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Morphological deformity of Bacillus megaterium NCIB758I grown at 37 "C in a minimal chemically defined medium could be prevented by addition of either biotin, aspartate or acetate (Al-ssum & White, 1977). The only carbon source in the minimal medium was glycerol or glucose, and the metabolism of either of these two substrates requires an adequate conversion of C, compounds [e.g. pyruvate or phosphoenolpyruvate (PEP)] to C, compounds anaplerotically, to replace citric acid cycle intermediates that are withdrawn for biosynthesis. Such conversion occurs in bacteria mainly by the action of a C0,-fixing enzyme, either the biotin-dependent pyruvate carboxylase, or the biotinindependent PEP carboxylase; generally, organisms have one or other (not both) of these enzymes (Kornberg, I 966). Anaplerotic synthesis of C, compounds could also occur independently of C0,-fixing enzymes by the operation of the glyoxylate cycle. Another biotinrequiring enzyme is acetyl coenzyme A carboxylase, which catalyses the ATP-dependent carboxylation of acetyl-CoA to yield malonyl-CoA (see review by Vagelos, I 964). In biotindeficient organisms, the activity of this enzyme might be lowered, so that synthesis of fatty acids (via malonyl-CoA) might be impaired. The nutritional evidence suggests that in B. megaterium N C I B ~ ~ ~ z an active pyruvate carboxylase is necessary unless a source of C, compounds (e.g. aspartate) is available or unless the glyoxylate cycle is functioning. In this paper, activities of three anaplerotic enzymes and of acetyl-CoA carboxylase and malic enzyme are compared in organisms grown with and without biotin. A preliminary report of some of these results has been made (Al-ssum & White, 1974).

Activities of Anaplerotic Enzymes and Acetyl Coenzyme A Carboxylase in Biotin-deficient Bacillus megaterium