Papain: Difference between revisions

Michal Harel (talk | contribs)
No edit summary
Michal Harel (talk | contribs)
No edit summary
Line 1: Line 1:
[[Image:papayas.jpg|525px|right|thumb|Papaya<ref>[http://dailyfitnessmagz.com/2011/03/papayas-nutrition-facts/] Papaya's Nutrition Facts</ref>]]
[[Image:papayas.jpg|525px|right|thumb|Papaya<ref>[http://dailyfitnessmagz.com/2011/03/papayas-nutrition-facts/] Papaya's Nutrition Facts</ref>]]
'''Papain'''. Meat tenderizer. Old time home remedy for insect, jellyfish, and stingray stings<ref>[http://www.ameriden.com/products/advanced-digestive-enzyme/] Ameridan International</ref>. Who would have thought that a sulfhydryl protease from the latex of the papaya fruit, ''Carica papaya'' and ''Vasconcellea cundinamarcensis'', would have such a practical application beyond Proteopedia?
__TOC__
__TOC__
== Introduction ==
== Introduction ==
'''Papain'''. Meat tenderizer. Old time home remedy for insect, jellyfish, and stingray stings<ref>[http://www.ameriden.com/products/advanced-digestive-enzyme/] Ameridan International</ref>. Who would have thought that a sulfhydryl protease from the latex of the papaya fruit, ''Carica papaya'' and ''Vasconcellea cundinamarcensis'', would have such a practical application beyond Proteopedia?
Papain is a 23.4 kDa, 212 residue cysteine protease, also known as '''papaya proteinase I''', from the peptidase C1 family ([[EC Number|E.C.]] [[Hydrolase|3.4.22.2]]).<ref>[http://www.uniprot.org/uniprot/P00784] Uniprot</ref><ref name="9PAP PDB">[http://www.pdb.org/pdb/explore/explore.do?structureId=9PAP] 9PAP PDB</ref> It is the natural product of the [http://en.wikipedia.org/wiki/Carica_papaya Papaya](''Carica papaya'')<ref name="Sigma Aldrich">[http://www.sigmaaldrich.com/life-science/metabolomics/enzyme-explorer/analytical-enzymes/papain.html] Sigma Aldrich</ref>, and may be extracted from the plant's latex, leaves and roots. Papain displays a broad range of functions, acting as an endopeptidase, exopeptidase, amidase, and esterase,<ref name="Worthington">[http://www.worthington-biochem.com/pap/default.html] Worthington</ref> with its optimal activity values for pH lying between 6.0 and 7.0, and its optimal temperature for activity is 65 °C. Its pI values are 8.75 and 9.55, and it is best visualized at a wavelength of 278 nm. <ref name="Sigma Aldrich" />
Papain is a 23.4 kDa, 212 residue cysteine protease, also known as '''papaya proteinase I''', from the peptidase C1 family ([[EC Number|E.C.]] [[Hydrolase|3.4.22.2]]).<ref>[http://www.uniprot.org/uniprot/P00784] Uniprot</ref><ref name="9PAP PDB">[http://www.pdb.org/pdb/explore/explore.do?structureId=9PAP] 9PAP PDB</ref> It is the natural product of the [http://en.wikipedia.org/wiki/Carica_papaya Papaya](''Carica papaya'')<ref name="Sigma Aldrich">[http://www.sigmaaldrich.com/life-science/metabolomics/enzyme-explorer/analytical-enzymes/papain.html] Sigma Aldrich</ref>, and may be extracted from the plant's latex, leaves and roots. Papain displays a broad range of functions, acting as an endopeptidase, exopeptidase, amidase, and esterase,<ref name="Worthington">[http://www.worthington-biochem.com/pap/default.html] Worthington</ref> with its optimal activity values for pH lying between 6.0 and 7.0, and its optimal temperature for activity is 65 °C. Its pI values are 8.75 and 9.55, and it is best visualized at a wavelength of 278 nm. <ref name="Sigma Aldrich" />


Line 59: Line 60:


There are a small number of <scene name='Papain/Stefin_b_hbonds/2'>direct hydrogen bonds</scene> (labeled in <scene name='Papain/Stefin_b_hbonds/1'>this scene</scene>, between Stefin B and Papain, however there are many more polar interactions mediated by <scene name='Papain/Stfn_b_solvent_intrxns/1'>solvent bridges</scene>, the solvent being mainly <big><b><font color='darkturquoise'>water</font></b></big>.  Thirteen solvent molecules of water bridge polar residues of the enzyme and inhibitor.  Seventeen hydrogen bonds are made with a solvent molecule and Stefin B.  Fourteen of these bridges form a Papain contact.  The rest of the interactions are largely hydrophobic-- involving apolar <scene name='Papain/Stefin_b_vdw/2'>Van der Waals forces</scene>.<ref> PMID:2347312 </ref>
There are a small number of <scene name='Papain/Stefin_b_hbonds/2'>direct hydrogen bonds</scene> (labeled in <scene name='Papain/Stefin_b_hbonds/1'>this scene</scene>, between Stefin B and Papain, however there are many more polar interactions mediated by <scene name='Papain/Stfn_b_solvent_intrxns/1'>solvent bridges</scene>, the solvent being mainly <big><b><font color='darkturquoise'>water</font></b></big>.  Thirteen solvent molecules of water bridge polar residues of the enzyme and inhibitor.  Seventeen hydrogen bonds are made with a solvent molecule and Stefin B.  Fourteen of these bridges form a Papain contact.  The rest of the interactions are largely hydrophobic-- involving apolar <scene name='Papain/Stefin_b_vdw/2'>Van der Waals forces</scene>.<ref> PMID:2347312 </ref>
__NOTOC__
</StructureSection>


{{Clear}}
{{Clear}}

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

Kirsten Eldredge, Kyle Burch, Elizabeth Miller, Samuel Bray, Jacinth Koh, Sara Kongkatong, David Canner, Michal Harel, Joel L. Sussman, Jaime Prilusky