Effect of NAD+-dependent isocitrate dehydrogenase gene (IDH1, IDH2) disruption of sake yeast on organic acid composition in sake mash

Asano, Tadao; Kurose, Naotaka; Hiraoka, Nobutsugu; Kawakita, Sadao

doi:10.1016/s1389-1723(00)80006-7

Cited by 31 publications

(21 citation statements)

References 16 publications

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“…Mitochondrial NAD + -specific Idh has been studied extensively from the aspects of the defective phenotype (Anderson et al 2005;Asano et al 1999;de Jong et al 2000;Lin et al 2001;Lin et al 2008), the kinetic characteristics (Anderson et al 2002;Lin and McAlister-Henn 2002;Lin and McAlister-Henn 2003;Lin et al 2001;Morgunov et al 2004a;Morgunov et al 2004b), and crystal structure (Garcia et al 2009;Hu et al 2005;Taylor et al 2008;Zheng and Jia 2010). However, there have been very limited researches on its involvement in lipid metabolism in oleaginous microorganism.…”

Section: Discussionmentioning

confidence: 99%

“…There are three Idh isozymes in the yeast Saccharomyces cerevisiae, including mitochondrial NAD + -specific Idh, mitochondrial NADP + -specific Idh (Idpl), and cytosol NADP + -specific Idh (Idp2) (Asano et al 1999). Mitochondrial Idh catalyzes the oxidative decarboxylation of isocitrate to form α-ketoglutarate, which is an essentially irreversible reaction (Garcia et al 2009;Hu and McAlisterHenn 2006).…”

Section: Introductionmentioning

confidence: 99%

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Characterization of the mitochondrial NAD+-dependent isocitrate dehydrogenase of the oleaginous yeast Rhodosporidium toruloides

Yang

Zhang

Zhou

et al. 2012

Appl Microbiol Biotechnol

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Early biochemical studies have demonstrated that lipid accumulation by oleaginous yeasts is linked to the activity of the NAD(+)-dependent isocitrate dehydrogenase (Idh). However, molecular study of Idh of oleaginous microorganisms remains limited. Here, we present the cloning of a mitochondrial NAD(+)-specific Idh from Rhodosporidium toruloides (RtIdh), an excellent microbial lipid producer that uses carbohydrates as the carbon source. The evolutionary relationship analyses among RtIdhs and other yeast Idhs revealed that RtIdh had a closer relationship with the Idhs of Ustilago maydis and Schizophyllum commune. We expressed the RtIDH gene in the yeast Saccharomyces cerevisiae idhΔ mutant. Under the nitrogen-limited condition, the intracellular lipid content and extracellular citrate concentration of the culture of the S. cerevisiae idhΔ carrying the RtIDH gene increased as the carbon/nitrogen molar ratio of the media increased, while the wild-type S. cerevisiae strain showed no correlation. Our data provided valuable information for elucidating the molecular mechanism of microbial oleaginicity and for engineering microorganisms to produce metabolites of fatty acid pathway.

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Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Characterization of the mitochondrial NAD+-dependent isocitrate dehydrogenase of the oleaginous yeast Rhodosporidium toruloides

Yang

Zhang

Zhou

et al. 2012

Appl Microbiol Biotechnol

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“…When the IDH1 or IDH2 genes encoding NAD + -dependent isocitrate dehydrogenase were disrupted, an increased production of citrate, malate and acetate occurred. Succinate production was reduced to approximately half of the parent strain 3 . Eight enzymes of the TCA cycle are encoded by at least 15 different nuclear genes in Saccharomyces cerevisiae 14 .…”

Section: Introductionmentioning

confidence: 96%

Beer with Reduced Ethanol Content Produced Using Saccharomyces cerevisiae Yeasts Deficient in Various Tricarboxylic Acid Cycle Enzymes

Selecký¹,

Šmogrovičová

Sulo

2008

Journal of the Institute of Brewing

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A collection of Saccharomyces cerevisiae strains deficient in the tricarboxylic acid cycle enzymes activities has been examined for the production of beer with reduced ethanol content. Strains deficient in fumarase and α-ketoglutarate dehydrogenase encoded by the genes FUM1 (0.48%), KGD1 (0.42%) and KGD2 (0.48%) made non-alcoholic beers with an alcohol content lower than 0.5% (v/v). The rest of the yeast mutants also gave rise to low-alcoholic beers but with a slightly elevated ethanol concentration (mostly in the range of 0.57-0.84% and 1.64% for the lip5 mutant). Low ethanol content was compensated by the considerable increase of organic acids (citrate succinate, fumarate, and malate). In addition, some of the mutants released high levels of lactic acid (144 (fum1), 622 (kgd1) and 495 (kgd2) mg/L). Lactic acid protects beers against contamination and masks an unacceptable worty off-flavour.

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“…It resulted in a two-fold increase in malate and an equal decrease in succinic acid production during sake fermentation (Arikawa et al, 1999a). Inhibition of NAD + -dependent isocitrate dehydrogenase via deletion of IDH1 or International Journal of Food Microbiology 204 (2015) [24][25][26][27][28][29][30][31][32] IDH2 decreased succinate production to about half of the wild-type strain during sake fermentation (Asano et al, 1999). Under aerobic conditions, deletion of these genes redirected the carbon flux towards the glyoxylate shunt and resulted in even higher yields of succinate (Raab et al, 2010).…”

Section: Introductionmentioning

confidence: 99%

Contribution of the tricarboxylic acid (TCA) cycle and the glyoxylate shunt in Saccharomyces cerevisiae to succinic acid production during dough fermentation

Rezaei

Aslankoohi

Verstrepen

et al. 2015

International Journal of Food Microbiology

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Effect of NAD+-dependent isocitrate dehydrogenase gene (IDH1, IDH2) disruption of sake yeast on organic acid composition in sake mash

Cited by 31 publications

References 16 publications

Characterization of the mitochondrial NAD+-dependent isocitrate dehydrogenase of the oleaginous yeast Rhodosporidium toruloides

Characterization of the mitochondrial NAD+-dependent isocitrate dehydrogenase of the oleaginous yeast Rhodosporidium toruloides

Beer with Reduced Ethanol Content Produced Using Saccharomyces cerevisiae Yeasts Deficient in Various Tricarboxylic Acid Cycle Enzymes

Contribution of the tricarboxylic acid (TCA) cycle and the glyoxylate shunt in Saccharomyces cerevisiae to succinic acid production during dough fermentation

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