Sandbox 34: Difference between revisions

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=== Introduction ===

'''Papain''' is a cysteine protease, also known as '''papaya proteinase I''', from the peptidase C1 family referenced as E.C. 3.4.22.2. It functions as a hydrolase, endopeptidase, and thiol protease.<ref name="UniProt">http://www.uniprot.org/uniprot/P00784</ref> Its optimal activity values for pH lie between 6.0 and 7.0, and 65 °C as its optimal temperature for activity. Its pI values are 8.75 and 9.55. Papain is best visualized at a wavelength of 278 nm. <ref>http://www.sigmaaldrich.com/life-science/metabolomics/enzyme-explorer/analytical-enzymes/papain.html</ref> Naturally found in the latex of the papaya fruit, one of the most common uses of papain is as a meat tenderizer because of its ability to hydrolyze esters and amides.<ref>IUBMB Enzyme Nomenclature: www.chem.qmul.ac.uk/iubmb/enzyme/EC3/4/22/2.html</ref> Another common use is as a digestive aid. Papaya is commonly referenced as a preferred fruit for those suffering from gastroesophageal reflux disease due to its ability to help the the stomach with digestion of complex proteins.

'''Papain''' is a cysteine protease, also known as '''papaya proteinase I''', from the peptidase C1 family referenced as E.C. 3.4.22.2. It functions as a hydrolase, endopeptidase, and thiol protease.<ref name="UniProt">http://www.uniprot.org/uniprot/P00784</ref> Its optimal activity values for pH lie between 6.0 and 7.0, and 65 °C as its optimal temperature for activity. Its pI values are 8.75 and 9.55. Papain is best visualized at a wavelength of 278 nm. <ref>http://www.sigmaaldrich.com/life-science/metabolomics/enzyme-explorer/analytical-enzymes/papain.html</ref> While only consisting of a single peptide chain, papain has two domains that form a cleft in which the active site lies.<ref name="PDBSum">http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl?pdbcode=9pap&template=clefts.html&r=speedfill</ref> Naturally found in the latex of the papaya fruit, one of the most common uses of papain is as a meat tenderizer because of its ability to hydrolyze esters and amides.<ref>IUBMB Enzyme Nomenclature: www.chem.qmul.ac.uk/iubmb/enzyme/EC3/4/22/2.html</ref> Another common use is as a digestive aid. Papaya is commonly referenced as a preferred fruit for those suffering from gastroesophageal reflux disease due to its ability to help the the stomach with digestion of complex proteins.

=== History ===

Sandbox 34: Difference between revisions

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 === Introduction ===
 <Structure load='9pap' size='500' frame='true' align='right' caption='Papain' scene='Sandbox_34/Entire_protein_with_ligandscys/1' />
-'''Papain''' is a cysteine protease, also known as '''papaya proteinase I''', from the peptidase C1 family referenced as E.C. 3.4.22.2. It functions as a hydrolase, endopeptidase, and thiol protease.<ref name="UniProt">http://www.uniprot.org/uniprot/P00784</ref> Its optimal activity values for pH lie between 6.0 and 7.0, and 65 °C as its optimal temperature for activity. Its pI values are 8.75 and 9.55. Papain is best visualized at a wavelength of 278 nm. <ref>http://www.sigmaaldrich.com/life-science/metabolomics/enzyme-explorer/analytical-enzymes/papain.html</ref> Naturally found in the latex of the papaya fruit, one of the most common uses of papain is as a meat tenderizer because of its ability to hydrolyze esters and amides.<ref>IUBMB Enzyme Nomenclature: www.chem.qmul.ac.uk/iubmb/enzyme/EC3/4/22/2.html</ref> Another common use is as a digestive aid. Papaya is commonly referenced as a preferred fruit for those suffering from gastroesophageal reflux disease due to its ability to help the the stomach with digestion of complex proteins.
+'''Papain''' is a cysteine protease, also known as '''papaya proteinase I''', from the peptidase C1 family referenced as E.C. 3.4.22.2. It functions as a hydrolase, endopeptidase, and thiol protease.<ref name="UniProt">http://www.uniprot.org/uniprot/P00784</ref> Its optimal activity values for pH lie between 6.0 and 7.0, and 65 °C as its optimal temperature for activity. Its pI values are 8.75 and 9.55. Papain is best visualized at a wavelength of 278 nm. <ref>http://www.sigmaaldrich.com/life-science/metabolomics/enzyme-explorer/analytical-enzymes/papain.html</ref> While only consisting of a single peptide chain, papain has two domains that form a cleft in which the active site lies.<ref name="PDBSum">http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl?pdbcode=9pap&template=clefts.html&r=speedfill</ref> Naturally found in the latex of the papaya fruit, one of the most common uses of papain is as a meat tenderizer because of its ability to hydrolyze esters and amides.<ref>IUBMB Enzyme Nomenclature: www.chem.qmul.ac.uk/iubmb/enzyme/EC3/4/22/2.html</ref> Another common use is as a digestive aid. Papaya is commonly referenced as a preferred fruit for those suffering from gastroesophageal reflux disease due to its ability to help the the stomach with digestion of complex proteins.
 === History ===