Usòrò:Protease mechanisms.png
Otu nyochaa a ha:800 × 307 piksels Ndị ọzọ mkpebi:320 × 123 piksels | 640 × 245 piksels | 1,437 × 551 piksels.
Failụ si na nke mbu (1,437 × 551 pixel, ívù akwukwo orunótu: 67 KB, MIME nke: image/png)
Mmẹkụwátá
| Nkówá |
English: Differences in cysteine and serine proteolysis mechanisms.
The protease (black) performs a nucleophilic attack on peptide substrate (red) to form a tetrahedral intermediate. This breaks down by ejection of the first product, the substrate C-terminus, to form the acyl-enzyme intermediate. Water replaces the first product and hydrolysis occurs via a second tetrahedral intermediate to regenerate free enzyme. Indicated differences are (a) the deprotonated cysteine, (b) aspartate (grey) not present in all cysteine proteases, (c) concerted deprotonation of serine, (d) aspartate hydrogen bonding, (e) amide protonation of the first leaving group, (f) alcohol protonation of the serine leaving group. |
| Ǹgụ́ụ̀bọ̀chị̀ | |
| Mkpọlọ́gwụ̀ | Thomas, Shafee, (2014). "Evolvability of a viral protease: experimental evolution of catalysis, robustness and specificity". PhD Thesis. University of Cambridge. |
| Odé ákwụ́kwọ́ | Thomas Shafee |
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