Abstract
The substrate specificity of the recently discovered enzyme, opine dehydrogenase (ODH) from Arthrobacter sp. strain 1C for amino donors in the reaction that forms secondary amines using pyruvate as a fixed amino acceptor is examined. The enzyme was active toward short-chain aliphatic ( S)-amino acids and those substituted with acyloxy, phosphonooxy, and halogen groups. The enzyme was named N-[1-( R)-(car☐yl)ethyl]-( S)-norvaline: NAD + oxidoreductase (L-norvaline forming). Other substrates for the enzyme were 3-aminobutyric acid and ( S)-phenylalaninol. Optically pure opine-type secondary amine car☐ylic acids were synthesized from amino acids and their analogs such as ( S)-methionine, ( S)-isoleucine, ( S)-leucine, ( S)-valine, ( S)-phenylalanine, ( S)-alanine, ( S)-threonine, ( S)-serine, and ( S)-phenylalaninol, and α-keto acids such as glyoxylate, pyruvate, and 2-oxobutyrate using the enzyme, with regeneration of NADH by formate dehydrogenase (FDH) from Moraxella sp. C-1. The absolute configuration of the nascent asymmetric center of the opines was of the ( R) stereochemistry with > 99.9% e.e. One-pot synthesis of N-[1-( R)-(car☐yl)ethyl]-( S)-phenylalanine from phenylpyruvate and pyruvate by using ODH, FDH, and phenylalanine dehydrogenase (PheDH) from Bacillus sphaericus, is also described.
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