The halo-substituent effect on Pseudomonas cepacia lipase-mediated regioselective acylation of nucleosides: A comparative investigation.
In this work, comparative experiments were explored to investigate the substrate specificity of Pseudomonas cepacia lipase in regioselective acylation of nucleosides carrying various substituents (such as the H, F, Cl, Br, I) at 2'- and 5-positions. Experimental data indicated that the catalytic performance of the enzyme depended very much on the halo-substituents in nucleosides. The increased bulk of 2'-substituents in ribose moiety of the nucleoside might contribute to the improved 3'-regioselectivity (90-98%, nucleosides a-d) in enzymatic decanoylation, while the enhancement of regioselectivity (93-99%) in 3'-O-acylated nucleosides e-h could be attributable to the increasing hydrophobicity of the halogen atoms at 5-positions. With regard to the chain-length selectivity, P. cepacia lipase displayed the highest 3'-regioselectivity toward the longer chain (C14) as compared to shorter (C6 and C10) ones. The position, orientation and property of the substituent, specific structure of the lipase's active site, and acyl structure could account for the diverse results.
School of Life Science and Chemical Engineering, Huaiyin Institute of Technology, Huai'an 223003, PR China; Jiangsu Provincial Engineering Laboratory for Biomass Conversion and Process Integration, Huai'an 223005, PR China. Electronic address: biowzy@126.com.
Zhao-Yu
ZY
Wang
School of Life Science and Chemical Engineering, Huaiyin Institute of Technology, Huai'an 223003, PR China.
Yan-Hong
YH
Bi
School of Life Science and Chemical Engineering, Huaiyin Institute of Technology, Huai'an 223003, PR China.
Rong-Ling
RL
Yang
Academy of State Administration of Grain, Beijing 100037, PR China.
Zhang-Qun
ZQ
Duan
School of Life Science and Chemical Engineering, Huaiyin Institute of Technology, Huai'an 223003, PR China.
Ling-Hong
LH
Nie
School of Life Science and Chemical Engineering, Huaiyin Institute of Technology, Huai'an 223003, PR China; Jiangsu Provincial Engineering Laboratory for Biomass Conversion and Process Integration, Huai'an 223005, PR China.
Xiang-Qian
XQ
Li
Lab of Applied Biocatalysis, South China University of Technology, Guangzhou 510640, PR China.
Min-Hua
MH
Zong
School of Life Science and Chemical Engineering, Huaiyin Institute of Technology, Huai'an 223003, PR China.
Jie
J
Wu
D000215:Acylation; D016956:Burkholderia cepacia / Q000201:enzymology*; D002384:Catalysis; D004800:Enzymes, Immobilized / Q000737:chemistry / Q000378:metabolism*; D008049:Lipase / Q000737:chemistry / Q000378:metabolism*; D009705:Nucleosides / Q000378:metabolism*; D013237:Stereoisomerism; D013379:Substrate Specificity
D004800:Enzymes, Immobilized; D009705:Nucleosides; D008049:Lipase
Enzymatic acylation; Halo-substituent recognition; Nucleoside modification; Pseudomonas cepacia lipase