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.