Asymmetric β-Methylation of l- and d-α-Amino Acids by a Self-Contained Enzyme Cascade

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Asymmetric β-Methylation of l- and d-α-Amino Acids by a Self-Contained Enzyme Cascade

JournalArticle (Originalarbeit in einer wissenschaftlichen Zeitschrift)

ID	4607246
Author(s)	Liao, Cangsong; Seebeck, Florian P.
Author(s) at UniBasel	Liao, Cangsong Seebeck, Florian Peter
Year	2020
Title	Asymmetric β-Methylation of l- and d-α-Amino Acids by a Self-Contained Enzyme Cascade
Journal	Angewandte Chemie International Edition
Volume	59
Number	18
Pages / Article-Number	7184-7187
Keywords	S-adenosylmethionine; amino acids; biocatalysis; methyltransferase; stereoselective C-alkylation
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.
Publisher	Wiley
ISSN/ISBN	1433-7851 ; 1521-3773
edoc-URL	https://edoc.unibas.ch/79597/
Full Text on edoc	Restricted
Digital Object Identifier DOI	10.1002/anie.201916025
PubMed ID	http://www.ncbi.nlm.nih.gov/pubmed/32048779
Document type (ISI)	Journal Article

11/05/2024

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