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- W2009241650 abstract "Methyl N-acetyl phenylserinates (1, 2), methyl N-acetyl nitrophenylserinates (3, 4), and methyl N-benzoyl threoninates (5, 6) were resolved conveniently into the enantiomers with high optical purities by enzymatic hydrolysis in the presence of α-chymotrypsin, subtilisin, or bromelain. The threo and erythro forms were treated separately and the latter form was usually more reactive. Chymotrypsin and subtilisin are highly specific for the enantiomer having the same configuration on carbon-2 (S) as the natural standard amino acids. In contrast, bromelain shows the reverse specificity on phenylserine derivatives. This is a notable exception to the usual S-stereospecificity pattern of proteases. Keywords: enzymatic hydrolysis, resolution of amino acids." @default.
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- W2009241650 date "1990-06-01" @default.
- W2009241650 modified "2023-10-17" @default.
- W2009241650 title "Resolution of β-hydroxy-α-amino acids by the action of proteases on their N-acyl methyl esters" @default.
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- W2009241650 doi "https://doi.org/10.1139/v90-150" @default.
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