Regioselective enzymatic acylation of methyl shikimate. Influence of acyl chain length and solvent polarity on enzyme specificity.
Candida antarctica lipase A (CAL-A) selectively catalyzes the acylation at the secondary C-4 hydroxyl group of methyl shikimate (2), which possesses three secondary hydroxyl groups, the C-3 allylic one being chemically more reactive. The effect both of the acyl group of the acylating agents and of the solvent polarity has been studied. The selectivity of CAL-A is almost complete with acyl donors that possess short chains. However, when acyl donors have longer chains, better results are obtained by C. antarctica lipase B (CAL-B).
Armesto
Nuria
N
Departamento de Química Orgánica e Inorgánica, Facultad de Química, Universidad de Oviedo, 33071-Oviedo, Spain.
Ferrero
Miguel
M
Fernández
Susana
S
Gotor
Vicente
V
D000215:Acylation; D016956:Burkholderia cepacia / Q000201:enzymology; D002175:Candida / Q000201:enzymology*; D002384:Catalysis; D002855:Chromatography, Thin Layer; D008049:Lipase / Q000378:metabolism*; D015394:Molecular Structure; D012765:Shikimic Acid / Q000031:analogs & derivatives* / Q000378:metabolism*; D013237:Stereoisomerism; D013329:Structure-Activity Relationship; D013379:Substrate Specificity; D013696:Temperature
C453473:methyl shikimate; D012765:Shikimic Acid; D008049:Lipase