This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
Sandbox 44
From Proteopedia
(→Introduction) |
|||
| Line 16: | Line 16: | ||
==Structural Aspects of Lipase == | ==Structural Aspects of Lipase == | ||
| - | + | The <scene name='Sandbox_44/Structure_of_lipase/1'>structure of lipase</scene> displays the enzyme in its natural form, with its two identical chains, each consisting of 449 amino acid residues. The <scene name='Sandbox_44/Secondary_structure/3'>secondary structures</scene> of human pancreatic lipase consists of 30% beta sheets (shown in orange), and 22% alpha helices (shown in fuschia). Here, beta sheets are depicted as planks, and alpha helices are shown as rockets. The remaining 48% of the enzyme's secondary structure consists of ordered, nonrepetitive sequence structure (shown in white) in contrast to the alpha helices and beta sheets. This even distribution of 48% ordered nonrepetitive structure to 52% alpha helix/beta sheet structure correlates to the appearance of the structure of lipase, which appears even to the casual observer to be about half alpha helix/beta sheet structure, and half ordered nonrepetitive structure depicted through the looping connective lines. This secondary structure of the enzyme, however, is formed due to the nature of the hydrogen bonding in between the main chains of lipase. | |
| - | + | ||
| - | <scene name='Sandbox_44/Structure_of_lipase/1'>structure of lipase</scene> | + | |
| - | + | ||
| - | <scene name='Sandbox_44/Secondary_structure/3'>secondary structures</scene> | + | |
<scene name='Sandbox_44/Hydrophobic_residues/1'>hydrophobic residues</scene> | <scene name='Sandbox_44/Hydrophobic_residues/1'>hydrophobic residues</scene> | ||
Revision as of 00:35, 14 November 2011
| 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. |
Contents |
Lipase
PDB ID: 1HPLE.C.: 3.1.1.3
Number of Amino Acid Residues: 449
Number of Chains: 2
Weight: 50kDa
Introduction
The lipase class of enzymes are known to cut a lipid substrate at a specific location on their glycerol backbone. Lipase catalyzes the lipid breakdown through the hydrolysis of the esters in fatty acids. While lipase is found primarily in the human pancreas, lipase can also be located in other areas in the body such as the mouth and the stomach. Pancreatic lipase, in particular, serves in human digestion to break down fats from the human diet. This lipase, therefore, is found in the digestive system of humans and is involved in the conversion of triglycerides to monoglycerides and free fatty acids.Human pancreatic lipase distinguishes itself from other pancreatic enzymes because when it is synthesized it is done so in its final form, without needing to be activated through proteolytic cleavage. However, while lipase does not need outside activation, it is not truly efficient without the presence of colipase in the duodenum.
The crystal structure of human pancreatic lipase is still yet to be determined and the research goal of many current scientists.
| |||||||||||
