm_and_hole/1'>Oxyanion Hole</scene> at Leu-67 and Gln-154 <ref name="dogs">PMID:20965171</ref>, that serves to stabilize the transition state. Structurally, the human gastric lipase exhibits a complex <scene name='72/728060/Secondary_structure/1'>Secondary Structure</scene> (beta sheets shown in yellow, alpha helices shown in orange, coiled coils shown in green, and amino acid side chains shown as purple). The <scene name='72/728060/1hlg_lid/5'>"Lid"</scene> of the lipase at residues 215-244 <ref name="dogs">PMID:20965171</ref> gives way to the <scene name='72/728060/Hydrophobic_regions/1'>Hydrophobic Areas</scene> (hydrophobic regions noted in red) both surrounding the active site and interfacing the lid. These areas are thought to draw lipids and promote docking <ref name="roussel" />. </div></td><td class='diff-marker'>+</td><td style="background: #cfc; color:black; font-size: smaller;"><div>HGL, a dimeric <ins style="color: red; font-weight: bold; text-decoration: none;">[[hydrolase]] </ins>enzyme consisting of two 379 amino acid residue-long subunits, possesses a <scene name='72/728060/Catalytic_elbow/3'>Catalytic Arm</scene> consisting of residues Ser-153, His-353, and Asp-324 essential to the breakdown of lipids, coordinated with an <scene name='72/728060/Arm_and_hole/1'>Oxyanion Hole</scene> at Leu-67 and Gln-154 <ref name="dogs">PMID:20965171</ref>, that serves to stabilize the transition state. Structurally, the human gastric lipase exhibits a complex <scene name='72/728060/Secondary_structure/1'>Secondary Structure</scene> (beta sheets shown in yellow, alpha helices shown in orange, coiled coils shown in green, and amino acid side chains shown as purple). The <scene name='72/728060/1hlg_lid/5'>"Lid"</scene> of the lipase at residues 215-244 <ref name="dogs">PMID:20965171</ref> gives way to the <scene name='72/728060/Hydrophobic_regions/1'>Hydrophobic Areas</scene> (hydrophobic regions noted in red) both surrounding the active site and interfacing the lid. These areas are thought to draw lipids and promote docking <ref name="roussel" />. </div></td></tr>
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<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>== Function ==</div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>== Function ==</div></td></tr>
</table>Megan M. Royhttp://52.214.119.220/wiki/index.php?title=Sandbox_78&diff=2587952&oldid=prevMegan M. Roy at 18:42, 20 April 20162016-04-20T18:42:41Z<p></p>
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<tr><td class='diff-marker'>-</td><td style="background: #ffa; color:black; font-size: smaller;"><div>[[Image:Hydrolysis triacylglycerol reaction.png|400px|left|thumb| <del style="color: red; font-weight: bold; text-decoration: none;">Hydrolysis </del>of triacylglycerol<del style="color: red; font-weight: bold; text-decoration: none;">. This reaction </del>is catalyzed by HGL <ref>Adapted from [http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/enzymes/GetPage.pl?ec_number=3.1.1.3]; image generated using [https://www.emolecules.com]</ref>.]]</div></td><td class='diff-marker'>+</td><td style="background: #cfc; color:black; font-size: smaller;"><div>[[Image:Hydrolysis triacylglycerol reaction.png|400px|left|thumb| <ins style="color: red; font-weight: bold; text-decoration: none;">The hydrolysis </ins>of triacylglycerol <ins style="color: red; font-weight: bold; text-decoration: none;">that </ins>is catalyzed by HGL <ref>Adapted from [http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/enzymes/GetPage.pl?ec_number=3.1.1.3]; image generated using [https://www.emolecules.com]</ref>.]]</div></td></tr>
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<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>HGL functions at an optimal pH of approximately five, and primarily catalyzes the hydrolysis of short-chain triacylglycerols <ref name="kinetic assay">PMID:3743968</ref>.</div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>HGL functions at an optimal pH of approximately five, and primarily catalyzes the hydrolysis of short-chain triacylglycerols <ref name="kinetic assay">PMID:3743968</ref>.</div></td></tr>
<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"></td></tr>
