Variation of activity of bacterial diaminopimelate decarboxylase under different conditions of growth

White, Peter J; Kelly, Bridget; Suffling, Audrey; Work, Elizabeth

doi:10.1042/bj0910600

Cited by 28 publications

(34 citation statements)

References 33 publications

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“…This was confirmed by data which showed that 8 hr hyphae oxidized glucose when the organisms were pre-incubated with Cetavlon. This surface-active agent has been used in amino acid decarboxylase assays to increase cell permeability (White et al 1964). When 8 hr hyphae were incubated with 0403 m-Cetavlon in the Warburg flasks, endogenous metabolism was maintained but permeability was increased sufficiently to allow glucose to penetrate, and oxygen uptake was stimulated.…”

Section: Discussionmentioning

confidence: 99%

Enzyme and Permeability Changes During Morphogenesis of Nocardia corallina

Brown

1967

Journal of General Microbiology

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SUMMARYInitial growth of Nocardia corallina occurred by germination and coenocytic hyphal development which resulted in a large surface-to-volume increase. During this period, endogenous respiration and the ability to oxidize fructose increased rapidly, but the stimulation of oxygen uptake by glucose decreased to zero. This inability to utilize glucose was due to loss of permeability rather than lack of a specific enzyme required for glucose metabolism. This was established by the following data: (1) cell-free extracts of hyphae contained the enzymes for conversion of glucose into fructose-6-phosphate ; (2) intact hyphae oxidized fructose; (3) incubation of hyphae with cetyltrimethylammonium bromide increased cell permeability to glucose and oxygen uptake was stimulated. Comparative determinations of enzymes involved in the early steps of glucose metabolism showed quantitative changes associated with the period of impermeability to glucose. The loss of permeability to glucose may represent an initial metabolic change fundamental to morphogenesis in this microbe.

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Section: Discussionmentioning

confidence: 99%

Enzyme and Permeability Changes During Morphogenesis of Nocardia corallina

Brown

1967

Journal of General Microbiology

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“…This accumulation probably results from the mode of control of DAP and lysine metabolism in these organisms. L-Lysine represses the formation of DAP decarboxylase in E. coli and in some but not all strains of S. aureus (White et al 1964, and it seems likely that it has the same effect in the pseudomonad (P. J. White, unpublished).…”

Section: Discussionmentioning

confidence: 99%

“…White. DAP decarboxylase was measured by the evolution of carbon dioxide from meso-DAP in the Warburg apparatus at 37" in an atmosphere of nitrogen (White, Kelly, Suffling & Work, 1964). DAP epimerase activity was measured manometrically by following the evolution of carbon dioxide from LL-DAP in the presence of excess CAP decarboxylase.…”

Section: Methodsmentioning

confidence: 99%

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Diaminopimelic Acid and Lysine Auxotrophs of Pseudomonas aeruginosa 8602

Clarkson¹,

Meadow

1971

Journal of General Microbiology

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“…Pyridoxal phosphate is required as cofactor (White & Kelly, 1965). Enzyme activity in most bacteria is lower when lysine is added to chemically defined media (Denman, Hoare & Work, 1955 ;Patte, Loviny & Cohen, 1962 ;White et al, 1964 ;Gilboe, Friede & Henderson, 1968 ;Grandgenett & Stahly, 1971). Adding diaminopimelate to minimal media does not significantly alter enzymic activity (Whi te et al, I 964).…”

Section: Introductionmentioning

confidence: 99%

The Regulation of Diaminopimelate Decarboxylase Activity in Escherichia coli strain W

White

1976

Journal of General Microbiology

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Activity of diaminopimelate decarboxylase in Escherichia coli strain w, growing in an aerated fermenter, was only slightly (14 yo) repressed by 2 mwlysine when approximately equimolar diaminopimelate was present in the medium. Lysine alone caused 78 % repression. Diaminopimelate did not interfere with uptake of lysine by growing organisms. Organisms grown in medium containing diaminopimelate, without lysine, had a decarboxylase activity 24% higher than organisms from minimal medium. The extent of repression by pyridoxine (56% when added to minimal medium) was decreased (to 3 I yo) when diaminopimelate was also present in the medium. A diaminopimelate-requiring mutant, with limited ability to take up diaminopimelate, formed almost three times less diaminopimelate decarboxylase than did a diaminopimelate-requiring second-stage mutant that had an increased rate of transport of this amino acid. The internal concentration of diaminopimelate thus probably regulates the activity of the decarboxylase by induction. Lysine might not directly repress the enzyme but might give an apparent repression by restricting the biosynthesis of diaminopimelate. This restriction is probably not caused only by inhibition or repression of aspartokinase. Lysine and threonine together, though not singly, almost completely inhibited aspartokinase in vitro but caused less apparent repression of diaminopimelate decarboxylase than did lysine alone. Lysine plus diaminopimelate strongly repressed the lysine-sensitive aspartokinase (85 %) without much affecting diaminopimelate decarboxylase formation, and pyridoxine repressed the decarboxylase without affecting aspartokinase.

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Variation of activity of bacterial diaminopimelate decarboxylase under different conditions of growth

Cited by 28 publications

References 33 publications

Enzyme and Permeability Changes During Morphogenesis of Nocardia corallina

Enzyme and Permeability Changes During Morphogenesis of Nocardia corallina

Diaminopimelic Acid and Lysine Auxotrophs of Pseudomonas aeruginosa 8602

The Regulation of Diaminopimelate Decarboxylase Activity in Escherichia coli strain W

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