Acetohydroxyacid synthase: A new enzyme for chiral synthesis of R-phenylacetylcarbinol

• Published in: Biotechnology and bioengineering Vol. 83; no. 7; pp. 833 - 840
• Main Authors: Engel, Stanislav, Vyazmensky, Maria, Geresh, Shimona, Barak, Ze'ev, Chipman, David M.
• Format: Journal Article
• Language: English
• Published: Hoboken Wiley Subscription Services, Inc., A Wiley Company 30.09.2003; Wiley
• Subjects: acetolactate synthase; Acetolactate Synthase - metabolism; Acetone - analogs & derivatives; Acetone - chemical synthesis; Acetone - chemistry; Acetone - isolation & purification; benzaldehyde; Benzaldehydes; Binding Sites; biocatalysis; Biological and medical sciences; Biotechnology; Catalysis; chiral; enantiomeric excess; Enzyme engineering; Escherichia coli - enzymology; Escherichia coli - genetics; Fermentation; Fundamental and applied biological sciences. Psychology; hydroxyketone; Isoenzymes - metabolism; Methods. Procedures. Technologies; Miscellaneous; Molecular Structure; pyruvate; pyruvate decarboxylase; Pyruvic Acid; Stereoisomerism; stereospecificity; Temperature; thiamin diphosphate; Time Factors; chiral; Enzyme; thiamin diphosphate; Benzaldehyde; Lyases; enantiomeric excess; pyruvate; biocatalysis; Biocatalyst; Oxo-acid-lyases; Carbon-carbon lyases; Carboxy-lyases; Chirality; Acetolactate synthase; Stereospecificity; hydroxyketone; Pyruvate decarboxylase

We have found that acetohydroxyacid synthase (AHAS) is an efficient catalyst for the enantiospecific (≥98% enantiomeric excess) synthesis of (R)‐phenylacetylcarbinol (R‐PAC) from pyruvate and benzaldehyde, despite the fact that its normal physiological role is synthesis of (S)‐acetohydroxyacids from...