Unexpected enantioselectivity and activity of penicillin acylase in the resolution of methyl 2,2-dimethyl-1,3-dioxane-4-carboxylate

The penicillin acylase (PA) from E. coli catalyzes the hydrolytic kinetic resolution of methyl 2,2-dimethyl-1,3-dioxane-4-carboxylate with remarkably high enantioselectivity and catalytic efficiency. This result is highly unusual as this ester does not contain the phenylacetic acid residue, normally...

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Bibliographic Details
Published in:Journal of molecular catalysis. B, Enzymatic Enzymatic, 2003-04, Vol.22 (1), p.55-59
Main Authors: Yao, Yiming, Lalonde, Jim J
Format: Article
Language:English
Subjects:
Bioconversions. Hemisynthesis
Biological and medical sciences
Biotechnology
C3 chiral synthon
Dioxalane
Enantioselective kinetic resolution
Fundamental and applied biological sciences. Psychology
Methods. Procedures. Technologies
Methyl 2,2-dimethyl-1,3-dioxane-4-carboxylate
Penicillin acylase
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Summary:The penicillin acylase (PA) from E. coli catalyzes the hydrolytic kinetic resolution of methyl 2,2-dimethyl-1,3-dioxane-4-carboxylate with remarkably high enantioselectivity and catalytic efficiency. This result is highly unusual as this ester does not contain the phenylacetic acid residue, normally considered to be a prerequisite for high activity and enantioselectivity in PA catalyzed resolutions. The apparent enantioselectivity ( E app) was found to be high (>50) at neutral or slightly acidic pH and to decrease at more alkaline pH (>7.5) due to significant non-specific chemical hydrolysis. Similarly, enantioselectivity increased with decreasing temperature. The substrate concentration had only a slight effect on enantioselectivity and activity. The rate of hydrolysis of ester 1 is comparable to that for PA’s “natural” substrate, penicillin G.
ISSN:1381-1177
1873-3158
DOI:10.1016/S1381-1177(03)00004-3