Recently, Associate Professor Chen Qi and Professor Zheng Gaowei from the State Key Laboratory of Bioreactor Engineering at East China University of Science and Technology proposed a rational enzyme engineering remodeling strategy based on dynamic cross-correlation network analysis. This strategy was applied to the remodeling work of halomethyl transferase BxHMT. The related research was published in "Applied Chemistry Germany".
S-Adenosylmethionine (SAM) is a widely used methyl donor in nature, serving as a cofactor for methyltransferases (MT) to achieve highly selective methylation of various substrates. Halomethyl transferase (HMT) can catalyze the reaction of halogenated alkane or sulfonic acid substrates with S-adenosylhomocysteine (SAH) to generate SAM, and cascade with MT to achieve methylation of the final substrate, greatly improving the atom economy of this reaction.
The research team proposed a dynamic cross-correlation network analysis strategy to guide the modification of the halomethyltransferase BxHMT. This strategy effectively addresses the long-standing challenge in enzyme engineering of identifying distal mutation sites, significantly reducing the burden of screening work. The substantial enhancement in catalytic performance of BxHMT-M4 also brings great hope for the effective utilization of non-natural substrates. This breakthrough lays a solid foundation for the wider application of the methylation reaction cascade between HMT and MT.
Source of the image: "German Applied Chemistry"
Related paper information: https://doi.org/10.1002/anie.202401235
