Sandbox 34: Difference between revisions
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<Structure load='9pap' size=' | <Structure load='9pap' size='400' frame='true' align='left' caption='Papain' scene='Sandbox_34/Entire_protein_with_ligandscys/1' /> | ||
== Structure == | == Structure == | ||
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The mechanism of cysteine proteases is very similar to that of serine proteases. The sulfhydryl group on cysteine executes a nucleophilic attack on the peptide bond of the protein it wishes to cleave. Asparagine-175 keeps histidine-159 in its stabilized imidazole form, while both histidine-159 and cysteine-25 take part in the actual mechanism. Opening up the carbonyl, the sulfhydryl group of CYS-25 is stabilized by HIS-159. As the carbonyl reforms, the peptide bond is broken, leaving the amide group to fend for itself.<ref>[http://chemistry.umeche.maine.edu/CHY431/Peptidase10.html] University of Maine</ref> [[Image:Papainmech6.jpg|200px|right|thumb| General mechanism of papain catalysis<ref>[http://chemistry.umeche.maine.edu/CHY431/Peptidase10.html] University of Maine</ref>.]] | The mechanism of cysteine proteases is very similar to that of serine proteases. The sulfhydryl group on cysteine executes a nucleophilic attack on the peptide bond of the protein it wishes to cleave. Asparagine-175 keeps histidine-159 in its stabilized imidazole form, while both histidine-159 and cysteine-25 take part in the actual mechanism. Opening up the carbonyl, the sulfhydryl group of CYS-25 is stabilized by HIS-159. As the carbonyl reforms, the peptide bond is broken, leaving the amide group to fend for itself.<ref>[http://chemistry.umeche.maine.edu/CHY431/Peptidase10.html] University of Maine</ref> [[Image:Papainmech6.jpg|200px|right|thumb| General mechanism of papain catalysis<ref>[http://chemistry.umeche.maine.edu/CHY431/Peptidase10.html] University of Maine</ref>.]] | ||
<Structure load='9pap' size='350' frame='true' align='left' caption='Papain' scene='Sandbox_34/Entire_protein_with_ligandscys/1' /> | |||
=== Inhibitors === | === Inhibitors === | ||
