Sandbox 35: Difference between revisions
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[[Image:Papain Simple Cleavage.jpg|200px|right|thumb|Simple Overview of Cleavage by Papain. <ref>[http://www.worthington-biochem.com/pap/default.html] Worthington Biochemical Corporation </ref>]] | [[Image:Papain Simple Cleavage.jpg|200px|right|thumb|Simple Overview of Cleavage by Papain. <ref>[http://www.worthington-biochem.com/pap/default.html] Worthington Biochemical Corporation </ref>]] | ||
Except for valine, papain prefers to cleave at hydrophobic residues alanine, leucine, isoleucine, phenylalanine, tryptophan, or tyrosine <ref>[http://www.sigmaaldrich.com/life-science/biochemicals/biochemical-products.html?TablePage=16410606] Sigma Aldrich Papain</ref>. | Except for valine, papain prefers to cleave at hydrophobic residues alanine, leucine, isoleucine, phenylalanine, tryptophan, or tyrosine <ref>[http://www.sigmaaldrich.com/life-science/biochemicals/biochemical-products.html?TablePage=16410606] Sigma Aldrich Papain</ref>. Because of the importance of the oxyanion hole formation and the nucleophilic attack of cysteine, substances like cysteine, sulfide/sulfite, heavy metal chelating agents like EDTA, and N-bromosuccinimide behave as activators of the enzyme while PMSF, Hg2+ and other heavy metals, cystatin, leupeptin, sulfhydryl binding agents, carbonyl reagents, and alkylating agents serve as inhibitors. <ref>PMID: 6388564 </ref><ref>[http://www.biozym.de/datasheets/papain.php] Biozym </ref> | ||
==Fun Trivia== | ==Fun Trivia== | ||
