Role of vitamin B12 and enzymes related to methylmalonyl-CoA mutase in a methanol-utilizing bacterium, Protaminobacter ruber.

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Abstract
A methanol-utilizing bacterium, P. ruber, required Co ion or vitamin B12 as its growth factor, which could be replaced by succinate among various additions to the Co-deficient medium. The presence of adenosylcobalamin (adenosyl-B12)-dependent methylmalonyl CoA mutase was demonstrated in the cell-free extracts of P. ruber. The specific activity of this mutase was not only fairly high in comparison with that reported with other organisms but also detected at a similar level throughout the cultivation period. The cell-free extracts of P. ruber grown on non-C1 compounds as a sole C and energy source also had methylmalonyl-CoA mutase activity. The extracts of this microorganism catalyzed the reactions from propionyl-CoA to succinyl-CoA and from .alpha.-ketoglutarate to .alpha.-hydroxyglutarate.

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