DIAMINOPIMELIC ACID DECARBOXYLASE OF THE AGENT OF MENINGOPNEUMONITIS

Author:

Moulder James W.1,Novosel Dorothy L.1,Tribby Ilse C.1

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.

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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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