THE METABOLISM OF TARTARIC ACID BY A <i>PSEUDOMONAS</i>. A NEW PATHWAY

Dagley, S.; Trudgill, Peter

doi:10.1042/bj0890022

Cited by 35 publications

(24 citation statements)

References 24 publications

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“…Indeed, one strain ofP. putida forms a tartrate dehydrase when grown with the L-isomer (81), but catabolizes meso-tartrate via glycerate (40,92); the enzymes involved are inducible, but their inducers have not been identified. In light of present biochemical knowledge, it should be possible (i) to determine the precise metabolic routes used for dissimilation of tartrate by individual strains of Pseudomonas, (ii) to identify the inductive mechanisms that govern the selection of specific pathways of tartrate catabolism, and (iii) to establish the…”

Section: Isolated Pathwaysmentioning

confidence: 99%

Regulation of catabolic pathways in Pseudomonas.

Ornston¹

1971

Bacteriological Reviews

110

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Section: Isolated Pathwaysmentioning

confidence: 99%

Regulation of catabolic pathways in Pseudomonas.

Ornston¹

1971

Bacteriological Reviews

110

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“…On the other hand, D-(+)-malate is usually referred to as the unnatural form of malic acid which does not occur in biological material. However, a variety of bacterial species, including members of the pseudomonads (9,25,27), enterobacteria (16,45,48), and Rhodospirillaceae (7,39,44,47), are known to grow on either L-(+)-tartrate or D-(+)malate as the carbon source. Different enzyme systems have been described which are involved in the catabolism of both compounds.…”

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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“…Phototrophic utilization of L-tartrate was reported for Rhodopseudomonas sphaeroides (van Niel 1944). Aerobically, L-tartrate is decomposed by coliform bacteria (Vaughn et al 1946) and Pseudomonas species (Shilo 1957;Dagley and Trudgill 1963). Some Salmonella species and some Pseudomonas strains degrade meso-or D-(-)-tartrate (Shilo and Stanier 1957;Rode and Giffhorn 1982).…”

mentioning

confidence: 99%

“…Some Salmonella species and some Pseudomonas strains degrade meso-or D-(-)-tartrate (Shilo and Stanier 1957;Rode and Giffhorn 1982). Degradation usually proceeds via dehydratation to oxaloacetate (Barker 1936;Nomura and Sakaguchi 1955;Hurlbert and Jakoby 1965); alternative pathways are decarboxylation to glycerate as with a Pseudomonas strain (Dagley and Trudgill 1963) or oxidation to oxaloglycolate as found in mitochondria (Kun 1956). The present investigation was initiated in order to compare the potential of anaerobic microbial degradation of the different tartrate isomers in natural and man-made anoxic ecosystems.…”

mentioning

confidence: 99%

Fermentation of tartrate enantiomers by anaerobic bacteria, and description of two new species of strict anaerobes, Ruminococcus pasteurii and Ilyobacter tartaricus

Schink

1984

Arch. Microbiol.

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Abstract. Enumerations of tartrate-fermenting anaerobic bacteria with L-, D-, and m-tartrate as substrates revealed that L-tartrate fermenters outnumbered D-and m-tartrate fermenters by one to three orders of magnitude in all three anoxic environments studied.Highest numbers of tartrate-fermenting bacteria were found in freshwater creek sediments, less in polluted marine channels, and lowest numbers in anoxic sewage digestor sludge. Prevailing bacteria were isolated on every tartrate enantiomer. They all degraded tartrates via oxaloacetate. D-and m-tartrate-fermenting anaerobes were able to ferment L-tartrate as well, and were assigned to the genera Bacteroides, Acetivibrio, and Ilyobacter. L-Tartrate-fermenting anaerobes only utilized this enantiomer, and were characterized in more detail. Fermentation products on tartrate, citrate, pyruvate, and oxaloacetate were acetate, formate, and carbon dioxide. On fructose and glucose, also ethanol was formed. Freshwater isolates were Gram-positive cocci with large slime capsules, and were described as a new species, Ruminococcus pasteurii. Saltwater isolates were Gram-negative short rods, and were also described as a new species, Ilyobacter tartaricus. The guanosine-plus-cytosine content of the DNA was 45.2% and 33.1%, respectively.

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THE METABOLISM OF TARTARIC ACID BY A PSEUDOMONAS. A NEW PATHWAY

Abstract: Many micro-organisms can utilize tartaric acid for growth. The only well-established reaction sequence for its dissimilation is that first proposed by Barker (1936) for the breakdown of (+ )-tartaric acid by Aerobacter aerogenre in which oxaloacetic

Cited by 35 publications

References 24 publications

Regulation of catabolic pathways in Pseudomonas.

Regulation of catabolic pathways in Pseudomonas.

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

Fermentation of tartrate enantiomers by anaerobic bacteria, and description of two new species of strict anaerobes, Ruminococcus pasteurii and Ilyobacter tartaricus

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