Please do NOT make changes to this Sandbox. Sandboxes 30-60 are reserved for use by Biochemistry 410 & 412 at Messiah College taught by Dr. Hannah Tims during Fall 2012 and Spring 2013.

Introduction

Lipase is an enzyme that functions to convert triacylglycerols to 2-monoacylglycerols, it catalyzes the reaction to break down lipids into its subunits. Lipase has 449 amino acid resiudes, and 2 domains, the C Terminal Domains is smaller with 112 residues, and the N Terminal Domain consists of 337 residues. Notice that each of these domains consist of 2 identical subunits. Lipase has an a chain and a b chain that each respectively contain 1 of the subunits of the C Terminal Domain and 1 of the subunits of the N terminal domains, all 4 parts come together to form the fully functional enzyme. The secondary structural elements of Lipase, including the Beta Sheets that make up 30 percent of the amino acid chain, and involving 139 residues as well as the Alpha Helices that make up 22 percent and 102 residues characterize the structure of the protein. The protein is held together by a combination of several factors, the hydrophobic residues certainly make a difference as one might expect, since all proteins generally fold to shield these from interaction with water, the cysteine residues that Lipase has also play a major role since they form Disulfide Bonds, Lipase has 12 disulfide bonds in all.