<tr><td class='diff-marker'>-</td><td style="background: #ffa; color:black; font-size: smaller;"><div>As an esterase with a catalytically active serine, HGL exhibits <del style="color: red; font-weight: bold; text-decoration: none;">an </del>established serine esterase mechanism. The active serine, located within the <scene name='72/728060/Catalytic_elbow/3'>Catalytic Arm</scene>, is facilitated first by the neighboring formation of a salt bridge between Asp-136 and His-152, which induces the appropriation of a proton from Ser-153. The now highly nucleophilic Ser-153 will attack the carbonyl carbon of the acetate group in a triacylglycerol molecule. The <del style="color: red; font-weight: bold; text-decoration: none;">now </del>tetrahedral species<del style="color: red; font-weight: bold; text-decoration: none;">, </del>stabilized by the oxyanion hole<del style="color: red; font-weight: bold; text-decoration: none;">; however</del>, as soon as the species disassembles into the covalently bonded acetate and lipase, <del style="color: red; font-weight: bold; text-decoration: none;">and </del>the serine undergoes deacylation <del style="color: red; font-weight: bold; text-decoration: none;">where </del>water acts <del style="color: red; font-weight: bold; text-decoration: none;">at </del>the <del style="color: red; font-weight: bold; text-decoration: none;">hydroxyl group</del>. This final step restores Ser-153 to its protonated state<ref name="esterase">PMID:23209280</ref>. </div></td><td class='diff-marker'>+</td><td style="background: #cfc; color:black; font-size: smaller;"><div>As an esterase with a catalytically active serine, HGL exhibits <ins style="color: red; font-weight: bold; text-decoration: none;">a mechanism resembling the </ins>established serine esterase mechanism. The active <ins style="color: red; font-weight: bold; text-decoration: none;">site </ins>serine, located within the <scene name='72/728060/Catalytic_elbow/3'>Catalytic Arm</scene>, is facilitated first by the neighboring formation of a salt bridge between Asp-136 and His-152, which induces the appropriation of a proton from Ser-153. The now highly nucleophilic Ser-153 will attack the carbonyl carbon of the acetate group in a triacylglycerol molecule. The tetrahedral species <ins style="color: red; font-weight: bold; text-decoration: none;">is </ins>stabilized by the oxyanion hole<ins style="color: red; font-weight: bold; text-decoration: none;">. However</ins>, as soon as the species disassembles into the covalently bonded acetate and lipase, the serine undergoes deacylation <ins style="color: red; font-weight: bold; text-decoration: none;">in which </ins>water acts <ins style="color: red; font-weight: bold; text-decoration: none;">as </ins>the <ins style="color: red; font-weight: bold; text-decoration: none;">nucleophile</ins>. This final step restores Ser-153 to its protonated state <ref name="esterase">PMID:23209280</ref>. </div></td></tr>
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<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>== Relevance to Human Health & Disease ==</div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>== Relevance to Human Health & Disease ==</div></td></tr>
<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"></td></tr>
<tr><td class='diff-marker'>-</td><td style="background: #ffa; color:black; font-size: smaller;"><div>Tomasik et al. (2013) <ref name="gastritis" /> investigated the hormonal regulation of <del style="color: red; font-weight: bold; text-decoration: none;">human gastric lipase </del>secretion in children and adolescents with gastritis <del style="color: red; font-weight: bold; text-decoration: none;">-- </del>the most common gastric condition, in which <del style="color: red; font-weight: bold; text-decoration: none;">inflammation occurs in </del>the lining <del style="color: red; font-weight: bold; text-decoration: none;">of the stomach -- as there </del>is <del style="color: red; font-weight: bold; text-decoration: none;">little existing literature regarding this subject</del>. HGL activity was compared across three groups: one experimental group consisting of adolescents diagnosed with Helicobacter pylori gastritis (n = 10), another experimental group consisting of adolescents with a non-H. pylori induced form of gastritis (n = 10), and one control group of healthy adolescents (n = 14). HGL activity, in addition to plasma concentrations of glucagon-like peptide-1, cholecystokinin, and glucose-dependent insulinotropic peptide, were observed through analysis of gastric juice samples that had been collected via endoscopic measurements from each patient.