Sandbox 49: Difference between revisions
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==Lipase Active Sites== | ==Lipase Active Sites== | ||
The Lipase Active Sites consists of a catalytic triad of residues: Ser 152, Asp 176, and His 263. Residues Phe 77 and Leu 153 are also important for the mechanism of Lipase, functioning as residues to aid in the stabilization of the oxyanion. The catalytic triad is covered by a “lid” that protects the active site of the enyzyme, and prevents the binding of substrate when it is closed and covering the active site. In total lipase has 2 active sites, 1 for each of the domains that make up the enzyme. | The Lipase Active Sites consists of a catalytic triad of residues: Ser 152, Asp 176, and His 263. Residues Phe 77 and Leu 153 are also important for the mechanism of Lipase, functioning as residues to aid in the stabilization of the oxyanion. The catalytic triad is covered by a “lid” that protects the active site of the enyzyme, and prevents the binding of substrate when it is closed and covering the active site, the open lid is stabilized by the formation of hydrogen bonds to neighboring residues. In total lipase has 2 active sites, 1 for each of the domains that make up the enzyme. | ||
==Mechanism== | ==Mechanism== | ||
