Unexpected reversal of the regioselectivity in Thermomyces lanuginosus lipase-catalyzed acylation of floxuridine.
Unexpected inversion of the 3':5'-regioselectivity was observed in the enzymatic methacryloylation, crotonylation and cinnamoylation of floxuridine (1.5:1, 2.3:1 and 4.4:1, respectively), where Thermomyces lanuginosus lipase preferentially catalyzed the acylation of 3'-hydroxyl rather than that of 5'-hydroxyl group. The possible reason might be the presence of a remote interaction between the unsaturated bond in the acyl group and the aromatic ring of amino acid residue Trp89 in the lid of the lipase.
Li
Ning
N
Lab of Applied Biocatalysis, College of Light Industry and Food Sciences, South China University of Technology, 510640, Guangzhou, China.
Zong
Min-Hua
MH
Ma
Ding
D
D000215:Acylation; D001203:Ascomycota / Q000201:enzymology* / Q000378:metabolism*; D005467:Floxuridine / Q000378:metabolism*; D008049:Lipase / Q000378:metabolism*; D013237:Stereoisomerism; D013379:Substrate Specificity
D005467:Floxuridine; D008049:Lipase