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. 2020 Sep 10;56(72):10537-10540.
doi: 10.1039/d0cc04305b.

Adaptation of thermophilic acetyltransferase to a water-mediated catalytic mechanism

Yu-Yung Chang  1 , Sora Hagawa  2 , Chun-Hua Hsu  3
Affiliations

Adaptation of thermophilic acetyltransferase to a water-mediated catalytic mechanism

Yu-Yung Chang et al. Chem Commun (Camb). .

Abstract

The common mechanism of N-acetyltransferases (NATs) is a water-mediated catalysis, which is not conducive to thermophilic acetyltransferases. The crystal structure of SsArd1 shows an ordered catalytic water molecule in a trap formed by the residues H88 and E127. Structure-guided mutagenesis, kinetic studies and MD simulation indicated that the turnover rates of H88A, E127A and H88A/E127A mutants were low, but that of the H88E/E127H mutant could be restored to the level of the wild type.

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