PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 21876375-4 2011 Metabolically engineered S. cerevisiae strains with overexpression of glycerol dissimilation pathway genes, including glycerol kinase (GUT1), glycerol 3-phosphate dehydrogenase (GUT2), glycerol dehydrogenase (gdh), and a glycerol transporter gene (GUP1), showed increased glycerol utilization and growth rate. Glycerol 70-78 glycerol-3-phosphate dehydrogenase Saccharomyces cerevisiae S288C 142-176 31141459-0 2019 Methylated metabolite of arsenite blocks glycerol production in yeast by inhibition of glycerol-3-phosphate dehydrogenase. Glycerol 41-49 glycerol-3-phosphate dehydrogenase Saccharomyces cerevisiae S288C 87-121 28280870-8 2017 To increase glycerol production and accumulation from glucose, we lowered the expression of TPI1 gene coding for triose phosphate isomerase; overexpressed the fused gene consisting the GPD1 and GPP2 parts coding for glycerol-3-phosphate dehydrogenase and glycerol-3-phosphate phosphatase, respectively; overexpressed the engineered FPS1 gene that codes for aquaglyceroporin; and overexpressed the truncated gene ILV2 that codes for acetolactate synthase. Glycerol 12-20 glycerol-3-phosphate dehydrogenase Saccharomyces cerevisiae S288C 216-250 26846624-4 2016 Glycerol is produced by diverting glycolytic glyceraldehyde-3-phosphate through the action of glycerol-3-phosphate dehydrogenase (coded by genes GPD1 and GPD2). Glycerol 0-8 glycerol-3-phosphate dehydrogenase Saccharomyces cerevisiae S288C 94-128 31141459-6 2019 We demonstrated that As(III) blocks glycerol production indirectly after its metabolic activation to methylarsenite (MAs(III)), which is a potent inhibitor of glycerol-3-phosphate dehydrogenase. Glycerol 36-44 glycerol-3-phosphate dehydrogenase Saccharomyces cerevisiae S288C 159-193 28549809-2 2017 In order to connect the glycolytic pathway with the pathway of 1,3-PDO synthesis from glycerol, i.e., to directly produce diol from glucose, glycerol-3-phosphate dehydrogenase and glycerol-3-phosphate phosphatase from Saccharomyces cerevisiae were overexpressed. Glycerol 86-94 glycerol-3-phosphate dehydrogenase Saccharomyces cerevisiae S288C 141-175 26596574-7 2016 In addition, ethanol production was reduced by deleting PDC1 and ADH1 genes encoding major pyruvate decarboxylase and alcohol dehydrogenase, respectively, and glycerol production was eliminated by deleting GPD1 and GPD2 genes encoding glycerol-3-phosphate dehydrogenase. Glycerol 159-167 glycerol-3-phosphate dehydrogenase Saccharomyces cerevisiae S288C 235-269 26276932-5 2015 The glycerol-producing PTS2 protein glycerol-3-phosphate dehydrogenase Gpd1p shows a tripartite localization in peroxisomes, in the cytosol, and in the nucleus under osmotic stress conditions. Glycerol 4-12 glycerol-3-phosphate dehydrogenase Saccharomyces cerevisiae S288C 36-70 26187821-5 2015 Of the eight proteins involved in glycerol metabolism, Gut2p was detected only under BFC while Pgs1p and Rhr2p were under NBFC. Glycerol 34-42 glycerol-3-phosphate dehydrogenase Saccharomyces cerevisiae S288C 55-60 24004455-2 2014 Recently, glycerol formation in anaerobic S. cerevisiae cultures was eliminated by expressing Escherichia coli (acetylating) acetaldehyde dehydrogenase (encoded by mhpF) and simultaneously deleting the GPD1 and GPD2 genes encoding glycerol-3-phosphate dehydrogenase, thus coupling NADH reoxidation to reduction of acetate to ethanol. Glycerol 10-18 glycerol-3-phosphate dehydrogenase Saccharomyces cerevisiae S288C 231-265 23537043-1 2013 BACKGROUND: Finely regulating the carbon flux through the glycerol pathway by regulating the expression of the rate controlling enzyme, glycerol-3-phosphate dehydrogenase (GPDH), has been a promising approach to redirect carbon from glycerol to ethanol and thereby increasing the ethanol yield in ethanol production. Glycerol 58-66 glycerol-3-phosphate dehydrogenase Saccharomyces cerevisiae S288C 136-170 23537043-1 2013 BACKGROUND: Finely regulating the carbon flux through the glycerol pathway by regulating the expression of the rate controlling