Purification and properties of <scp>d</scp>-4-deoxy-5-oxoglucarate hydro-lyase (decarboxylating)

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

doi:10.1042/bj1150977

Cited by 32 publications

(28 citation statements)

References 15 publications

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“…For instance, only a small amount of data for KDG dehydratase are available. Procedures for the purification and the activity assay of the enzyme have been published (11,13,14), but, to our best knowledge, there is no report on gene identification or enzymatic properties. Moreover, although gene identification was recently achieved for ␣-KGSA dehydrogenase, investigations were restricted to Azospirillum brasilense and Bacillus subtilis (15).…”

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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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confidence: 99%

“…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).…”

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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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“…The HPC used in these assays (46), and more recently P. putida ⌬ 1 -pyrroline-4-hydroxy-2-carboxylate deaminase (LhpC), have been characterized (12). The HypD of S. meliloti characterized in this study has 31%, 26%, 26%, 27%, and 74% identities to the above-named enzymes, respectively (see Fig.…”

Section: Resultsmentioning

confidence: 99%

l-Hydroxyproline andd-Proline Catabolism in Sinorhizobium meliloti

et al. 2016

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Sinorhizobium meliloti IMPORTANCEHydroxyproline is abundant in proteins in animal and plant tissues and serves as a carbon and a nitrogen source for bacteria in diverse environments, including the rhizosphere, compost, and the mammalian gut. While the main biochemical features of bacterial hydroxyproline catabolism were elucidated in the 1960s, the genetic and molecular details have only recently been determined. Elucidating the genetics of hydroxyproline catabolism will aid in the annotation of these genes in other genomes and metagenomic libraries. This will facilitate an improved understanding of the importance of this pathway and may assist in determining the prevalence of hydroxyproline in a particular environment.4-Hydroxyproline and 3-hydroxyproline in animal and plant proteins are formed through the posttranslational modification of proline residues by the enzyme proline hydroxylase. In some bacteria, hydroxyproline is synthesized from free L-proline, where it is employed in the synthesis of secondary metabolites (1, 2). 4-Hydroxyproline has two chiral carbon atoms, and of its four isomeric forms, trans-4-hydroxy-L-proline (trans-4-L-Hyp) and cis-4-hydroxy-D-proline (cis-4-D-Hyp) appear to be the two most common isomers. trans-4-

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“…Galactarolactone cycloisomerase (EC 5.5.1.-) then catalyses ring opening and the formation of 3-deoxy-2-keto-l-threo-hexarate (Andberg et al, 2012). The 3-deoxy-2-keto-l-threo-hexarate is converted by a decarboxylating hydrolyase (EC 4.2.1.41) into -ketoglutaric semialdehyde (Jeffcoat et al, 1969;Aghaie et al, 2008). In the final step -ketoglutaric semialdehyde is oxidized by a dehydrogenase to -ketoglutarate, which is a metabolite of the TCA cycle (Watanabe et al, 2007).…”

Section: Introductionmentioning

confidence: 99%

Purification, crystallization and preliminary X-ray diffraction analysis of a novel keto-deoxy-D-galactarate (KDG) dehydratase fromAgrobacterium tumefaciens

et al. 2013

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d-Galacturonic acid is the main component of pectin. It could be used to produce affordable renewable fuels, chemicals and materials through biotechnical conversion. Keto-deoxy-d-galactarate (KDG) dehydratase is an enzyme in the oxidative pathway of d-galacturonic acid in Agrobacterium tumefaciens (At). It converts 3-deoxy-2-keto-l-threo-hexarate to -ketoglutaric semialdehyde. At KDG dehydratase was crystallized by the hanging-drop vapour-diffusion method. The crystals belonged to the monoclinic space group C2, with unit-cell parameters a = 169.1, b = 117.8, c = 74.3 Å , = 112.4and an asymmetric unit of four monomers. X-ray diffraction data were collected to 1.9 Å resolution using synchrotron radiation. The three-dimensional structure of At KDG dehydratase will provide valuable information on the function of the enzyme and will allow it to be engineered for biorefinery-based applications.

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Purification and properties of d-4-deoxy-5-oxoglucarate hydro-lyase (decarboxylating)

Cited by 32 publications

References 15 publications

New Insights into the Alternative d-Glucarate Degradation Pathway

New Insights into the Alternative d-Glucarate Degradation Pathway

l-Hydroxyproline andd-Proline Catabolism in Sinorhizobium meliloti

Purification, crystallization and preliminary X-ray diffraction analysis of a novel keto-deoxy-D-galactarate (KDG) dehydratase fromAgrobacterium tumefaciens

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