Sandbox 36
From Proteopedia
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Revision as of 03:22, 12 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. |
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Papain
Introduction
Papain is a sulfhydryl protease derived from the papaya fruit. Papain has many varied and important commercial uses. It is often used as a meat tenderizer because it can hydrolyze the peptide bonds of collagen, elastin, and actomyosin. It is also used in contact lens solution to remove protein deposits on the lenses. Papain also has many medical uses and is used to treat pain, swelling, and fluid retention following trauma and surgery. More commonly, papain is used as a digestive supplement.
Structure
It consists of a single polypeptide chain of 212 amino acid residues folded into two domains. The active site is located in a groove between the two domains. The active site contains a catalytic diad made up of Cysteine-25 and Histidine-159. Aspartate-158 also plays a role in catalysis. Papain's active site can accommodate seven amino acids of a substrate. When the peptide is cleaved, the first four resides reside on the amino side of the peptide bond while the other three reside on the carboxyl side.
