Degree Type


Date of Award


Degree Name

Doctor of Philosophy



First Advisor

Paul A. Hartman

Second Advisor

Milton J. Allison


Strictly anaerobic wall-less bacteria (Class Mollicutes, Order Anaeroplasmatales) were examined for enzymic activities of carbohydrate, purine, and pyrimidine metabolism. Cell-free extracts of Anaeroplasma intermedium and Asteroleplasma anaerobium had enzymic activities of the Embden-Meyerhof-Parnas pathway and the nonoxidative portion of the pentose phosphate pathway. The phosphofructokinase (PFK) of An. intermedium was pyrophosphate-dependent (PP[subscript] i-dependent) whereas the PFK of As. anaerobium was active only with ATP. In addition, An. intermedium had pyruvate kinase activity and As. anaerobium had activity for pyruvate, orthophosphate dikinase. An. intermedium was able to carboxylate phosphoenolpyruvate (PEP) to oxaloacetate via PEP carboxykinase and possibly PEP carboxytransphosphorylase; As. anaerobium did not have activities for either enzyme. In the tricarboxylic acid cycle, An. intermedium had malate dehydrogenase and isocitrate dehydrogenase, but As. anaerobium had only malate dehydrogenase activity. As. anaerobium possessed enzymes for purine salvage, interconverting purine bases, (deoxy)ribonucleosides, and (deoxy)ribomononucleotides; the nucleoside kinase was PP[subscript] i-dependent. As. anaerobium possessed enzymic activities for salvage synthesis of dTDP, but it lacked detectable activities for dCMP deaminase and cytidine deaminase;Walled bacteria that are phylogenetically related to the Mollicutes were examined for PP[subscript] i-dependent enzymes as indicators of their relatedness. Clostridium innocuum, Streptococcus pleomorphus, and Erysipelothrix rhusiopathiae had PP[subscript] i-PFK, and the PFK of Clostridium ramosum, Lactobacillus catenaformis, and Lactobacillus vitulinus was ATP-dependent. All the walled relatives except E. rhusiopathiae had pyruvate, orthophosphate dikinase. C. innocuum, C. ramosum, and S. pleomorphus had PEP carboxytransphosphorylase. The acetate kinases of all the bacteria, including the strictly anaerobic mollicutes, were active with ATP but not PP[subscript] i. The pyruvate kinase activities of C. innocuum, C. ramosum, and S. pleomorphus were activated to a greater extent by glucose 6-phosphate than by fructose 1,6-bisphosphate. AMP was the best activator in the two lactobacilli. The distributions of PP[subscript] i-dependent enzymes among these bacteria correlated with the proposed subdivisions of this group based on rRNA analyses.



Digital Repository @ Iowa State University,

Copyright Owner

James P. Petzel



Proquest ID


File Format


File Size

151 pages

Included in

Microbiology Commons