Tryptophan catabolism in Bacillus megaterium

Bouknight, Reynard R.; Sadoff, H. L.

doi:10.1128/jb.121.1.70-76.1975

Cited by 24 publications

(11 citation statements)

References 18 publications

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“…However, they were unable to experimentally induce tryptophan oxygenase with exogenously supplied tryptophan. This contrasts with the results obtained for other organisms (2,16).…”

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confidence: 99%

“…However, they were unable to experimentally induce tryptophan oxygenase with exogenously supplied tryptophan. This contrasts with the results obtained for other organisms (2,16).We report in this paper a more detailed analysis of tryptophan oxygenase induction and its relationship to actinomycin D production. Evidence is also presented which suggests that induction of this enzyme may actually be due to a release from glutamate-induced catabolite repression.…”

contrasting

confidence: 81%

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Control of Actinomycin D Biosynthesis inStreptomyces parvullus: Regulation of Tryptophan Oxygenase Activity

Foster

Katz

1981

J Bacteriol

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Tryptophan oxygenase (tryptophan 2,3-dioxygenase) activity increases immediately before the initiation of actinomycin D production by Streptomyces parvullus. We have attempted to discern whether this increase is due to a release from catabolite repression or to the synthesis of an inducer substance. The standard culture medium (glutamic acid-histidine-fructose medium) used in antibiotic production studies with S. parvullus contains L-glutamate as a major constituent. L-Glutamate is almost totally consumed before the onset of actinomycin D synthesis. The addition of 10 mM L-glutamate at this stage completely abolished actinomycin D production as well as tryptophan oxygenase synthesis. Fourteen amino acids were tested for a similar effect. Of these, L-glutamate and L-aspartate had the most dramatic effect on tryptophan oxygenase and ,8-galactosidase (fl-D-galactosidase), another inducible enzyme. Standard glutamic acidhistidine-fructose medium, preincubated for 23 h to remove L-glutamate, allowed the synthesis of actinomycin D and tryptophan oxygenase by cells at a stage of growth normally considered too early for antibiotic production. A chemically defined medium lacking L-glutamate and adjusted to pH 8.0 was designed to simulate the preincubation medium. The transfer of cells to this artificial preincubation medium resulted in the appearance of tryptophan oxygenase as early as 19 h before normal synthesis occurred, eliminating the possibility that an inducer molecule is synthesized and excreted during the preincubation period. The results of these studies suggest that the increase in tryptophan oxygenase activity before the onset of actinomycin D synthesis, as well as the synthesis of actinomycin D itself, is due to a release from L-glutamate catabolite repression.The antibiotic actinomycin D is a secondary metabolite produced by several Streptomyces species. Most of these species produce more than one form of actinomycin (5). Streptomyces parvullus is unusual in that it only synthesizes one class of actinomycin, class IV (12). Consequently, research into the biochemistry of antibiotic production in this organism is uncomplicated by the presence of multiple enzyme systems responsible for the production of more than one form of actinomycin.Tryptophan has been implicated as a precursor of the actinocin ring structure of actinomycin D (6, 7). In addition, Lingens and Vollprecht (9) have presented evidence that, in at least one streptomycete, NAD is also synthesized from tryptophan. Figure 1, therefore, presents the pathways of tryptophan metabolism as they are believed to occur in Streptomyces spp. (19).Tryptophan oxygenase (tryptophan 2,3-dioxygenase; L-tryptophan:oxygen 2,3-oxidoreductase; EC 1.13.11.11) is the first enzyme involved t Present address: in both the primary metabolic pathway to NAD and the secondary metabolic pathway in actinomycin D. Its activity was first demonstrated in S. parvullus by M. J. M. Hitchcock and E. Katz (unpublished data), who demonstrated its apparent induction during the onset of ac...

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“…However, they were unable to experimentally induce tryptophan oxygenase with exogenously supplied tryptophan. This contrasts with the results obtained for other organisms (2,16).…”

contrasting

confidence: 99%

contrasting

confidence: 81%

Control of Actinomycin D Biosynthesis inStreptomyces parvullus: Regulation of Tryptophan Oxygenase Activity

Foster

Katz

1981

J Bacteriol

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“…Trp has also been implicated as the sole source of carbon and nitrogen in some species of Pseudomonadaceae and Bacillaceae [36][37][38][39][40]. The resumption of growth after an intervening stationary phase when Trp was present in Fig.…”

Section: Discussionmentioning

confidence: 99%

Growth and indole-3-acetic acid biosynthesis ofAzospirillum brasilenseSp245 is environmentally controlled

Ona

Impe

Prinsen

et al. 2005

FEMS Microbiology Letters

104

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Batch and fed batch cultures of Azospirillum brasilense Sp245 were conducted in a bioreactor. Growth response, IAA biosynthesis and the expression of the ipdC gene were monitored in relation to the environmental conditions (temperature, availability of a carbon source and aeration). A. brasilense can grow and produce IAA in batch cultures between 20 and 38 degrees C in a standard minimal medium (MMAB) containing 2.5 gl(-1)l-malate and 50 microgml(-1) tryptophan. IAA synthesis requires depletion of the carbon source from the growth medium in batch culture, causing growth arrest. No significant amount of IAA can be detected in a fed batch culture. Varying the concentration of tryptophan in batch experiments has an effect on both growth and IAA synthesis. Finally we confirmed that aerobic growth inhibits IAA synthesis. The obtained profile for IAA synthesis coincides with the expression of the indole-3-pyruvate decarboxylase gene (ipdC), encoding a key enzyme in the IAA biosynthesis of A. brasilense.

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“…Unfortunately, little is known concerning the ability of Bacillus species to catabolize aromatic molecules. Certain Bacillus strains appear to degrade benzenoid compounds via reaction sequences similar to those described in other bacterial genera (1,2,9,17,(22)(23)(24)(25). However, recent investigations indicate that many bacilli may catabolize aromatic molecules via reaction sequences involving novel chemistry (4, 6, 10-12, 20, 21).…”

mentioning

confidence: 91%

Degradation of 3-Hydroxybenzoate by Bacteria of the Genus Bacillus

Crawford¹

1975

Applied Microbiology

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Tryptophan catabolism in Bacillus megaterium

Cited by 24 publications

References 18 publications

Control of Actinomycin D Biosynthesis inStreptomyces parvullus: Regulation of Tryptophan Oxygenase Activity

Control of Actinomycin D Biosynthesis inStreptomyces parvullus: Regulation of Tryptophan Oxygenase Activity

Growth and indole-3-acetic acid biosynthesis ofAzospirillum brasilenseSp245 is environmentally controlled

Degradation of 3-Hydroxybenzoate by Bacteria of the Genus Bacillus

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