The role of manganese in growth and sporulation of Bacillus subtilis.
Phosphoglycerate phosphomutase of Bacillus subtilis, Bacillus cereus and Bacillus megaterium required Mn2+ as cofactor, whereas the wheat germ and rabbit liver enzymes did not. In the absence of Mn2+, B. subtilis did not sporulate in normal sporulation media but it did sporulate if the proper ratio of glucose or glycerol and malate was used. Decoyinine, an inhibitor of guanosine monophosphate synthesis, induced sporulation in the presence of excess glucose and malate to the same extent with and without Mn2+. Apparently, phosphoglycerate phosphomutase is the only strictly Mn2+-requiring enzyme needed for optimal sporulation in normal sporulation media.
D000241:Adenosine / Q000031:analogs & derivatives / Q000494:pharmacology; D001412:Bacillus subtilis / Q000201:enzymology / Q000254:growth & development / Q000502:physiology*; D008345:Manganese / Q000494:pharmacology / Q000502:physiology*; D010736:Phosphoglycerate Mutase / Q000378:metabolism; D013171:Spores, Bacterial / Q000187:drug effects
D008345:Manganese; D010736:Phosphoglycerate Mutase; D000241:Adenosine