Sandbox 36: Difference between revisions

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==Catalytic Diad==

The 212 residues of Papain can be split nearly in half to produce <scene name='Sandbox_36/Papain_domains/2'>two domains</scene> though the enzyme consists only of one polypeptide chain. The <scene name='Sandbox_36/Papain_active_site_use/2'>active site</scene> is located in the cleft between the two domains. The active site contains a <scene name='Sandbox_36/Papain_catalytic_diad/2'>catalytic diad</scene> made up of Cysteine-25 and Histidine-159. Aspartate-158 also plays a role in catalysis but it is not considered part of the diad. Papain's active site can accommodate seven amino acids of a substrate. When the peptide is cleaved, the first four resides reside on the amino side of the peptide bond while the other three reside on the carboxyl side. <ref>http://pubs.acs.org/doi/abs/10.1021/bi00544a013 </ref> Papain prefers to cleave at: (hydrophobic)-(Arg or Lys)- cleaves here -(not Val). Hydrophobic is Ala, Val, Leu, Ile, Phe, Trp, or Tyr. <ref> http://www.sigmaaldrich.com/life-science/biochemicals/biochemical-products.html?TablePage=16410606 </ref>

The 212 residues of Papain can be split nearly in half to produce <scene name='Sandbox_36/Papain_domains/2'>two domains</scene> though the enzyme consists only of one polypeptide chain. The <scene name='Sandbox_36/Papain_active_site_use/3'>active site</scene> is located in the cleft between the two domains. The active site contains a <scene name='Sandbox_36/Papain_catalytic_diad/2'>catalytic diad</scene> made up of Cysteine-25 and Histidine-159. Aspartate-158 also plays a role in catalysis but it is not considered part of the diad. Papain's active site can accommodate seven amino acids of a substrate. When the peptide is cleaved, the first four resides reside on the amino side of the peptide bond while the other three reside on the carboxyl side. <ref>http://pubs.acs.org/doi/abs/10.1021/bi00544a013 </ref> Papain prefers to cleave at: (hydrophobic)-(Arg or Lys)- cleaves here -(not Val). Hydrophobic is Ala, Val, Leu, Ile, Phe, Trp, or Tyr. <ref> http://www.sigmaaldrich.com/life-science/biochemicals/biochemical-products.html?TablePage=16410606 </ref>

Sandbox 36: Difference between revisions

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Revision as of 22:03, 12 March 2012 view source Student (talk \| contribs) students 33,923 edits No edit summary ← Older edit		Revision as of 22:24, 12 March 2012 view source Student (talk \| contribs) students 33,923 edits No edit summary Newer edit →
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	==Catalytic Diad==		==Catalytic Diad==
	The 212 residues of Papain can be split nearly in half to produce <scene name='Sandbox_36/Papain_domains/2'>two domains</scene> though the enzyme consists only of one polypeptide chain. The <scene name='Sandbox_36/Papain_active_site_use/2'>active site</scene> is located in the cleft between the two domains. The active site contains a <scene name='Sandbox_36/Papain_catalytic_diad/2'>catalytic diad</scene> made up of Cysteine-25 and Histidine-159. Aspartate-158 also plays a role in catalysis but it is not considered part of the diad. Papain's active site can accommodate seven amino acids of a substrate. When the peptide is cleaved, the first four resides reside on the amino side of the peptide bond while the other three reside on the carboxyl side. <ref>http://pubs.acs.org/doi/abs/10.1021/bi00544a013 </ref> Papain prefers to cleave at: (hydrophobic)-(Arg or Lys)- cleaves here -(not Val). Hydrophobic is Ala, Val, Leu, Ile, Phe, Trp, or Tyr. <ref> http://www.sigmaaldrich.com/life-science/biochemicals/biochemical-products.html?TablePage=16410606 </ref>		The 212 residues of Papain can be split nearly in half to produce <scene name='Sandbox_36/Papain_domains/2'>two domains</scene> though the enzyme consists only of one polypeptide chain. The <scene name='Sandbox_36/Papain_active_site_use/3'>active site</scene> is located in the cleft between the two domains. The active site contains a <scene name='Sandbox_36/Papain_catalytic_diad/2'>catalytic diad</scene> made up of Cysteine-25 and Histidine-159. Aspartate-158 also plays a role in catalysis but it is not considered part of the diad. Papain's active site can accommodate seven amino acids of a substrate. When the peptide is cleaved, the first four resides reside on the amino side of the peptide bond while the other three reside on the carboxyl side. <ref>http://pubs.acs.org/doi/abs/10.1021/bi00544a013 </ref> Papain prefers to cleave at: (hydrophobic)-(Arg or Lys)- cleaves here -(not Val). Hydrophobic is Ala, Val, Leu, Ile, Phe, Trp, or Tyr. <ref> http://www.sigmaaldrich.com/life-science/biochemicals/biochemical-products.html?TablePage=16410606 </ref>