Adaptation of
            <i>Rhodopseudomonas sphaeroides</i>
            to Growth on
            <scp>d</scp>
            -(—)-Tartrate and Large-Scale Production of a Constitutive
            <scp>d</scp>
            -(—)-Tartrate Dehydratase During Growth on
            <scp>dl</scp>
            -Malate

Rode, Hergo; Giffhorn, Friedrich

doi:10.1128/aem.45.2.716-719.1983

Cited by 24 publications

(9 citation statements)

References 15 publications

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“…The purple non-sulfur bacterium Rhodobacter sphaeroides strain Si4 (DSM 8371) is an isolate from this laboratory (Rode & Giffhorn, 1983). R. sphaeroides strain M22 is a transposon mutant of strain Si4 with Tn 5 inserted in the MDH gene (mtlK) (Schneider et al, 1993).…”

Section: Methodsmentioning

confidence: 99%

“…and pH regulation. The medium contained the following components in a final volume of 1 1: D -glucitol, 9 g; KH 2 PO 4 ,1 ·0 g; NH 4 C1,1 g; MgSO 4 .7H a O, 0·4 g; NaCl, 0·4 g; CaCl 2 .2H 2 O, 0·05 g; 10 × trace element solution SL4 (Pfennig & Lippert, 1966), 1·0 ml; 10 × vitamin solution (Rode & Giffhorn, 1983), 1 ml. The pH was adjusted to 6·8 with NaOH.…”

Section: Methodsmentioning

confidence: 99%

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Polyol metabolism of Rhodobacter sphaeroides: biochemical characterization of a short-chain sorbitol dehydrogenase

1995

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A sorbitol dehydrogenase (SDH; L-iditol: NAD+ 2-oxidoreductase; EC 1.1.1.14) was isolated from the phototrophic bacterium Rhodobacter sphaeroides strain M22, a transposon mutant of R. sphaeroides Si4 with the transposon inserted in the mannitol dehydrogenase (MDH) gene. SDH was purified 470-fold to apparent homogeneity by ammonium sulfate precipitation, chromatography on Phenyl-Sepharose, Q-Sepharore and Matrex Gel Red-A, and by gel filtration on Superdex 200. The relative molecular mass (M,) of the native SDH was 61 000 as calculated from its Stokes' radius (r, = 3.5 nm) and sedimentation coefficient (S20,w = 4.235). SDS-PAGE resulted in one single band representing a polypeptide with a M, of 29 000, indicating that the native protein is a dimer. The isoelectric point of SDH was determined to be pH 4.8. The enzyme was specific for NAD+ and catalysed the oxidation of D-glucitol (sorbitol) to Dfructose, galactitol to D-tagatose and of L-iditol. The apparent K, values were NAD+, 096 mM; D-glucitol, 6 2 mM; galactitol, 1.5 mM; NADH, 013 mM; Dfructose, 160 mM; and D-tagatose, 13 mM. The pH-optimum of substrate oxidation was 11.0 and that of substrate reduction 69-7.2. It was demonstrated that SDH is expressed in the wild-type strain R. sphaeroides Si4 together with MDH during growth on D-glucitol. Forty-four amino acids of the SDH N terminus were sequenced. This sequence exhibited 45-55% identity to the N-terminal sequence of 10 enzymes belonging to the short-chain alcohol dehydrogenase family.

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Section: Methodsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

Polyol metabolism of Rhodobacter sphaeroides: biochemical characterization of a short-chain sorbitol dehydrogenase

1995

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“…The mineral base of the medium was described previously (12). It contained 20 mM L-(+)-tartrate or 20 mM D-(+)-malate as the carbon source, and instead of yeast extract, 3 ml of a vitamin solution (38,41) per liter was used.…”

Section: Methodsmentioning

confidence: 99%

“…Both types of enzymes have only been purified and characterized from Pseudomonas putida (20,29), and because of their instability, attempts to purify the corresponding enzymes from other microorganisms have been unsuccessful (9,24,30,42). Only recently, D-(-)-tartrate dehydratases, specific for the D-(-) stereoisomer, have been isolated from Rhodopseudomonas sphaeroides (39,41) and from two Pseudomonas strains (40). D-282 GIFFHORN AND KUHN (+)-Malate is degraded by a D-(+)-malic enzyme which is found to be present in various bacterial extracts (16,21,25,45).…”

mentioning

confidence: 99%

Purification and characterization of a bifunctional L-(+)-tartrate dehydrogenase-D-(+)-malate dehydrogenase (decarboxylating) from Rhodopseudomonas sphaeroides Y

