Pyruvate metabolism in Saccharomyces cerevisiae.

Pronk JT; Yde Steensma H; Van Dijken JP

doi:10.1002/(sici)1097-0061(199612)12:16<1607::aid-yea70>3.0.co;2-4

Pyruvate metabolism in Saccharomyces cerevisiae.

Pronk JT ¹,

Yde Steensma H ,

Van Dijken JP

Affiliations

1. Department of Microbiology an Enzymology, Kluyver Laboratory of Biotechnology, Delft University of Technology, The Netherlands.
Authors
Pronk JT¹
(1 author)

ORCIDs linked to this article

Pronk JT | 0000-0002-5617-4611

Yeast (Chichester, England), 01 Dec 1996, 12(16):1607-1633
https://doi.org/10.1002/(sici)1097-0061(199612)12:16<1607::aid-yea70>3.0.co;2-4 PMID: 9123965

Review

Abstract

In yeasts, pyruvate is located at a major junction of assimilatory and dissimilatory reactions as well as at the branch-point between respiratory dissimilation of sugars and alcoholic fermentation. This review deals with the enzymology, physiological function and regulation of three key reactions occurring at the pyruvate branch-point in the yeast Saccharomyces cerevisiae: (i) the direct oxidative decarboxylation of pyruvate to acetyl-CoA, catalysed by the pyruvate dehydrogenase complex, (ii) decarboxylation of pyruvate to acetaldehyde, catalysed by pyruvate decarboxylase, and (iii) the anaplerotic carboxylation of pyruvate to oxaloacetate, catalysed by pyruvate carboxylase. Special attention is devoted to physiological studies on S. cerevisiae strains in which structural genes encoding these key enzymes have been inactivated by gene disruption.

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References

Articles referenced by this article (160)

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Proteins in UniProt (Showing 5 of 11)

Pyruvate decarboxylase isozyme 3(UniProt - P26263)
Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochond(UniProt - P12695)
Pyruvate dehydrogenase complex protein X component, mitochondrial(UniProt - P16451)
Pyruvate decarboxylase isozyme 2(UniProt - P16467)
Pyruvate carboxylase 1(UniProt - P11154)

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Saccharomyces Genome Database

https://www.yeastgenome.org/reference/S000058092

Search life-sciences literature (45,103,589 articles, preprints and more)

Pyruvate metabolism in Saccharomyces cerevisiae.

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Abstract

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References

A method for gene disruption that allows repeated use of URA3 selection in the construction of multiply disrupted yeast strains.

The movement of monocarboxylic acids across phospholipid membranes: evidence for an exchange diffusion between pyruvate and other monocarboxylate ions.

Structural properties of pyruvate carboxylases from chicken liver and other sources.

Title not supplied

and (1990). Yeasts: Characteristics and Identification, 2nd edn. Cambridge University Press, Cambridge, U.K.

(1985). Regulation of enzymatic activity. In and (Eds), Pyruvate Carboxylase. CRC Press, Boca Raton, pp. 141–177.

Nucleotide and deduced amino acid sequence of the alpha subunit of yeast pyruvate dehydrogenase.

Cloning and nucleotide sequence of the gene for protein X from Saccharomyces cerevisiae.

Porin from bacterial and mitochondrial outer membranes.

ACS2, a Saccharomyces cerevisiae gene encoding acetyl-coenzyme A synthetase, essential for growth on glucose.

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Smart citations by scite.ai
Explore citation contexts and check if this article has been supported or disputed.
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Article citations

Regulating the metabolic flux of pyruvate dehydrogenase bypass to enhance lipid production in Saccharomyces cerevisiae.

Central Carbon Metabolism in Candida albicans Biofilms Is Altered by Dimethyl Sulfoxide.

Production and Characterization of Red Fruit Spirits Made from Red Raspberries, Blueberries, and Strawberries.

Spontaneous Attenuation of Alcoholic Fermentation via the Dysfunction of Cyc8p in Saccharomyces cerevisiae.

Antifungal activity of the repurposed drug disulfiram against <i>Cryptococcus neoformans</i>.

Data

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Proteins in UniProt (Showing 5 of 11)

Saccharomyces Genome Database

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Pyruvate metabolism in Saccharomyces cerevisiae.

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References

Title not supplied

and (1990). Yeasts: Characteristics and Identification, 2nd edn. Cambridge University Press, Cambridge, U.K.

(1985). Regulation of enzymatic activity. In and (Eds), Pyruvate Carboxylase. CRC Press, Boca Raton, pp. 141–177.

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