Some of the wall-less bacteria of the class (mycoplasmas) have pyrophosphate (PP)-dependent enzymic activities, including PP-dependent phosphofructokinase (PP-PFK), PP-dependent nucleoside kinase, and pyruvate, orthophosphate dikinase (PPDK) activities. In most other bacteria, adenosine 5′-triphosphate (ATP), not PP, is the cofactor of analogous enzymic reactions. Because PP-dependent enzymes are more common among mollicutes than other bacteria, we describe here an examination of the six walled bacteria that have been reported to be phylogenetically related to the mollicutes (, and ) for PP-PFK, ATP-dependent PFK, phosphoenolpyruvate carboxytransphosphorylase, PPDK, and PP- and ATP-dependent acetate kinases. Two anaerobic mollicutes, and , were also tested. , and had PP-PFK activities, whereas , the two lactobacilli, and had only ATP-dependent PFK activities. and all of the walled bacteria except had PPDK activities. All of the species except and also had pyruvate kinase activities; the effects of allosteric activators were tested. Phosphoenolpyruvate carboxytransphosphorylase was detected by using two methods in , and . All of the species tested had ATP-dependent acetate kinase activities, but none had detectable PP-dependent acetate kinase activity. The occurrence of one or more PP-dependent enzymes in the mollicutes and their walled relatives is a phenotypic indicator of the phylogenetic relatedness of these organisms. The distribution of these enzymes among members of this group substantiates the subgroups proposed by other workers who used 16S ribosomal ribonucleic acid analysis.


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