Sandbox 34: Difference between revisions

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=== Specificity ===

Papain digests a large variety of proteins, with a very broad specificity. Its <scene name='Sandbox_34/9pap_active_site/1'>active site</scene>consists of the residues cysteine-25, histidine-159, and asparagine-175. While asparagine-175 is included with the active site, it does not play a direct role in the mechanism of papain. Rather, it supports the It cleaves the peptide bonds of basic amino acids, leucine and glycine by nucleophilic attack with its sulfhydryl group on cysteine-25 <ref>http://www.ebi.ac.uk/QuickGO/GTerm?id=GO:0004197</ref>. It also hydrolyzes esters and amides. It prefers amino acids that bear large hydrophobic side chains at the P2 position, and will not accept valine at the P1' position. <ref name="UniProt" />

Papain digests a large variety of proteins, with a very broad specificity. Its <scene name='Sandbox_34/9pap_active_site/1'>active site</scene> consists of the residues cysteine-25, histidine-159, and asparagine-175. While asparagine-175 is included with the active site, it does not play a direct role in the mechanism of papain. Rather, it supports the It cleaves the peptide bonds of basic amino acids, leucine and glycine by nucleophilic attack with its sulfhydryl group on cysteine-25 <ref>http://www.ebi.ac.uk/QuickGO/GTerm?id=GO:0004197</ref>. It also hydrolyzes esters and amides. It prefers amino acids that bear large hydrophobic side chains at the P2 position, and will not accept valine at the P1' position. <ref name="UniProt" />

[[Image:Papainmech6.jpg|~~500px~~|right|thumb| A general mechanism of papain catalysis<ref>[http://chemistry.umeche.maine.edu/CHY431/Peptidase10.html] University of Maine</ref>.]]

[[Image:Papainmech6.jpg|400px|right|thumb| A general mechanism of papain catalysis<ref>[http://chemistry.umeche.maine.edu/CHY431/Peptidase10.html] University of Maine</ref>.]]

Sandbox 34: Difference between revisions

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@@ Line 37: / Line 37: @@
 === Specificity ===
-Papain digests a large variety of proteins, with a very broad specificity. Its <scene name='Sandbox_34/9pap_active_site/1'>active site</scene>consists of the residues cysteine-25, histidine-159, and asparagine-175. While asparagine-175 is included with the active site, it does not play a direct role in the mechanism of papain. Rather, it supports the It cleaves the peptide bonds of basic amino acids, leucine and glycine by nucleophilic attack with its sulfhydryl group on cysteine-25 <ref>http://www.ebi.ac.uk/QuickGO/GTerm?id=GO:0004197</ref>. It also hydrolyzes esters and amides. It prefers amino acids that bear large hydrophobic side chains at the P2 position, and will not accept valine at the P1' position. <ref name="UniProt" />
+Papain digests a large variety of proteins, with a very broad specificity. Its <scene name='Sandbox_34/9pap_active_site/1'>active site</scene> consists of the residues cysteine-25, histidine-159, and asparagine-175. While asparagine-175 is included with the active site, it does not play a direct role in the mechanism of papain. Rather, it supports the It cleaves the peptide bonds of basic amino acids, leucine and glycine by nucleophilic attack with its sulfhydryl group on cysteine-25 <ref>http://www.ebi.ac.uk/QuickGO/GTerm?id=GO:0004197</ref>. It also hydrolyzes esters and amides. It prefers amino acids that bear large hydrophobic side chains at the P2 position, and will not accept valine at the P1' position. <ref name="UniProt" />
-[[Image:Papainmech6.jpg|500px|right|thumb| A general mechanism of papain catalysis<ref>[http://chemistry.umeche.maine.edu/CHY431/Peptidase10.html] University of Maine</ref>.]]
+[[Image:Papainmech6.jpg|400px|right|thumb| A general mechanism of papain catalysis<ref>[http://chemistry.umeche.maine.edu/CHY431/Peptidase10.html] University of Maine</ref>.]]