</div></td><td class='diff-marker'>+</td><td style="background: #cfc; color:black; font-size: smaller;"><div>Tomasik et al. (2013) <ref name="gastritis" /> investigated the hormonal regulation of <ins style="color: red; font-weight: bold; text-decoration: none;">HGL </ins>secretion in children and adolescents with gastritis <ins style="color: red; font-weight: bold; text-decoration: none;">(</ins>the most common gastric condition, in which the <ins style="color: red; font-weight: bold; text-decoration: none;">stomach </ins>lining is <ins style="color: red; font-weight: bold; text-decoration: none;">inflamed)</ins>. HGL activity was compared across three groups: one experimental group consisting of adolescents diagnosed with Helicobacter pylori gastritis (n = 10), another experimental group consisting of adolescents with a non-H. pylori induced form of gastritis (n = 10), and one control group of healthy adolescents (n = 14). HGL activity, in addition to plasma concentrations of glucagon-like peptide-1, cholecystokinin, and glucose-dependent insulinotropic peptide, were observed through analysis of gastric juice samples that had been collected via endoscopic measurements from each patient.</div></td></tr>
<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"></td></tr>
<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>Patients whose superficial gastritis was induced by pathogens other than H. pylori exhibited lower levels of HGL activity compared to both healthy adolescents (p < .005) and those who were diagnosed with H. pylori gastritis (p < .005). Mean plasma concentrations of glucose-dependent insulinotropic peptide were lower in healthy patients (p < 0.005) than in those with non-H. pylori gastritis (p < .003) and those with H. pylori gastritis (p < 0.01). Regulation of HGL secretion by glucagon-like peptide-1 and cholecystokinin was therefore found to be altered in adolescents with gastritis. In addition, glucose-dependent insulinotropic peptide was found to be a powerful activator of human gastric lipase activity in all experimental and control groups <ref name="gastritis" />.</div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>Patients whose superficial gastritis was induced by pathogens other than H. pylori exhibited lower levels of HGL activity compared to both healthy adolescents (p < .005) and those who were diagnosed with H. pylori gastritis (p < .005). Mean plasma concentrations of glucose-dependent insulinotropic peptide were lower in healthy patients (p < 0.005) than in those with non-H. pylori gastritis (p < .003) and those with H. pylori gastritis (p < 0.01). Regulation of HGL secretion by glucagon-like peptide-1 and cholecystokinin was therefore found to be altered in adolescents with gastritis. In addition, glucose-dependent insulinotropic peptide was found to be a powerful activator of human gastric lipase activity in all experimental and control groups <ref name="gastritis" />.</div></td></tr>
</table>Megan M. Royhttp://52.214.119.220/wiki/index.php?title=Sandbox_78&diff=2587949&oldid=prevMegan M. Roy at 18:33, 20 April 20162016-04-20T18:33:25Z<p></p>
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<tr><td class='diff-marker'>-</td><td style="background: #ffa; color:black; font-size: smaller;"><div>HGL, a dimeric enzyme consisting of two 379 amino acid residue-long subunits, possesses a <scene name='72/728060/Catalytic_elbow/3'>Catalytic Arm</scene> consisting of residues Ser-153, His-353, and Asp-324 essential to the breakdown of lipids, coordinated with an <scene name='72/728060/Arm_and_hole/1'>Oxyanion Hole</scene> at Leu-67 and Gln-154 <ref name="dogs">PMID:20965171</ref>, that serves to stabilize the transition state. Structurally, the human gastric lipase exhibits a complex <scene name='72/728060/Secondary_structure/1'>Secondary Structure</scene> (beta sheets shown in yellow, alpha helices shown in orange, coiled coils shown in green, and amino acid side chains shown as purple). The <scene name='72/728060/1hlg_lid/<del style="color: red; font-weight: