Sandbox 78: Difference between revisions
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== Structural highlights == | == 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 <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 (Gln-154), 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" />. | ||
== Function == | == Function == | ||