Gate residues, acting in concert with distal dynamic networks, are important yet underexploited regulators of enzymatic catalysis. Here, the authors report conformational dynamics analysis of fluoroacetate dehalogenase RPA1163, which reveals a gate-based allosteric pair (K181–W185) that governs substrate access and reactivity, and engineer this pair to obtain a highly active variant for turnover of α-fluorophenylpropionic acid.
- Cui-zhen Wang
- Huisi Huang
- Jian-bo Wang