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Issue 2, 1988
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Biotransformations with acetolactate decarboxylase: unusual conversions of both substrate enantiomers into products of high optical purity

Abstract

Acetolactate decarboxylase catalyses the decarboxylation of both enantiomers of 2-ethyl-2-hydroxy-3-oxobutanoate to isomeric ketois of high optical purity and both enantiomers of α-acetolactate (2-hydroxy-2-methyl-3-oxobutanoate) to acetoin (3-hydroxybutan-2-one) of high optical purity.

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Article type: Paper
DOI: 10.1039/C39880000098
J. Chem. Soc., Chem. Commun., 1988, 98-99

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    Biotransformations with acetolactate decarboxylase: unusual conversions of both substrate enantiomers into products of high optical purity

    D. H. G. Crout and D. L. Rathbone, J. Chem. Soc., Chem. Commun., 1988, 98
    DOI: 10.1039/C39880000098

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