Regio- and Stereoselective Aliphatic-Aromatic Cross-Benzoin Reaction: Enzymatic Divergent Catalysis

The catalytic asymmetric synthesis of chiral 2‐hydroxy ketones by using different thiamine diphosphate dependent enzymes, namely benzaldehyde lyase from Pseudomonas fluorescens (PfBAL), a variant of benzoylformate decarboxylase from Pseudomonas putida (PpBFD‐L461A), branched‐chain 2‐keto acid decarb...

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Bibliographic Details
Published in:	Chemistry : a European journal Vol. 22; no. 39; pp. 13999 - 14005
Main Authors:	Beigi, Maryam, Gauchenova, Ekaterina, Walter, Lydia, Waltzer, Simon, Bonina, Fabrizio, Stillger, Thomas, Rother, Dörte, Pohl, Martina, Müller, Michael
Format:	Journal Article
Language:	English
Published:	Germany Blackwell Publishing Ltd 19-09-2016 Wiley Subscription Services, Inc
Subjects:	Accessibility Acetobacter - enzymology Acetobacter pasteurianus Acetone - analogs & derivatives Acetone - chemical synthesis Acetone - chemistry Acetophenone Aldehyde-Lyases - chemistry Aldehydes Aldehydes - chemistry Aliphatic compounds Asymmetric synthesis Asymmetry Benzaldehyde Benzoin Benzoin - chemistry Benzoylformate decarboxylase Biocatalysis Carboxy-Lyases - chemistry Catalysis Catalysts Chain branching Chains Chemical synthesis Chemistry Chemistry Techniques, Synthetic - methods C−C coupling Derivatives Enzymes Hydroxypropiophenone - chemical synthesis Hydroxypropiophenone - chemistry Ketones Lactococcus lactis Lactococcus lactis - enzymology Phenylacetylcarbinol Pseudomonas Pseudomonas fluorescens Pseudomonas fluorescens - enzymology Pseudomonas putida Pseudomonas putida - enzymology Pyruvate decarboxylase Pyruvic acid Stereochemistry Stereoisomerism Substrates Synthesis Thiamine Thiamine diphosphate Thiamine Pyrophosphate - chemistry vitamin B1 thiamine diphosphate asymmetric synthesis C−C coupling biocatalysis vitamin B1
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Summary:	The catalytic asymmetric synthesis of chiral 2‐hydroxy ketones by using different thiamine diphosphate dependent enzymes, namely benzaldehyde lyase from Pseudomonas fluorescens (PfBAL), a variant of benzoylformate decarboxylase from Pseudomonas putida (PpBFD‐L461A), branched‐chain 2‐keto acid decarboxylase from Lactococcus lactis (LlKdcA) and a variant of pyruvate decarboxylase from Acetobacter pasteurianus (ApPDC‐E469G), was studied. Starting with the same set of substrates, substituted benzaldehydes in combination with different aliphatic aldehydes, PfBAL and PpBFD‐L461A selectively deliver the (R)‐ and (S)‐2‐hydroxy‐propiophenone derivatives, respectively. The (R)‐ and (S)‐phenylacetylcarbinol (1‐hydroxy‐1‐phenylacetone) derivatives are accessible in a similar way using LlKdcA and ApPDC‐E469G, respectively. In many cases excellent stereochemical purities (>98 % enantiomeric excess) could be achieved. Hence, the regio‐ and stereochemistry of the product in the asymmetric aliphatic–aromatic cross‐benzoin reaction can be controlled solely by choice of the appropriate enzyme or enzyme variant. Divergent biocatalysis: The catalytic asymmetric synthesis of chiral 2‐hydroxy ketones using different thiamine diphosphate dependent enzymes, namely PfBAL, PpBFD‐L461A, LlKdcA and ApPDC‐E469G, was studied (see scheme). The results show that the regio‐ and stereochemistry of the product in the reaction can be controlled solely by choice of the appropriate enzyme.
Bibliography:	istex:AE4EEA69D922C37E4B58E725415CF70325A96ED3 DFG ark:/67375/WNG-6FHMW98B-0 ArticleID:CHEM201602084 ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23
ISSN:	0947-6539 1521-3765
DOI:	10.1002/chem.201602084