The metabolism of <scp>d</scp>-glucarate by <i>Pseudomonas acidovorans</i>

Jeffcoat, Roger; Hassall, H.; Dagley, S.

doi:10.1042/bj1150969

Cited by 26 publications

(19 citation statements)

References 21 publications

(24 reference statements)

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“…In Escherichia c6li, the KDG product of the glucarate dehydrase reaction is an approximately 85:15 mixture of 5-keto-4-deoxy-and 2-keto-3-deoxy-D-glucarate (2, 3), indicating that the preferred site for the dehydration is on the hydroxyl groups attached to carbon atoms 4 and 5 of GlcA. Similar results were obtained with Pseudomonas acidovorans (14). However, in Agrobacterium tumefaciens the preferred site (about 80%) for dehydration was at the hydroxyl groups attached to carbon atoms 2 and 3 (8).…”

Section: Eo8-supporting

confidence: 69%

Catabolism of d -Glucaric Acid to α-Ketoglutarate in Bacillus megaterium

Sharma

Blumenthal

1973

J Bacteriol

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Crude cell-free extracts of D-glucarate-grown cells of Bacillus megaterium converted D-glucarate to a-keto-fl-deoxy-D-glucarate (KDG). Charcoal-treated cell-free extracts or partially purified enzyme preparations converted KDG to an intermediate which was isolated and identified as 2,5-diketoadipate (DKA). This compound was synthesized, and the cell-free extracts of D-glucarate grown cells were found to catalyze the reduction of nicotinamide adenine dirrucleotide (NAD) in its presence. In the absence of NAD, the same enzyme preparation catalyzed the decarboxylation of the DKA to a-ketoglutarate semialdehyde (KGS), whereas in the presence of NAD the KGS was subsequently oxidized to a-ketoglutarate by a-ketoglutarate semialdehyde dehydrogenase. Since galactarate-grown B. megaterium contains a galactarate dehydrase forming KDG, the complete pathway for the metabolism of D-glucarate or galactarate to a-ketoglutarate and CO2 is now known in a gram-positive bacterium.

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Section: Eo8-supporting

confidence: 69%

Catabolism of d -Glucaric Acid to α-Ketoglutarate in Bacillus megaterium

Sharma

Blumenthal

1973

J Bacteriol

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“…It is of interest to note that, while in the case of Pseudomonas sp. (Dagley & Trudgill, 1965;Jeffcoat et al, 1969a;K. C. Backman, personal communication) (Blumenthal & Fish, 1963;Jeffcoat et al, 1969a,b).…”

Section: P¯anking Motif Is Taken By Janec ïEk As Possible Evidencmentioning

confidence: 90%

Structure and mechanism of a sub-family of enzymes related to N -acetylneuraminate lyase 1 1Edited by F. E. Cohen

Lawrence¹,

Barbosa²,

Smith³

et al. 1997

Journal of Molecular Biology

100

107

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“…The genes of E. coli responsible for the different enzymatic activities of the pathway have been identified (6,7). An alternative pathway has been proposed in a limited number of bacteria (8 -10), including Pseudomonas species, in which the enzymes of the pathway have been characterized (9,11,12) (Fig. 1).…”

mentioning

confidence: 99%

New Insights into the Alternative d-Glucarate Degradation Pathway

Aghaie¹,

Lechaplais

Sirven

et al. 2008

Journal of Biological Chemistry

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Although the D-glucarate degradation pathway is well characterized in Escherichia coli, genetic and biochemical information concerning the alternative pathway proposed in Pseudomonas species and Bacillus subtilis remains incomplete. Acinetobacter baylyi ADP1 is a Gram-negative soil bacterium possessing the alternative pathway and able to grow using D-glucarate as the only carbon source. Based on the annotation of its sequenced genome (1), we have constructed a complete collection of singlegene deletion mutants (2). High throughput profiling for growth on a minimal medium containing D-glucarate as the only carbon source for ϳ2450 mutants led to the identification of the genes involved in D-glucarate degradation. Protein purification after recombinant production in E. coli allowed us to reconstitute the enzymatic pathway in vitro. We describe here the kinetic characterization of D-glucarate dehydratase, D-5-keto-4-deoxyglucarate dehydratase, and of cooperative ␣-ketoglutarate semialdehyde dehydrogenase. Transcription and expression analyses of the genes involved in D-glucarate metabolism within a single organism made it possible to access information regarding the regulation of this pathway for the first time.

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The metabolism of d-glucarate by Pseudomonas acidovorans

Cited by 26 publications

References 21 publications

Catabolism of d -Glucaric Acid to α-Ketoglutarate in Bacillus megaterium

Catabolism of d -Glucaric Acid to α-Ketoglutarate in Bacillus megaterium

Structure and mechanism of a sub-family of enzymes related to N -acetylneuraminate lyase 1 1Edited by F. E. Cohen

New Insights into the Alternative d-Glucarate Degradation Pathway

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