Sandbox 78: Difference between revisions

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== Structural highlights ==

HGL, a 379 amino acid residue-long lipase enzyme, possesses a catalytic arm consisting of residues Ser-153, His-353, and Asp-324 essential to the breakdown of lipids, coordinated with an oxyanion hole Leu-67 Gln-154 <ref name="dogs">PMID:20965171</ref>, that serves to stabilize the transition state. Structurally, the human gastric lipase exhibits a complex, coordinated conformation, where the "lid" of the lipase gives way to the hydrophobic areas both surrounding the active site and interfacing the lid, thought to draw lipids and promote docking <ref name="roussel" />.

HGL, a 379 amino acid residue-long lipase enzyme, possesses a catalytic arm consisting of residues Ser-153, His-353, and Asp-324 essential to the breakdown of lipids, coordinated with an oxyanion hole Leu-67 Gln-154 <ref name="dogs">PMID:20965171</ref>, that serves to stabilize the transition state. Structurally, the human gastric lipase exhibits a complex, coordinated conformation, where the "lid", residues 215-244 <ref name="dogs">PMID:20965171</ref>, of the lipase gives way to the hydrophobic areas both surrounding the active site and interfacing the lid, thought to draw lipids and promote docking <ref name="roussel" />.

== Function ==

HGL, similarly to other members of the human lipase superfamily, are all serine esterases and have similar tertiary structure, evident by the conserved disulfide bonds. However, HGL is much more pH stable, allowing this pre-duodenal lipase to be active in the stomach (pH 1.7)'''*** CITE http://www.ncbi.nlm.nih.gov/pubmed/2395805''' and continue to be active as chyme moves into the duodenum (pH 6.1)'''*** CITE http://www.ncbi.nlm.nih.gov/pubmed/2395805'''.

== Relevance to Human Health & Disease ==

Sandbox 78: Difference between revisions

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 == Structural highlights ==
-HGL, a 379 amino acid residue-long lipase enzyme, possesses a catalytic arm consisting of residues Ser-153, His-353, and Asp-324 essential to the breakdown of lipids, coordinated with an oxyanion hole Leu-67 Gln-154 <ref name="dogs">PMID:20965171</ref>, that serves to stabilize the transition state. Structurally, the human gastric lipase exhibits a complex, coordinated conformation, where the "lid" of the lipase gives way to the hydrophobic areas both surrounding the active site and interfacing the lid, thought to draw lipids and promote docking   <ref name="roussel" />.
+HGL, a 379 amino acid residue-long lipase enzyme, possesses a catalytic arm consisting of residues Ser-153, His-353, and Asp-324 essential to the breakdown of lipids, coordinated with an oxyanion hole Leu-67 Gln-154 <ref name="dogs">PMID:20965171</ref>, that serves to stabilize the transition state. Structurally, the human gastric lipase exhibits a complex, coordinated conformation, where the "lid", residues 215-244 <ref name="dogs">PMID:20965171</ref>, of the lipase gives way to the hydrophobic areas both surrounding the active site and interfacing the lid, thought to draw lipids and promote docking   <ref name="roussel" />.
 == Function ==
+HGL, similarly to other members of the human lipase superfamily, are all serine esterases and have similar tertiary structure, evident by the conserved disulfide bonds. However, HGL is much more pH stable, allowing this pre-duodenal lipase to be active in the stomach (pH 1.7)'''*** CITE http://www.ncbi.nlm.nih.gov/pubmed/2395805''' and continue to be active as chyme moves into the duodenum (pH 6.1)'''*** CITE http://www.ncbi.nlm.nih.gov/pubmed/2395805'''.
 == Relevance to Human Health & Disease ==