Substrate specificity of lipase from Burkholderia cepacia in the synthesis of 3'-arylaliphatic acid esters of floxuridine.
Among the five vinyl esters bearing phenyl ring in acyl moiety, the lipase from Burkholderia cepacia was most specific toward vinyl 4-phenylbutyrate. Additionally, 3'-regioselectivity of the enzyme was enhanced with the increment of acyl chain length. The lipophilic 3'-arylaliphatic acid esters of floxuridine, its potential prodrugs, were synthesized with high conversions (>98%) and good to excellent regioselectivities (85-99%) via the enzymatic approach.
Li
Ning
N
State Key Laboratory of Pulp and Paper Engineering, South China University of Technology, Guangzhou 510640, China.
Zeng
Quan-Ming
QM
Zong
Min-Hua
MH
D000215:Acylation; D016956:Burkholderia cepacia / Q000201:enzymology*; D005227:Fatty Acids / Q000378:metabolism*; D005467:Floxuridine / Q000031:analogs & derivatives* / Q000378:metabolism; D008049:Lipase / Q000737:chemistry / Q000378:metabolism*; D013237:Stereoisomerism; D013379:Substrate Specificity
D005227:Fatty Acids; D005467:Floxuridine; D008049:Lipase