Sandbox 33: Difference between revisions
From Proteopedia
Jump to navigationJump to search
No edit summary |
No edit summary |
||
| Line 9: | Line 9: | ||
Papain was first named in the late nineteenth century by Wurtz and Bouchut who partially purified the product from the sap of papaya. When named, it was simply recognized as proteolytically active constituent in the latex of tropical papaya fruit. | Papain was first named in the late nineteenth century by Wurtz and Bouchut who partially purified the product from the sap of papaya. When named, it was simply recognized as proteolytically active constituent in the latex of tropical papaya fruit. | ||
Throughout the mid 1950's and 1960's, purification and separation techniques improved greatly and pure papain was isolated. The study of papain allowed for great advances in understanding enzymes as proteins. In 1968, papin was the second enzyme to be crystallized and its structure determined by X-ray methods. Papain was the first cysteine protease to have its structure identified. | Throughout the mid 1950's and 1960's, purification and separation techniques improved greatly and pure papain was isolated. The study of papain allowed for great advances in understanding enzymes as proteins. In 1968, papin was the second enzyme to be crystallized and its structure determined by X-ray methods. Papain was the first cysteine protease to have its structure identified. | ||
In the 1980's, the geometry of the <scene name='Sandbox_33/Cys_residues/3'>active site</scene> | In the 1980's, the geometry of the <scene name='Sandbox_33/Cys_residues/3'>active site</scene> was reviewed and the three-dimensional structure was determined to a 1.65 Angstrom resolution. The precursors and inhibitors of papain were extensively studied into the 1990's. Today's research aims to further understand the specificity and structural perturbations brought about by inhibitors, low pH, metal ions, and fluorinated alcohols<ref>http://www.worthington-biochem.com/pap/default.html</ref>. | ||
