Sandbox 38: Difference between revisions

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Papain is a cysteine protease derived from the papaya plant. This protein consists of 212 amino acids that contribute to a single polypeptide chain with a molecular weight of 23.4 kD. Like other proteins, Papain contains a <scene name='Sandbox_38/C-n_terminus/1'>3' Carbon and a 5' Nitrogen terminus</scene>. The red end of the protein indicates the 3' Carbon end, while the blue end indicates the 5' Nitrogen terminal. The varying colors in between are merely used to show the progression between the two terminals. The <scene name='Sandbox_38/Ss/2'>secondary structure</scene> of this molecule consists of 25% alpha helices, seen as pink "rockets", and 21% beta sheets, seen as orange "planks" . Traditionally, Papain has be used as a commercial meat tenderizer. This enzyme also has some medicinal uses, as it has be been used in wound debridement, and is occasionally administered as a dietary supplement. This enzyme is able to aid in digestive problems, as it is able to break down food so it is easier to digest.

== History: ==

Papain was originally discovered during the colonial period in Congo. The native inhabitants discovered that wrapping their elephant meat in papaya leaves helped to tenderize the meat. While they did not know the direct cause, this was when the proteolytic enzyme was first discovered. The active binding site of this enzyme was first discovered by Drenth et al., through the crystallographic analysis of the enzymes structure.

== Function: ==

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[[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/3'>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: ==~~

Papain was originally discovered during the colonial period in Congo. The native inhabitants discovered that wrapping their elephant meat in papaya leaves helped to tenderize the meat. While they did not know the direct cause, this was when the proteolytic enzyme was first discovered. The active binding site of this enzyme was first discovered by Drenth et al., through the crystallographic analysis of the enzymes structure.

== Composition of Papain: ==

Sandbox 38: Difference between revisions

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 Papain is a cysteine protease derived from the papaya plant.  This protein consists of 212 amino acids that contribute to a single polypeptide chain with a molecular weight of 23.4 kD.  Like other proteins, Papain contains a <scene name='Sandbox_38/C-n_terminus/1'>3' Carbon and a 5' Nitrogen terminus</scene>. The red end of the protein indicates the 3' Carbon end, while the blue end indicates the 5' Nitrogen terminal. The varying colors in between are merely used to show the progression between the two terminals. The <scene name='Sandbox_38/Ss/2'>secondary structure</scene> of this molecule consists of 25% alpha helices, seen as pink "rockets", and 21% beta sheets, seen as orange "planks" . Traditionally, Papain has be used as a commercial meat tenderizer. This enzyme also has some medicinal uses, as it has be been used in wound debridement, and is occasionally administered as a dietary supplement. This enzyme is able to aid in digestive problems, as it is able to break down food so it is easier to digest.
+== History: ==
+Papain was originally discovered during the colonial period in Congo.  The native inhabitants discovered that wrapping their elephant meat in papaya leaves helped to tenderize the meat.  While they did not know the direct cause, this was when the proteolytic enzyme was first discovered.  The active binding site of this enzyme was first discovered by Drenth et al., through the crystallographic analysis of the enzymes structure.
 == Function: ==
@@ Line 14: / Line 16: @@
 [[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/3'>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: ==
-Papain was originally discovered during the colonial period in Congo.  The native inhabitants discovered that wrapping their elephant meat in papaya leaves helped to tenderize the meat.  While they did not know the direct cause, this was when the proteolytic enzyme was first discovered.  The active binding site of this enzyme was first discovered by Drenth et al., through the crystallographic analysis of the enzymes structure.
 == Composition of Papain: ==