ܠܦܦܐ:Triad chemical mech.png

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ܡܢ ܘܝܩܝܦܕܝܐ، ܐܝܢܣܩܠܘܦܕܝܐ ܚܐܪܬܐ

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Description
English: A catalytic triad charge-relay system as commonly found in proteases. The acid residue (commonly glutamate or aspartate) aligns and polarises the base (usually histidine) which activates the nucleophile (often serine or cysteine, occasionally threonine). The catalytic triad reduces the pKa of the nucleophilic residue which then performs a nucleophilic attack on the substrate.
ܣܝܩܘܡܐ
ܡܒܘܥܐ Thomas, Shafee, (2014). "Evolvability of a viral protease: experimental evolution of catalysis, robustness and specificity". PhD Thesis. University of Cambridge.
ܣܝܘܡܐ Thomas Shafee

ܦܣܣܐ

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