bold; text-decoration: none;">4</del>'>"Lid"</scene> of the lipase at residues 215-244 <ref name="dogs">PMID:20965171</ref> gives way to the <scene name='72/728060/Hydrophobic_regions/1'>Hydrophobic Areas</scene> (hydrophobic regions noted in red) both surrounding the active site and interfacing the lid. These areas are thought to draw lipids and promote docking <ref name="roussel" />. </div></td><td class='diff-marker'>+</td><td style="background: #cfc; color:black; font-size: smaller;"><div>HGL, a dimeric enzyme consisting of two 379 amino acid residue-long subunits, possesses a <scene name='72/728060/Catalytic_elbow/3'>Catalytic Arm</scene> consisting of residues Ser-153, His-353, and Asp-324 essential to the breakdown of lipids, coordinated with an <scene name='72/728060/Arm_and_hole/1'>Oxyanion Hole</scene> at Leu-67 and Gln-154 <ref name="dogs">PMID:20965171</ref>, that serves to stabilize the transition state. Structurally, the human gastric lipase exhibits a complex <scene name='72/728060/Secondary_structure/1'>Secondary Structure</scene> (beta sheets shown in yellow, alpha helices shown in orange, coiled coils shown in green, and amino acid side chains shown as purple). The <scene name='72/728060/1hlg_lid/<ins style="color: red; font-weight: bold; text-decoration: none;">5</ins>'>"Lid"</scene> of the lipase at residues 215-244 <ref name="dogs">PMID:20965171</ref> gives way to the <scene name='72/728060/Hydrophobic_regions/1'>Hydrophobic Areas</scene> (hydrophobic regions noted in red) both surrounding the active site and interfacing the lid. These areas are thought to draw lipids and promote docking <ref name="roussel" />. </div></td></tr>
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<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>== Function ==</div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>== Function ==</div></td></tr>
</table>Megan M. Royhttp://52.214.119.220/wiki/index.php?title=Sandbox_78&diff=2587948&oldid=prevMegan M. Roy at 18:32, 20 April 20162016-04-20T18:32:04Z<p></p>
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<tr><td class='diff-marker'>-</td><td style="background: #ffa; color:black; font-size: smaller;"><div>HGL, a dimeric enzyme consisting of two 379 amino acid residue-long subunits, possesses a <scene name='72/728060/Catalytic_elbow/3'>Catalytic Arm</scene> consisting of residues Ser-153, His-353, and Asp-324 essential to the breakdown of lipids, coordinated with an <scene name='72/728060/Arm_and_hole/1'>Oxyanion Hole</scene> at Leu-67 and Gln-154 <ref name="dogs">PMID:20965171</ref>, that serves to stabilize the transition state. Structurally, the human gastric lipase exhibits a complex <scene name='72/728060/Secondary_structure/1'>Secondary Structure</scene> (beta sheets shown in yellow, alpha helices shown in orange, coiled coils shown in green, and amino acid side chains shown as purple). The <scene name='72/728060/1hlg_lid/<del style="color: red; font-weight: bold; text-decoration: none;">3</del>'>"Lid"</scene> of the lipase at residues 215-244 <ref name="dogs">PMID:20965171</ref> gives way to the <scene name='72/728060/Hydrophobic_regions/1'>Hydrophobic Areas</scene> (hydrophobic regions noted in red) both surrounding the active site and interfacing the lid. These areas are thought to draw lipids and promote docking <ref name="roussel" />. </div></td><td class='diff-marker'>+</td><td style="background: #cfc; color:black; font-size: smaller;"><div>HGL, a dimeric enzyme consisting of two 379 amino acid residue-long subunits, possesses a <scene name='72/728060/Catalytic_elbow/3'>Catalytic Arm</scene> consisting of residues Ser-153, His-353, and Asp-324 essential to the breakdown of lipids, coordinated with an <scene name='72/728060/Arm_and_hole/1'>Oxyanion Hole</scene> at Leu-67 and Gln-154 <ref name="dogs">PMID:20965171</ref>, that serves to stabilize the transition state. Structurally, the human gastric lipase exhibits a complex <scene name='72/728060/Secondary_structure/1'>Secondary Structure</scene> (beta sheets shown in yellow, alpha helices shown in orange, coiled coils shown in green, and amino acid side chains shown as purple). The <scene name='72/728060/1hlg_lid/<ins style="color: red; font-weight: bold; text-decoration: none;">4</ins>'>"Lid"</scene> of the lipase at residues 215-244 <ref name="dogs">PMID:20965171</ref> gives way to the <scene name='72/728060/Hydrophobic_regions/1'>Hydrophobic Areas</scene> (hydrophobic regions noted in red) both surrounding the active site and interfacing the lid. These areas are thought to draw lipids and promote docking <ref name="roussel" />. </div></td></tr>
