Structural highlights
Publication Abstract from PubMed
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.
Adaptation of thermophilic acetyltransferase to a water-mediated catalytic mechanism.,Chang YY, Hagawa S, Hsu CH Chem Commun (Camb). 2020 Sep 10;56(72):10537-10540. doi: 10.1039/d0cc04305b. PMID:32780067[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Chang YY, Hagawa S, Hsu CH. Adaptation of thermophilic acetyltransferase to a water-mediated catalytic mechanism. Chem Commun (Camb). 2020 Sep 10;56(72):10537-10540. doi: 10.1039/d0cc04305b. PMID:32780067 doi:http://dx.doi.org/10.1039/d0cc04305b
