Abstract
A coenzyme B(12)-dependent glycerol dehydratase from Lactobacillus reuteri has been purified and characterized. The dehydratase has a molecular weight of approximately 200,000, and sodium dodecyl sulfate-polyacrylamide gel electrophoresis yielded a single major band with a molecular weight of 52,000. K(m) values for substrates and coenzyme B(12) were in the millimolar and the submicromolar range, respectively.
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