Affiliation:
1. Department of Microbiology, University of Chicago, Chicago, Illinois
Abstract
Moulder, James
W. (University of Chicago, Chicago, Ill.),
Dorothy L. Novosel, and Ilse C. Tribby
. Diaminopimelic acid decarboxylase of the agent of meningopneumonitis. J. Bacteriol.
85:
701–706. 1963.—Evidence is presented for the presence in meningopneumonitis particles and extracts of an enzyme decarboxylating α, ε-diaminopimelic acid to lysine and for the absence of a corresponding enzyme in the uninfected host. Properties of the enzyme are described and compared with those of bacterial diaminopimelic acid decarboxylases. The significance of these observations with respect to the mode of lysine biosynthesis in the psittacosis group and to its phylogenetic origin is pointed out.
Publisher
American Society for Microbiology
Subject
Molecular Biology,Microbiology
Reference26 articles.
1. Lysine, methionine and tryptophan content of microorganisms;ANDERSON R. F.;I. Bacteria. J. Bacteriol.,1958
2. Latent viral infection of cells in tissue culture. VI. Role of amino acids, glutamine and glucose in psittacosis virus propagation in L cells;BADER J. D.;J. Exptl. Med.,1958
3. Phosphorus assay in column chromatography;BARTLETT G. R.;J. Biol. Chem.,1959
4. Enzymes for formation of citrovorum factor in members of the psittacosis group of microorganisms;COL N, J;J. Bacteriol.,1960
5. The role of folic acid in the metabolism of members of the psittacosis group of microorganisms;COL N, J;Ann. N. Y. Acad. Sci.,1962
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