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<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>== Function ==</div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>== Function ==</div></td></tr>
</table>Megan M. Royhttp://52.214.119.220/wiki/index.php?title=Sandbox_78&diff=2587947&oldid=prevMegan M. Roy at 18:30, 20 April 20162016-04-20T18:30:31Z<p></p>
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<tr><td class='diff-marker'>-</td><td style="background: #ffa; color:black; font-size: smaller;"><div>HGL, a dimeric enzyme consisting of two 379 amino acid residue-long subunits, possesses a <scene name='72/728060/Catalytic_elbow/3'>Catalytic Arm</scene> consisting of residues Ser-153, His-353, and Asp-324 essential to the breakdown of lipids, coordinated with an <scene name='72/728060/Arm_and_hole/1'>Oxyanion Hole</scene> at Leu-67 and Gln-154 <ref name="dogs">PMID:20965171</ref>, that serves to stabilize the transition state. Structurally, the human gastric lipase exhibits a complex <scene name='72/728060/Secondary_structure/1'>Secondary Structure</scene> (beta sheets shown in yellow, alpha helices shown in orange, coiled coils shown in green, and amino acid side chains shown as purple). The <scene name='72/728060/1hlg_lid/<del style="color: red; font-weight: bold; text-decoration: none;">2</del>'>"Lid"</scene> of the lipase at residues 215-244 <ref name="dogs">PMID:20965171</ref> gives way to the <scene name='72/728060/Hydrophobic_regions/1'>Hydrophobic Areas</scene> (hydrophobic regions noted in red) both surrounding the active site and interfacing the lid. These areas are thought to draw lipids and promote docking <ref name="roussel" />. </div></td><td class='diff-marker'>+</td><td style="background: #cfc; color:black; font-size: smaller;"><div>HGL, a dimeric enzyme consisting of two 379 amino acid residue-long subunits, possesses a <scene name='72/728060/Catalytic_elbow/3'>Catalytic Arm</scene> consisting of residues Ser-153, His-353, and Asp-324 essential to the breakdown of lipids, coordinated with an <scene name='72/728060/Arm_and_hole/1'>Oxyanion Hole</scene> at Leu-67 and Gln-154 <ref name="dogs">PMID:20965171</ref>, that serves to stabilize the transition state. Structurally, the human gastric lipase exhibits a complex <scene name='72/728060/Secondary_structure/1'>Secondary Structure</scene> (beta sheets shown in yellow, alpha helices shown in orange, coiled coils shown in green, and amino acid side chains shown as purple). The <scene name='72/728060/1hlg_lid/<ins style="color: red; font-weight: bold; text-decoration: none;">3</ins>'>"Lid"</scene> of the lipase at residues 215-244 <ref name="dogs">PMID:20965171</ref> gives way to the <scene name='72/728060/Hydrophobic_regions/1'>Hydrophobic Areas</scene> (hydrophobic regions noted in red) both surrounding the active site and interfacing the lid. These areas are thought to draw lipids and promote docking <ref name="roussel" />. </div></td></tr>
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<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>== Function ==</div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>== Function ==</div></td></tr>
</table>Megan M. Royhttp://52.214.119.220/wiki/index.php?title=Sandbox_78&diff=2587946&oldid=prevMegan M. Roy at 18:26, 20 April 20162016-04-20T18:26:21Z<p></p>
