The functional pathway of lysine biosynthesis in Escherichia coli

Rhuland, L. E.; Hamilton, Ramon D.

doi:10.1016/0006-3002(61)90609-6

Cited by 9 publications

(1 citation statement)

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“…The principal, and probably only, pathway of lysine biosynthesis in bacteria is via DAP (Dewey and Work, 1952;Davis, 1952;Vogel, 1959c; Rhuland and Hamilton, 1961;Finlayson and Simpson, 1961). Therefore, the presence of DAP decarboxylase in the agent of meningopneumonitis and the absence of any exogenous lysine requirement for multiplication of the 6BC strain of psittacosis agent in L cells (Bader and Morgan, 1958) may be explained by assuming that members of the psittacosis group make their own lysine via DAP.…”

Section: Discussionmentioning

confidence: 99%

Diaminopimelic Acid Decarboxylase of the Agent of Meningopneumonitis

1963

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Evidence is presented for the presence in meningopneumonitis particles and extracts of an enzyme decarboxylating a, Ediaminopimelic 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. Bader and MIorgan (1958) observed that lysine is not required for multiplication of the 6BC strain of psittacosis agent in L cells, although this amino acid is a constituent of the agent (Ross and Gogolak, 1957) and is necessary for growth of the L cells themselves (Eagle, 1955). This suggested that members of the psittacosis group may synthesize their own lysine via a, E-diaminopimelic acid (DAP) as do bacteria (Dewey and Work, 1952; Davis, 1952). This hypothesis was tested by examining concentrated suspensions of the agent of meningopneumonitis, a typical member of the psittacosis group and also known to contain lysine (Jenkin, 1960), for diaminopimelic acid decarboxylase (Dewey, Hoare, and Work, 1954), the enzyme catalyzing the final step in the bacterial synthesis of DAP. The search was facilitated by the absence of this enzyme in the chick embryo host.

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Section: Discussionmentioning

confidence: 99%