Abstract
Bacteria (Micrococcus ureae) were grown in a medium containing 2,3-butanediol or acetylmethylcarbinol as the sole source of C and energy. Cell-free extracts of these bacteria contain an enzyme that irreversibly converts diacetyl to di-acetylmethylcarbinol and acetic acid. The enzyme was purified and the stoichiometry of the reaction studied. Diacetylmethylcarbinol is an acyloin condensation product, and diphosphothiamine and a divalent cation, such as Mg, are cofactors for the enzyme involved in the synthesis. Several inhibitors of the system were tested. Diacetyl is not oxidized either aerobically or anaerobically in the presence of ferricyanide. The enzyme is specific for diacetyl and related alpha-dike-tones and will not degrade pyruvic acid. Diacetylmethyl carbinol is a fairly strong inhibitor of its own synthesis. Artifacts encountered when using diacetyl as a substrate are discussed.

This publication has 20 references indexed in Scilit: