Regulation of Nicotinamide Adenine Dinucleotide Phosphate-specific Glutamate Dehydrogenase from Brevibacterium flavum, a Glutamate-producing Bacterium*

Shiio, Isamu; Ozaki, Hachiro

doi:10.1093/oxfordjournals.jbchem.a129397

Cited by 56 publications

(28 citation statements)

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“…That Mtb nonetheless contained glutamate in what is estimated to be a high millimolar to molar range suggests that Mtb might accumulate glutamate during growth in culture as a reserve for use under more stringent conditions in the host. Accumulation of glutamate would likely exert feedback inhibition on glutamate dehydrogenase (48), and may account for our inability to detect glutamate dehydrogenase activity in Mtb and M. bovis bacillus Calmette-Guérin lysates.…”

Section: Discussionmentioning

confidence: 97%

Variant tricarboxylic acid cycle in Mycobacterium tuberculosis : Identification of α-ketoglutarate decarboxylase

Tian

Bryk

Itoh

et al. 2005

Proc. Natl. Acad. Sci. U.S.A.

179

171

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Mycobacterium tuberculosis (Mtb) has adapted its metabolism for persistence in the human macrophage. The adaptations are likely to involve Mtb's core intermediary metabolism, whose enzymes have been little studied. The tricarboxylic acid cycle is expected to yield precursors for energy, lipids, amino acids, and heme. The genome sequence of Mtb H37Rv predicts the presence of a complete tricarboxylic acid cycle, but we recently found that ␣-ketoglutarate dehydrogenase (KDH) activity is lacking in Mtb lysates. Here we showed that citrate synthase, aconitase, isocitrate dehydrogenase, fumarase, malate dehydrogenase, and succinate dehydrogenase, but not KDH, are present, raising the possibility of separate oxidative and reductive half-cycles. As a potential link between the half-cycles, we found that Rv1248c, annotated as encoding SucA, the putative E1 component of KDH, instead encodes ␣-ketoglutarate decarboxylase (Kgd) and produces succinic semialdehyde. Succinic semialdehyde dehydrogenase activity was detected in Mtb lysates and recapitulated with recombinant

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Section: Discussionmentioning

confidence: 97%

Variant tricarboxylic acid cycle in Mycobacterium tuberculosis : Identification of α-ketoglutarate decarboxylase

Tian

Bryk

Itoh

et al. 2005

Proc. Natl. Acad. Sci. U.S.A.

179

171

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“…Glutamate dehydrogenase (GDH) was assayed by the method of Shiio and Ozaki. 7) The activity was expressed as f.,lmol NADP formed/min/mg protein.…”

Section: Methodsmentioning

confidence: 99%

Relationship between the Glutamate Production and the Activity of 2-Oxoglutarate Dehydrogenase inBrevibacterium lactofermentum

Kawahara

Takahashi-Fuke

Shimizu

et al. 1997

Bioscience, Biotechnology, and Biochemistry

101

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“…Due to its pivotal role in glutamate production, basic biochemical work on the glutamate-producing enzymes of C. glutamicum was already started in the 1960s (Kimura, 1962;Oshima et al, 1964;Shiio and Ozaki, 1970;Tochikura et al, 1984). As most bacteria, C. glutamicum has two primary pathways to facilitate the incorporation of ammonium into the key nitrogen donors for biosynthetic reactions, l-glutamate and lglutamine (Shiio and Ozaki, 1970;Jakoby et al, 1997;Tesch et al, 1998).…”

Section: Introductionmentioning

confidence: 99%

“…As most bacteria, C. glutamicum has two primary pathways to facilitate the incorporation of ammonium into the key nitrogen donors for biosynthetic reactions, l-glutamate and lglutamine (Shiio and Ozaki, 1970;Jakoby et al, 1997;Tesch et al, 1998). Glutamate dehydrogenase (GDH) assimilates ammonium by the reductive amination of 2-oxoglutarate to l-glutamate.…”

Section: Introductionmentioning

confidence: 99%

Mutation-induced metabolite pool alterations in Corynebacterium glutamicum: Towards the identification of nitrogen control signals

Müller¹,

Strösser²,

Buchinger³

et al. 2006

Journal of Biotechnology

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The influence of glutamate dehydrogenase activity on nitrogen regulation in Corynebacterium glutamicum was investigated. As shown by RNA hybridization experiments deletion of the gdh gene results in a rearrangement of nitrogen metabolism. Even when sufficiently supplied with nitrogen sources, a gdh deletion strain showed the typical nitrogen starvation response of C. glutamicum. These changes in transcription correlate with distinct alterations of intracellular metabolite pattern. Metabolite analyses of different mutant strains and the wild type indicated that ammonium and 2-oxoglutarate might influence the nitrogen regulation system of C. glutamicum cells.

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Regulation of Nicotinamide Adenine Dinucleotide Phosphate-specific Glutamate Dehydrogenase from Brevibacterium flavum, a Glutamate-producing Bacterium*

Cited by 56 publications

References 0 publications

Variant tricarboxylic acid cycle in Mycobacterium tuberculosis : Identification of α-ketoglutarate decarboxylase

Variant tricarboxylic acid cycle in Mycobacterium tuberculosis : Identification of α-ketoglutarate decarboxylase

Relationship between the Glutamate Production and the Activity of 2-Oxoglutarate Dehydrogenase inBrevibacterium lactofermentum

Mutation-induced metabolite pool alterations in Corynebacterium glutamicum: Towards the identification of nitrogen control signals

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