Journal
ACS CATALYSIS
Volume 9, Issue 6, Pages 5657-5667Publisher
AMER CHEMICAL SOC
DOI: 10.1021/acscatal.9b01084
Keywords
biocatalysis; enantioselectivity; density functional theory; carboligation; benzoylformate decarboxylase; reaction mechanism; enzymology; asymmetric synthesis
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Funding
- Swedish Research Council
- National Science Foundation [CHE 1306877]
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Benzoylformate decarboxylase (BFDC) is a thiamin-diphosphate enzyme that catalyzes the decarboxylation of benzoylformate to yield benzaldehyde and carbon dioxide. In addition to its natural reaction, BFDC is able to catalyze carboligation reactions in a highly enantioselective fashion, making the enzyme a potentially important biocatalyst. Here we use density functional theory calculations to investigate the detailed mechanism of BFDC-catalyzed carboligation and to elucidate the sources of the enantioselectivity. Benzaldehyde and acetaldehyde are studied as acceptors, for, when reacting with a benzaldehyde donor, they yield products with opposite enantiospecificity. For each of the acceptors, several possible binding modes to the active site are initially examined before the individual reaction paths leading to the two enantiomeric products are followed. The calculated energies are in good agreement with the experimental results, and the analysis of the transition states gives insight into the origins of the enantioselectivity.
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