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<tr><td class='diff-marker'>-</td><td style="background: #ffa; color:black; font-size: smaller;"><div>HGL, a dimeric enzyme consisting of two 379 amino acid residue-long subunits, possesses a <scene name='72/728060/Catalytic_elbow/3'>Catalytic Arm</scene> consisting of residues Ser-153, His-353, and Asp-324 essential to the breakdown of lipids, coordinated with an <scene name='72/728060/Arm_and_hole/1'>Oxyanion Hole</scene> at Leu-67 and Gln-154 <ref name="dogs">PMID:20965171</ref>, that serves to stabilize the transition state. Structurally, the human gastric lipase exhibits a complex <scene name='72/728060/Secondary_structure/1'>Secondary Structure</scene> (beta sheets shown in yellow, alpha helices shown in orange, coiled coils shown in green, and amino acid side chains shown as purple). The "<del style="color: red; font-weight: bold; text-decoration: none;">lid</del>" of the lipase at residues 215-244 <ref name="dogs">PMID:20965171</ref> gives way to the <scene name='72/728060/Hydrophobic_regions/1'>Hydrophobic Areas</scene> (hydrophobic regions noted in red) both surrounding the active site and interfacing the lid. These areas are thought to draw lipids and promote docking <ref name="roussel" />. </div></td><td class='diff-marker'>+</td><td style="background: #cfc; color:black; font-size: smaller;"><div>HGL, a dimeric enzyme consisting of two 379 amino acid residue-long subunits, possesses a <scene name='72/728060/Catalytic_elbow/3'>Catalytic Arm</scene> consisting of residues Ser-153, His-353, and Asp-324 essential to the breakdown of lipids, coordinated with an <scene name='72/728060/Arm_and_hole/1'>Oxyanion Hole</scene> at Leu-67 and Gln-154 <ref name="dogs">PMID:20965171</ref>, that serves to stabilize the transition state. Structurally, the human gastric lipase exhibits a complex <scene name='72/728060/Secondary_structure/1'>Secondary Structure</scene> (beta sheets shown in yellow, alpha helices shown in orange, coiled coils shown in green, and amino acid side chains shown as purple). The <ins style="color: red; font-weight: bold; text-decoration: none;"><scene name='72/728060/1hlg_lid/2'></ins>"<ins style="color: red; font-weight: bold; text-decoration: none;">Lid</ins>"<ins style="color: red; font-weight: bold; text-decoration: none;"></scene> </ins>of the lipase at residues 215-244 <ref name="dogs">PMID:20965171</ref> gives way to the <scene name='72/728060/Hydrophobic_regions/1'>Hydrophobic Areas</scene> (hydrophobic regions noted in red) both surrounding the active site and interfacing the lid. These areas are thought to draw lipids and promote docking <ref name="roussel" />. </div></td></tr>
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<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>== Function ==</div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>== Function ==</div></td></tr>
</table>Megan M. Royhttp://52.214.119.220/wiki/index.php?title=Sandbox_78&diff=2587943&oldid=prevMegan M. Roy at 17:57, 20 April 20162016-04-20T17:57:28Z<p></p>
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<td colspan='2' style="background-color: white; color:black;">Revision as of 17:57, 20 April 2016</td>
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<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>== Introduction ==</div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>== Introduction ==</div></td></tr>
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<tr><td class='diff-marker'>-</td><td style="background: #ffa; color:black; font-size: smaller;"><div>Human gastric lipase (HGL, E.C. 3.1.1.3) (PBD ID: 1hlg) is <del style="color: red; font-weight: bold; text-decoration: none;">a type of </del>[[lipase]] <del style="color: red; font-weight: bold; text-decoration: none;">(of the enzyme class [[hydrolase]]) </del>that is responsible for initiating the digestion of dietary fats in the stomach <ref name="armand">PMID:7598069</ref>. This acid-stable enzyme <ref name="gastritis">PMID:23899880</ref> is secreted by the fundic chief cells of the human stomach and catalyzes 10-20% of total lipolytic processes (i.e., those involving fat breakdown) in healthy adults <ref name="armand" />. HGL specifically catalyzes the hydrolysis of triacylglycerol in order to produce diacylglycerol and a carboxylate byproduct <ref name="roussel">PMID:10358049</ref>, a process that facilitates subsequent fat breakdown by pancreatic lipase <ref name="dogs">PMID:20965171</ref>. In terms of disease implications, there is evidence to suggest that HGL secretion is altered in individuals with gastritis <ref name="gastritis" />.