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Summary
| Description |
General reaction mechanism of catalysed by a catalytic triad (black): nucleophilic substitution at a carbonyl substrate (red) by a second substrate (blue). First, the enzyme's nucleophile (X) attacks the carbonyl to form a covalently linked acyl-enzyme intermediate. This intermediate is then attacked by the second nucleophile (X') of the second substrate. If the second nucleophile is the hydroxyl of water, the result is hydrolysis, otherwise the result is group transfer of X'. |
| Date | |
| Source | Thomas, Shafee, (2014). "Evolvability of a viral protease: experimental evolution of catalysis, robustness and specificity". PhD Thesis. University of Cambridge. |
| Author | Thomas Shafee |
| Other versions | For unannotated version see File:Triad mechanism unannotated.svg |
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| Date/Time | Thumbnail | Dimensions | User | Comment | |
|---|---|---|---|---|---|
| current | 11:16, 20 August 2015 | | 1,225 × 221 (225 KB) | Evolution and evolvability | slightly smaller text size |
| 11:59, 16 August 2015 |  | 1,225 × 220 (386 KB) | Evolution and evolvability | Slightly smaller titles text | |
| 10:14, 16 August 2015 |  | 1,225 × 220 (409 KB) | Evolution and evolvability | text to paths | |
| 10:11, 16 August 2015 |  | 1,225 × 220 (206 KB) | Evolution and evolvability | User created page with UploadWizard |
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