Asymmetric β‐Methylation of l‐ and d‐α‐Amino Acids by a Self‐Contained Enzyme Cascade. Issue 18 (11th March 2020)

• Record Type: Journal Article
• Authors: Liao, Cangsong; Seebeck, Florian P.
• Is Part Of: Angewandte Chemie international edition. Volume 59:Issue 18(2020)
• Page Start: 7184
• Page End: 7187
• Publication Date: 2020-03-11
• Subjects: amino acids -- biocatalysis -- methyltransferase -- S-adenosylmethionine -- stereoselective C-alkylation; Chemistry -- Periodicals; 540
• DOI: 10.1002/anie.201916025
• Languages: English
• ISSNs: 1433-7851

Abstract

Abstract: This report describes a modular enzyme‐catalyzed cascade reaction that transforms l ‐ or d ‐α‐amino acids to β‐methyl‐α‐amino acids. In this process an α‐amino acid transaminase, an α‐keto acid methyltransferase, and a halide methyltransferase cooperate in two orthogonal reaction cycles that mediate product formation and regeneration of the cofactor pyridoxal‐5′‐phosphate and the co‐substrate S‐adenosylmethionine. The only stoichiometric reagents consumed in this process are the unprotected l ‐ or d ‐α‐amino acid and methyl iodide. Abstract : A modular enzyme‐catalyzed one‐pot reaction that produces l ‐ and d ‐β‐methyl‐α‐amino acids from unprotected l ‐ or d ‐α‐amino acids is described. In this system an α‐amino acid transaminase (TA), an α‐keto acid methyltransferase (MT), and a halide methyltransferase (HMT) cooperate in two orthogonal reaction cycles that mediate product formation and regeneration of the cofactor pyridoxal‐5′‐phosphate and the co‐substrate S‐adenosylmethionine.