Sandbox 38: Difference between revisions

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== Function: ==

[[Image:Papainmech6.jpg|200px|left|thumb| mechanism of papain <ref>[http://chemistry.umeche.maine.edu/CHY431/Peptidase10.html] University of Maine</ref>.]]~~This~~ hydrolytic enzyme is able to break peptide bonds through the deprotonation of Cys-25 by His-159, with the help of Aspartate-125, which stabilizes the Histadine ring in order for this deprotonation to take place. The Cys-25 residue is then able to perform a nucleophilic attack on the carbonyl carbon of the peptide backbone, freeing the amino terminal of the peptide, forming a covalent intermediate. Next, the enzyme is deacylated by water, and the carboxy-terminal portion of the peptide is released.

[[Image:Papainmech6.jpg|200px|left|thumb| mechanism of papain <ref>[http://chemistry.umeche.maine.edu/CHY431/Peptidase10.html] University of Maine</ref>.]]The <scene name='Sandbox_38/Active_site/2'>active site</scene> of this hydrolytic enzyme is able to break peptide bonds through the deprotonation of Cys-25 by His-159, with the help of Aspartate-125, which stabilizes the Histadine ring in order for this deprotonation to take place. The Cys-25 residue is then able to perform a nucleophilic attack on the carbonyl carbon of the peptide backbone, freeing the amino terminal of the peptide, forming a covalent intermediate. Next, the enzyme is deacylated by water, and the carboxy-terminal portion of the peptide is released.

== History: ==

Sandbox 38: Difference between revisions

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@@ Line 12: / Line 12: @@
 == Function: ==
-[[Image:Papainmech6.jpg|200px|left|thumb| mechanism of papain <ref>[http://chemistry.umeche.maine.edu/CHY431/Peptidase10.html] University of Maine</ref>.]]This hydrolytic enzyme is able to break peptide bonds through the deprotonation of Cys-25 by His-159, with the help of Aspartate-125, which stabilizes the Histadine ring in order for this deprotonation to take place. The Cys-25 residue is then able to perform a nucleophilic attack on the carbonyl carbon of the peptide backbone, freeing the amino terminal of the peptide, forming a covalent intermediate.  Next, the enzyme is deacylated by water, and the carboxy-terminal portion of the peptide is released.
+[[Image:Papainmech6.jpg|200px|left|thumb| mechanism of papain <ref>[http://chemistry.umeche.maine.edu/CHY431/Peptidase10.html] University of Maine</ref>.]]The <scene name='Sandbox_38/Active_site/2'>active site</scene> of this hydrolytic enzyme is able to break peptide bonds through the deprotonation of Cys-25 by His-159, with the help of Aspartate-125, which stabilizes the Histadine ring in order for this deprotonation to take place. The Cys-25 residue is then able to perform a nucleophilic attack on the carbonyl carbon of the peptide backbone, freeing the amino terminal of the peptide, forming a covalent intermediate.  Next, the enzyme is deacylated by water, and the carboxy-terminal portion of the peptide is released.
 == History: ==