Comparative Biosynthesis of Ornithine and Lysine by Mycoplasma and L Forms

AUTOR(ES)

Smith, Paul F.

RESUMO

Smith, Paul F. (University of South Dakota, Vermillion). Comparative biosynthesis of ornithine and lysine by Mycoplasma and L forms. J. Bacteriol. 92:164–169. 1966.—Seven species of Mycoplasma, two L forms not requiring salt and their parent bacteria, and two yeasts were examined for enzymes involved in the biosynthesis of ornithine and lysine. All organisms tested, except two species of Mycoplasma and the yeasts, decarboxylated meso-α, ε-diaminopimelic acid. None of the Mycoplasma species or L forms was capable either of reducing α-aminoadipic acid to its semialdehyde or of incorporating α-aminoadipic acid-6-C14 into lysine. All organisms, except the yeasts and Mycoplasma sp. caprine strain 14, acetylated glutamic acid, and all organisms possessed Nα-acetyl-l-ornithine:2-oxo-glutarate aminotransferase activity. Nα-acetylornithase activity was negligible in all organisms except Proteus and its L form. No transacetylation between acetylglutamic acid and ornithine, and vice versa, was demonstrable in any of the organisms. Mycoplasma species appear to possess the bacterial pathway to lysine. Ornithine does not appear to arise from glutamic acid.

Documentos Relacionados

• Comparative Biosynthesis of Mevalonic Acid by Mycoplasma
• Morphology and Reproductive Processes of the L Forms of Bacteria II. Comparative Study of L Forms and Mycoplasma with the Electron Microscope
• The L box regulon: Lysine sensing by leader RNAs of bacterial lysine biosynthesis genes
• Vital Staining of Mycoplasma and L-Forms with Chlorazol Black E
• Permanent Stained Agar Preparation of Mycoplasma and of L Forms of Bacteria