Enantioselective Synthesis of (S)-2-Hydroxypropanone Derivatives by Benzoylformate Decarboxylase Catalyzed C−C Bond Formation

Abstract

Chiral 2-hydroxypropanone derivatives 5a−v, 8a−d, and 10a, b were formed by benzoylformate decarboxylase (BFD) catalyzed C−C bond formation. A donor aldehyde and acetaldehyde as an acceptor were carboligated in aqueous buffer solution with remarkable ease in high chemical yield and good to high optical purity. The substrate range of this thiamin diphosphate dependent enzyme was examined to employ this benzoin condensation type reaction in stereoselective synthesis. The observed dependence of the enantiomeric excess on the substitution pattern could be exploited to design sub-

Stereoselective synthesis of bulky 1,2-diols with alcohol dehydrogenases

“…The synthesis was carried out according to the literature. 16,17 Spectroscopic data are in full agreement with those previously published.…”

“…The substrate was synthesised as previously described. 16,17 Spectroscopic data are again in full agreement with the literature.…”

Stereoselective synthesis of bulky 1,2-diols with alcohol dehydrogenases

“…The synthesis was carried out according to the literature. 16,17 Spectroscopic data are in full agreement with those previously published.…”

“…The substrate was synthesised as previously described. 16,17 Spectroscopic data are again in full agreement with the literature.…”

Hydrophobic Complexation Promotes Enzymatic Surfactant Synthesis from Alkyl Glucoside/Cyclodextrin Mixtures

“…After a given threshold (in Figure ), however, complexation will affect or even inhibit the enzymatic reaction, and the complexation limited regime is reached (comparable to the donor-limiting regime in Figure ). Especially for other reaction systems not utilizing CD as an actual substrate, complexation usually causes enzyme inhibition. ,, However, some enzymes, because of their active site architecture, may utilize the complex in a manner similar to what we have reported in this article for CGTase. Thus, complexation may lead to increased pseudomonomer availability by forming reactive complexes (scenario 1 in Figure ) and thereby changing kinetic parameters.…”

“…Especially for other reaction systems not utilizing CD as an actual substrate, complexation usually causes enzyme inhibition. 18,52,53 However, some enzymes, because of their active site architecture, may utilize the complex in a manner similar to what we have reported in this article for CGTase. Thus, complexation may lead to increased pseudomonomer availability by forming reactive complexes (scenario 1 in Figure 9) and thereby changing kinetic parameters.…”

Propioin synthesis using thiamine diphosphate‐dependent enzymes

“…This hints to a high K M value for this substrate, as saturation of the active centers could not be achieved up to 1500 mM. This is not surprising, because propanal is quite small and it is well known that BFD prefers aromatic substrates 9, 17. The same kinetic behavior of BFD was reported for the decarboxylation of pyruvate and 2‐keto‐4‐methylhexanoic acid as substrates 21…”

Stereoselective synthesis of bulky 1,2-diols with alcohol dehydrogenases

“…The synthesis was carried out according to the literature. 16,17 Spectroscopic data are in full agreement with those previously published.…”

“…The substrate was synthesised as previously described. 16,17 Spectroscopic data are again in full agreement with the literature.…”

Hydrophobic Complexation Promotes Enzymatic Surfactant Synthesis from Alkyl Glucoside/Cyclodextrin Mixtures

“…After a given threshold (in Figure ), however, complexation will affect or even inhibit the enzymatic reaction, and the complexation limited regime is reached (comparable to the donor-limiting regime in Figure ). Especially for other reaction systems not utilizing CD as an actual substrate, complexation usually causes enzyme inhibition. ,, However, some enzymes, because of their active site architecture, may utilize the complex in a manner similar to what we have reported in this article for CGTase. Thus, complexation may lead to increased pseudomonomer availability by forming reactive complexes (scenario 1 in Figure ) and thereby changing kinetic parameters.…”

“…Especially for other reaction systems not utilizing CD as an actual substrate, complexation usually causes enzyme inhibition. 18,52,53 However, some enzymes, because of their active site architecture, may utilize the complex in a manner similar to what we have reported in this article for CGTase. Thus, complexation may lead to increased pseudomonomer availability by forming reactive complexes (scenario 1 in Figure 9) and thereby changing kinetic parameters.…”

Propioin synthesis using thiamine diphosphate‐dependent enzymes

“…This hints to a high K M value for this substrate, as saturation of the active centers could not be achieved up to 1500 mM. This is not surprising, because propanal is quite small and it is well known that BFD prefers aromatic substrates 9, 17. The same kinetic behavior of BFD was reported for the decarboxylation of pyruvate and 2‐keto‐4‐methylhexanoic acid as substrates 21…”

Stereoselective synthesis of bulky 1,2-diols with alcohol dehydrogenases

“…The synthesis was carried out according to the literature. 16,17 Spectroscopic data are in full agreement with those previously published.…”

“…The substrate was synthesised as previously described. 16,17 Spectroscopic data are again in full agreement with the literature.…”

Hydrophobic Complexation Promotes Enzymatic Surfactant Synthesis from Alkyl Glucoside/Cyclodextrin Mixtures

“…After a given threshold (in Figure ), however, complexation will affect or even inhibit the enzymatic reaction, and the complexation limited regime is reached (comparable to the donor-limiting regime in Figure ). Especially for other reaction systems not utilizing CD as an actual substrate, complexation usually causes enzyme inhibition. ,, However, some enzymes, because of their active site architecture, may utilize the complex in a manner similar to what we have reported in this article for CGTase. Thus, complexation may lead to increased pseudomonomer availability by forming reactive complexes (scenario 1 in Figure ) and thereby changing kinetic parameters.…”

“…Especially for other reaction systems not utilizing CD as an actual substrate, complexation usually causes enzyme inhibition. 18,52,53 However, some enzymes, because of their active site architecture, may utilize the complex in a manner similar to what we have reported in this article for CGTase. Thus, complexation may lead to increased pseudomonomer availability by forming reactive complexes (scenario 1 in Figure 9) and thereby changing kinetic parameters.…”

Propioin synthesis using thiamine diphosphate‐dependent enzymes

“…This hints to a high K M value for this substrate, as saturation of the active centers could not be achieved up to 1500 mM. This is not surprising, because propanal is quite small and it is well known that BFD prefers aromatic substrates 9, 17. The same kinetic behavior of BFD was reported for the decarboxylation of pyruvate and 2‐keto‐4‐methylhexanoic acid as substrates 21…”