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Sandbox 34
From Proteopedia
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<StructureSection load='9pap' size='500' side='right' caption='Structure of 9PAP (PDB entry [[9pap]])' scene='Sandbox_34/9pap_without_solvent_meoh/3'> | <StructureSection load='9pap' size='500' side='right' caption='Structure of 9PAP (PDB entry [[9pap]])' scene='Sandbox_34/9pap_without_solvent_meoh/3'> | ||
| - | + | '''Papain''' is a cysteine protease, also known as '''papaya proteinase I''',from the peptidase C1 family. 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. 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 | + | |
</StructureSection> | </StructureSection> | ||
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Papain is a relatively simple enzyme. It consists of only one chain of 212 residues with three disulfide bonds.<ref>PMID:6502713</ref> A modified cysteine residue with a sulhydryl group, <scene name='Sandbox_34/Entire_protein_with_ocs_focus/2'>cysteine sulfonic acid</scene>, is necessary for the activity of the enzyme.<ref>http://www.sigmaaldrich.com/life-science/metabolomics/enzyme-explorer/analytical-enzymes/papain.html</ref> | Papain is a relatively simple enzyme. It consists of only one chain of 212 residues with three disulfide bonds.<ref>PMID:6502713</ref> A modified cysteine residue with a sulhydryl group, <scene name='Sandbox_34/Entire_protein_with_ocs_focus/2'>cysteine sulfonic acid</scene>, is necessary for the activity of the enzyme.<ref>http://www.sigmaaldrich.com/life-science/metabolomics/enzyme-explorer/analytical-enzymes/papain.html</ref> | ||
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| - | <scene name='Sandbox_34/9pap_without_solvent_meoh/2'>TextToBeDisplayed</scene> | ||
| - | <scene name='Sandbox_34/Entire_protein_with_ocs_focus/1'>TextToBeDisplayed</scene> | ||
| - | <scene name='Sandbox_34/Entire_protein_with_ocs_focus/2'>TextToBeDisplayed</scene> | ||
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| + | </StructureSection> | ||
| + | == Specificity == | ||
| + | <StructureSection load='9pap' size='500' side='right' caption='Structure of 9PAP (PDB entry [[9pap]])' scene='Sandbox_34/9pap_without_solvent_meoh/3'> | ||
| + | Papain will digest most protein substrates more extensively than the pancreatic proteases. Papain exhibits broad specificity, cleaving peptide bonds of basic amino acids, leucine, or glycine. It also hydrolyzes esters and amides. Papain exhibits a preference for an amino acid bearing a large hydrophobic side chain at the P2 position. It does not accept Val at the P1' position. 1 | ||
| + | </StructureSection> | ||
== References == | == References == | ||
<references /> | <references /> | ||
Revision as of 17:50, 13 November 2011
| Please do NOT make changes to this Sandbox. Sandboxes 30-60 are reserved for use by Biochemistry 410 & 412 at Messiah College taught by Dr. Hannah Tims during Fall 2012 and Spring 2013. |
Contents |
Papain
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Structure
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Specificity
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References
- ↑ IUBMB Enzyme Nomenclature: www.chem.qmul.ac.uk/iubmb/enzyme/EC3/4/22/2.html
- ↑ Kamphuis IG, Kalk KH, Swarte MB, Drenth J. Structure of papain refined at 1.65 A resolution. J Mol Biol. 1984 Oct 25;179(2):233-56. PMID:6502713
- ↑ http://www.sigmaaldrich.com/life-science/metabolomics/enzyme-explorer/analytical-enzymes/papain.html
