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Triad_chemical_mech.png (566 Γ— 267 π€πŒΉπŒΊπƒπŒ΄πŒ»πŒ°, π†πŒ΄πŒΉπŒ»π…πŒ°πŒ·πƒπ„πŒΏπƒ: 7 KB, 𐌼𐌹𐌼𐌴 𐌺𐌿𐌽𐌹: image/png)

𐍃𐍉 πŒ³πŒ°π„πŒ° πŒΉπƒπ„ π†π‚πŒ°πŒΌ Wikimedia Commons 𐌾𐌰𐌷 𐌼𐌰𐌲 πŒ±π‚πŒΏπŒΊπŒΎπŒ°πŒ³πŒ° π†π‚πŒ°πŒΌ πŒ°πŒ½πŒΈπŒ°π‚πŒ°πŒΉπŒΌ π†πŒ°πŒΏπ‚πŒ°π…πŒ°πŒΏπ‚π€π‰πŒΌ. πŒ²πŒ°πƒπŒΊπŒ΄πŒΉπ‚πŒ΄πŒΉπŒ½πƒ 𐌰𐌽𐌰 πƒπŒ΄πŒΉπŒ½πŒ°πŒΌπŒΌπŒ° πŒ³πŒ°π„πŒ° πƒπŒΊπŒ΄πŒΉπ‚πŒ΄πŒΉπŒ½πŒΉπŒ»πŒ°πŒΏπŒ±πŒ° πŒΎπŒ°πŒΉπŒ½πŒ°π‚ πŒ°π„πŒ°πŒΏπŒ²πŒΉπŒΈπƒ πŒΉπƒπ„ πŒΏπ†.

πŒΌπŒ°πŒΏπ‚πŒ²πŒΏπƒ πƒπŒΊπŒ΄πŒΉπ‚πŒ΄πŒΉπŒ½πƒ

πƒπŒΊπŒ΄πŒΉπ‚πŒ΄πŒΉπŒ½πƒ
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.
Date
πŒ±π‚πŒΏπŒ½πŒ½πŒ° Thomas, Shafee, (2014). "Evolvability of a viral protease: experimental evolution of catalysis, robustness and specificity". PhD Thesis. University of Cambridge.
πŒ±π‰πŒΊπŒ°π‚πŒ΄πŒΉπƒ Thomas Shafee

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23 πŒ°πŒΏπŒΊπ„π‰πŒ±πŒ°πŒΉπ‚ 2013

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