Giffhorn¹,

Kuhn²

1983

J Bacteriol

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A bifunctional enzyme, L-(+)-tartrate dehydrogenase-D-(+)-malate dehydrogenase (decarboxylating) (EC 1.1.1.93 and EC 1.1.1..., respectively), was discovered in cells of Rhodopseudomonas sphaeroides Y, which accounts for the ability of this organism to grow on L-(+)-tartrate and D-(+)-malate. The enzyme was purified 110-fold to homogeneity with a yield of 51%. During the course of purification, including ion-exchange chromatography and preparative gel electrophoresis, both enzyme activities appeared to be in association. The ratio of their activities remained almost constant [1:10, L-(+)-tartrate dehydrogenase/D-(+)malate dehydrogenase (decarboxylating)] throughout all steps of purification. Analysis by polyacrylamide gel electrophoresis revealed the presence of a single protein band, the position of which was coincident with both L-(+)-tartrate dehydrogenase and D-(+)-malate dehydrogenase (decarboxylating) activities. The apparent molecular weight of the enzyme was determined to be 158,000 by gel filtration and 162,000 by ultracentrifugation. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis yielded a single polypeptide chain with an estimated molecular weight of 38,500, indicating that the enzyme consisted of four subunits of identical size. The isoelectric point of the enzyme was between pH 5.0 and 5.2. The enzyme catalyzed the NAD-linked oxidation of L-(+)-tartrate as well as the oxidative decarboxylation of D-(+)-malate. For both reactions, the optimal pH was in a range from 8.4 to 9.0. The activation energy of the reaction (AlP) was 71.8 kJ/mol for L-(+)-tartrate and 54.6 kJ/mol for D-(+)-malate. NAD was required as a cosubstrate, and optimal activity depended on the presence of both

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“…Utilization of D‐tartaric acid by several strains of Pseudomonas and Pectobacterium occurring in soil has been reported. For example, Rode and Giffhorn reported growth of Rhodopseudomonas sp. on D‐tartaric acid after an extensive lag phase due to growth of only part of the population on this substrate.…”

Section: Why Include Enantiomers?mentioning

confidence: 99%

Natural Occurrence of Enantiomers of Organic Compounds Versus Phytoremediations: Should Research on Phytoremediations Be Revisited? A Mini‐review

et al. 2013

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Decontamination of polluted soils using plants is based on the ability of plant species (including transgenic plants) to enhance bioavailability of pollutants in the rhizosphere and support growth of pollutant-degrading microorganisms via root exudation and plant species-specific composition of the exudates. In this work, we review current knowledge of enantiomers of low-molecular-weight (LMW) organic compounds with emphasis on their use in phytoremediation. Many research studies have been performed to search for plants suitable for decontamination of polluted soils. Nevertheless, the natural occurrence of L- versus D-enantiomers of dominant compounds of plant root exudates which play different roles in the complexation of heavy metals, chemoattraction, and support of pollutant-degrading microorganisms were not included in these studies. D-enantiomers of aliphatic organic acids and amino acids or L-enantiomers of carbohydrates occur in high concentrations in root exudates of some plant species, especially under stress, and are less stimulatory for plants to extract heavy metals or for rhizosphere microflora to degrade pollutants compared with L-enantiomers (organic acids and amino acids) or D-carbohydrates. Determining the ratio of L- versus D-enantiomers of organic compounds as a criterion of plant suitability for decontamination of polluted soils and development of other types of bioremediation technologies need to be subjects of future research.

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Adaptation of Rhodopseudomonas sphaeroides to Growth on d -(—)-Tartrate and Large-Scale Production of a Constitutive d -(—)-Tartrate Dehydratase During Growth on dl -Malate

Cited by 24 publications

References 15 publications

Polyol metabolism of Rhodobacter sphaeroides: biochemical characterization of a short-chain sorbitol dehydrogenase

Polyol metabolism of Rhodobacter sphaeroides: biochemical characterization of a short-chain sorbitol dehydrogenase

Purification and characterization of a bifunctional L-(+)-tartrate dehydrogenase-D-(+)-malate dehydrogenase (decarboxylating) from Rhodopseudomonas sphaeroides Y

Natural Occurrence of Enantiomers of Organic Compounds Versus Phytoremediations: Should Research on Phytoremediations Be Revisited? A Mini‐review

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