科研之友
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摘要
The rapidly growing appreciation of entries' catalytic and substrate promiscuity may lead to their,expandecl use in the fields of chemical synthesis and industrial biotechnology. Here, we-explore:file substrate promiscuity of enoyl-aryl carrier protein reductases (commonly. known as FabI) and how that promiscuity is a function of inherent reactivity and file geometric demands of the enzyme's active site. We demonstrate that these enzymes catalyte the reduction of a wide range of substrates; particularly alpha,ss-unsaturate daldehydes. In addition, we demonstrate that a combination of quantum mechanical hydride affinity calculations and molecular docking can be used to rapidly categorize compounds that FabI can use as substrates. The results here provide new insight into the determinants of catalysis for FabI and set the stage for the developinent of a new assay for drug discovery, organic synthesis, and novel biocatalysts.
- 出版日期2017-9
