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From Proteopedia
(Difference between revisions)
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5. Acid catalysis by the breaking of the C-O covalent bond of the tetrahedral intermediate, releasing the peptide from the enzyme substrate complex. Once the peptide is released, the enzyme once again becomes active. <ref>PMID:16636277</ref>. | 5. Acid catalysis by the breaking of the C-O covalent bond of the tetrahedral intermediate, releasing the peptide from the enzyme substrate complex. Once the peptide is released, the enzyme once again becomes active. <ref>PMID:16636277</ref>. | ||
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== Disease == | == Disease == | ||
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<scene name='72/725338/Ribbon_diagram_n_c_rainbow/1'>Ribbon Diagram (N-->C Rainbow)</scene> | <scene name='72/725338/Ribbon_diagram_n_c_rainbow/1'>Ribbon Diagram (N-->C Rainbow)</scene> | ||
| + | Serine 195 - Base Catalysis Residue | ||
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| + | Histidine 57 - Acid Catalysis Residue | ||
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| + | Aspartic Acid 102 - Important Residue in Stabilization of Catalytic Mechanism | ||
</StructureSection> | </StructureSection> | ||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 03:41, 15 February 2016
Trypsin Structure
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