A cobamide-requiring glycerol dehydrase from an acrolein-forming lactobacillus

A glycerol dehydrase has been isolated from Lactobacillus 208-A which requires a cobamide coenzyme and a univalent cation for activity. The enzyme is measured by the colorimetric determination of the acrolein formed from β-hydroxypropionaldehyde produced from glycerol by the dehydrase. Vitamin B 12 inhibits the dehydrase. The degree of inhibition by vitamin B 12 is greater when it contacts the apoenzyme before the cobamide coenzyme. The toxicity of mercurial compounds can be relieved by cobamide coenzymes or by 2,3-dimercaptopropanol (BAL). This dehydrase has an optimum pH of 5.8–6.0.