Abstract
Bacteria grown on a 2,3-butanediol-mineral medium elaborate a 2,3-butanediol dehydrogenase lacking in substrate specificity. The same enzyme seems to be involved in more than one reaction of the pathway for the dissimilation of 2,3-butanediol. 2,3-Butanediol dehydrogenases from several glucose-grown microorganisms have different substrate specificities as well as different substrate affinities. Aerobacter aerogenes forms different 2,3-butanediol dehydrogenases when grown with glucose and acetylmethylcarbinol as C sources. These investigations have failed to furnish evidence for the existence of a diacetyl reductase enzyme distinct from 2,3-butanediol dehydrogenase. The properties of 2,3-butanediol dehydrogenases from several sources were studied and compared.

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