Mitochondrial and Cytoplasmic Enzymes for the Reduction of Fumarate to Succinate in Yeast

Rossi, C.S.; Hauber, J.; Singer, Thomas P.

doi:10.1038/204167a0

Cited by 45 publications

(19 citation statements)

References 14 publications

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“…Many different microorganisms like fungi (different Aspergillus stc., Byssochlamys nivea, Lentinus degener, Paecilomyces varioti, Penicillium viniferum [10,11]), yeast (Saccharomyces cerevisiae), and Gram-positive bacteria (Corynebacterium glutamicum, Enterococcus faecalis) have been screened and studied for succinic acid production. Most intensively studied are Anaerobiospirillum succiniciproducens [12] and Actinobacillus succinogenes [13] due to their ability to produce a comparatively large amount of succinic acid.…”

Section: Biotechnologymentioning

confidence: 99%

Succinic Acid: A New Platform Chemical for Biobased Polymers from Renewable Resources

et al. 2008

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Succinic acid is predicted to be one of the future platform chemicals that can be derived from renewable resources. The improvements in biotechnological succinic acid production are presented. Chemical conversion pathways to c-butyrolactone, tetrahydrofuran, 1,4-butanediole, and pyrrolidones are reviewed. An overview of possible new biopolymers (e. g. polyesters, polyamides, and poly(ester amide)s) based on succinic acid and its derivatives is given. Nevertheless, industrial processes using purified succinic acid from fermentation broths are not state of the art yet. Further improvements are needed until succinic acid-based chemical production will be economically favorable.

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Section: Biotechnologymentioning

confidence: 99%

Succinic Acid: A New Platform Chemical for Biobased Polymers from Renewable Resources

et al. 2008

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“…The fumarate reductase enzyme of yeasts irreversibly catalyzes the reduction of fumarate to succinate [1]. The enzyme is a soluble protein, bound non-covalently to £avin adenine dinucleotide (FAD).…”

Section: Introductionmentioning

confidence: 99%

Soluble fumarate reductase isoenzymes from Saccharomyces cerevisiae are required for anaerobic growth

Arikawa

1998

FEMS Microbiology Letters

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In Saccharomyces cerevisiae, the cytosolic and promitochondrial isoenzymes of fumarate reductase are encoded by the FRDS and OSM1 genes, respectively. The product of the OSM1 gene is reported to be required for growth in hypertonic medium. Simultaneous disruption of the FRDS and OSM1 genes resulted in the inability of the yeasts to grow anaerobically on glucose as a carbon source, and disruption of the OSM1 gene caused poor growth under anaerobic conditions. However, the disruption of both the FRDS and/or OSM1 genes had no effect on aerobic growth or growth under hypertonic conditions. These results suggest that the fumarate reductase isoenzymes in Saccharomyces cerevisiae are essential for anaerobic growth but not for growth under hypertonic conditions. z

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“…of yeast A search for fumarate reductase in the cytoplasm of aerobic and anaerobic yeast cells and in mutants revealed the existence of a whole group of flavoproteins for the reduction of fumarate to succinate which are clearly distinct from mitochondria1 succinate dehydrogenase in molecular composition, properties, and genetic control. Parts of this study have been briefly reported [13,14] ; the present paper and the next one in this series [15] give a detailed account of these studies. For the previous paper in this series see reference 111.…”

Section: Several Years Later [4] Succinate Dehydrogenasementioning

confidence: 99%

Studies on Succinate Dehydrogenase

Hauber

Singer

1967

European Journal of Biochemistry

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The cytoplasm of yeast contains several enzymes for the reduction of fumarate to succinate. One of these is excluded on Sephadex G-200 and in this respect as in all of its known properties, resembles mitochondrial succinate dehydrogenase in the soluble form. Another type is distinguished by the apparent inability to oxidize succinate with any of the conventional electron acceptors.This enzyme has been subdivided into two types (I and 11) which may be readily separated by chromatography on hydroxylapatite. Type I and I1 fumarate reductases differ from mitochondrial succinate dehydrogenase in containing acid-extractable (rather than covalently bound) FAD, in their intracellular location, in being more stable and more resistant to inhibition by mercurials. The fumarate reductases also differ from the dehydrogenase in molecular weight, in lack of activation by substrate, and in having lower affinities for succinate and malonate and a higher one for fumarate. Conditions which are optimal for the development of mitochondrial succinate dehydrogenase (high 0, tension, low glucose concentration) repress the development of type I and I1 fumarate reductases and vice versa. "Petite" mutants, which lack succinate dehydrogenase, have a normal content of these fumarate reductases. Type I and I1 fumarate reductases, while similar in most respects, differ in molecular weight, kinetic constants and reactivity with electron donors.Thirty years ago Fischer and Eysenbach [2] found that partially purified preparations of the "old yellow enzyme" from yeast contained an enzyme which catalyzed the reduction of fumarate by certain reduced dyes of low potential but did not oxidize succinate with methylene blue as electron acceptor. Since methylene blue was thought a t the time to provide a direct assay for succinate dehydrogenase activity, the action of the new enzyme was taken to be unidirectional and the enzyme was named fumaric hydrogenasel. Although isolation of the enzyme was not undertaken, it was later reported [3] that dialysis inactivated the enzyme and that added FAD restored the activity.

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Mitochondrial and Cytoplasmic Enzymes for the Reduction of Fumarate to Succinate in Yeast

Cited by 45 publications

References 14 publications

Succinic Acid: A New Platform Chemical for Biobased Polymers from Renewable Resources

Succinic Acid: A New Platform Chemical for Biobased Polymers from Renewable Resources

Soluble fumarate reductase isoenzymes from Saccharomyces cerevisiae are required for anaerobic growth

Studies on Succinate Dehydrogenase

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