</div></td><td class='diff-marker'>+</td><td style="background: #cfc; color:black; font-size: smaller;"><div>Human gastric lipase (HGL, E.C. 3.1.1.3) (PBD ID: 1hlg) is <ins style="color: red; font-weight: bold; text-decoration: none;">the </ins>[[lipase]] that is responsible for initiating the digestion of dietary fats in the stomach <ref name="armand">PMID:7598069</ref>. This acid-stable enzyme <ref name="gastritis">PMID:23899880</ref> is secreted by the fundic chief cells of the human stomach and catalyzes 10-20% of total lipolytic processes (i.e., those involving fat breakdown) in healthy adults <ref name="armand" />. HGL specifically catalyzes the hydrolysis of triacylglycerol in order to produce diacylglycerol and a carboxylate byproduct <ref name="roussel">PMID:10358049</ref>, a process that facilitates subsequent fat breakdown by pancreatic lipase <ref name="dogs">PMID:20965171</ref>. In terms of disease implications, there is evidence to suggest that HGL secretion is altered in individuals with gastritis <ref name="gastritis" />.</div></td></tr>
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<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>== Structural highlights ==</div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>== Structural highlights ==</div></td></tr>
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<tr><td class='diff-marker'>-</td><td style="background: #ffa; color:black; font-size: smaller;"><div>HGL, a dimeric enzyme consisting of two 379 amino acid residue-long subunits, possesses a <scene name='72/728060/Catalytic_elbow/3'>Catalytic Arm</scene> consisting of residues Ser-153, His-353, and Asp-324 essential to the breakdown of lipids, coordinated with an <scene name='72/728060/Arm_and_hole/1'>Oxyanion Hole</scene> at Leu-67 and Gln-154 <ref name="dogs">PMID:20965171</ref>, that serves to stabilize the transition state. Structurally, the human gastric lipase exhibits a complex<del style="color: red; font-weight: bold; text-decoration: none;">, </del><scene name='72/728060/Secondary_structure/1'>Secondary Structure</scene> (beta sheets shown in yellow, alpha helices shown in orange, coiled coils shown in green, and amino acid side chains shown as purple)<del style="color: red; font-weight: bold; text-decoration: none;">, where the </del>"lid"<del style="color: red; font-weight: bold; text-decoration: none;">, </del>residues 215-244 <ref name="dogs">PMID:20965171</ref><del style="color: red; font-weight: bold; text-decoration: none;">, of the lipase </del>gives way to the <scene name='72/728060/Hydrophobic_regions/1'>Hydrophobic Areas</scene> (hydrophobic regions noted in red) both surrounding the active site and interfacing the lid<del style="color: red; font-weight: bold; text-decoration: none;">, </del>thought to draw lipids and promote docking <del style="color: red; font-weight: bold; text-decoration: none;"> </del><ref name="roussel" />. </div></td><td class='diff-marker'>+</td><td style="background: #cfc; color:black; font-size: smaller;"><div>HGL, a dimeric enzyme consisting of two 379 amino acid residue-long subunits, possesses a <scene name='72/728060/Catalytic_elbow/3'>Catalytic Arm</scene> consisting of residues Ser-153, His-353, and Asp-324 essential to the breakdown of lipids, coordinated with an <scene name='72/728060/Arm_and_hole/1'>Oxyanion Hole</scene> at Leu-67 and Gln-154 <ref name="dogs">PMID:20965171</ref>, that serves to stabilize the transition state. Structurally, the human gastric lipase exhibits a complex <scene name='72/728060/Secondary_structure/1'>Secondary Structure</scene> (beta sheets shown in yellow, alpha helices shown in orange, coiled coils shown in green, and amino acid side chains shown as purple)<ins style="color: red; font-weight: bold; text-decoration: none;">. The </ins>"lid" <ins style="color: red; font-weight: bold; text-decoration: none;">of the lipase at </ins>residues 215-244 <ref name="dogs">PMID:20965171</ref> gives way to the <scene name='72/728060/Hydrophobic_regions/1'>Hydrophobic Areas</scene> (hydrophobic regions noted in red) both surrounding the active site and interfacing the lid<ins style="color: red; font-weight: bold; text-decoration: none;">. These areas are </ins>thought to draw lipids and promote docking <ins style="color: red; font-weight: bold; text-decoration: none;"> </ins><ref name="roussel" />. </div></td></tr>
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<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>== Function ==</div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>== Function ==</div></td></tr>
</table>Megan M. Roy