enzyme, glycerol-3-phosphate dehydrogenase (GPDH), has been a promising approach to redirect carbon from glycerol to ethanol and thereby increasing the ethanol yield in ethanol production. Glycerol 58-66 glycerol-3-phosphate dehydrogenase Saccharomyces cerevisiae S288C 172-176 23537043-1 2013 BACKGROUND: Finely regulating the carbon flux through the glycerol pathway by regulating the expression of the rate controlling enzyme, glycerol-3-phosphate dehydrogenase (GPDH), has been a promising approach to redirect carbon from glycerol to ethanol and thereby increasing the ethanol yield in ethanol production. Glycerol 136-144 glycerol-3-phosphate dehydrogenase Saccharomyces cerevisiae S288C 172-176 21724879-1 2011 Gpd1 and Gpd2 are the two isoforms of glycerol 3-phosphate dehydrogenase (GPDH), which is the rate-controlling enzyme of glycerol formation in Saccharomyces cerevisiae. Glycerol 38-46 glycerol-3-phosphate dehydrogenase Saccharomyces cerevisiae S288C 74-78 21876375-4 2011 Metabolically engineered S. cerevisiae strains with overexpression of glycerol dissimilation pathway genes, including glycerol kinase (GUT1), glycerol 3-phosphate dehydrogenase (GUT2), glycerol dehydrogenase (gdh), and a glycerol transporter gene (GUP1), showed increased glycerol utilization and growth rate. Glycerol 70-78 glycerol-3-phosphate dehydrogenase Saccharomyces cerevisiae S288C 178-182 19727706-8 2010 Glycerol is produced to dispose excess cytosolic reduced nicotinamide adenine dinucleotide (NADH), and the regulating step in the pathway is mediated by glycerol 3-phosphate dehydrogenase (encoded by GPD1 and GPD2 genes). Glycerol 0-8 glycerol-3-phosphate dehydrogenase Saccharomyces cerevisiae S288C 153-187 20492645-4 2010 In order to assess whether glycerol production can be reduced to a certain extent without jeopardizing growth and stress tolerance, the yeast"s capacity to synthesize glycerol was adjusted by fine-tuning the activity of the rate-controlling enzyme glycerol 3-phosphate dehydrogenase (GPDH). Glycerol 27-35 glycerol-3-phosphate dehydrogenase Saccharomyces cerevisiae S288C 248-282 20492645-4 2010 In order to assess whether glycerol production can be reduced to a certain extent without jeopardizing growth and stress tolerance, the yeast"s capacity to synthesize glycerol was adjusted by fine-tuning the activity of the rate-controlling enzyme glycerol 3-phosphate dehydrogenase (GPDH). Glycerol 167-175 glycerol-3-phosphate dehydrogenase Saccharomyces cerevisiae S288C 248-282 20492645-4 2010 In order to assess whether glycerol production can be reduced to a certain extent without jeopardizing growth and stress tolerance, the yeast"s capacity to synthesize glycerol was adjusted by fine-tuning the activity of the rate-controlling enzyme glycerol 3-phosphate dehydrogenase (GPDH). Glycerol 167-175 glycerol-3-phosphate dehydrogenase Saccharomyces cerevisiae S288C 284-288 17520483-3 2007 PC depletion was found to reduce growth on glycerol and to increase glycerol excretion, both indicating that PC is needed for optimal Gut2 functioning in vivo. Glycerol 43-51 glycerol-3-phosphate dehydrogenase Saccharomyces cerevisiae S288C 134-138 18698584-0 2008 Glycerol accumulation in the dimorphic yeast Saccharomycopsis fibuligera: cloning of two glycerol 3-phosphate dehydrogenase genes, one of which is markedly induced by osmotic stress. Glycerol 0-8 glycerol-3-phosphate dehydrogenase Saccharomyces cerevisiae S288C 89-123 17520483-3 2007 PC depletion was found to reduce growth on glycerol and to increase glycerol excretion, both indicating that PC is needed for optimal Gut2 functioning in vivo. Glycerol 68-76 glycerol-3-phosphate dehydrogenase Saccharomyces cerevisiae S288C 134-138 17132142-1 2007 This study focuses on unravelling the carbon and redox metabolism of a previously developed glycerol-overproducing Saccharomyces cerevisiae strain with deletions in the structural genes encoding triosephosphate isomerase (TPI1), the external mitochondrial NADH dehydrogenases (NDE1 and NDE2) and the respiratory chain-linked glycerol-3-phosphate dehydrogenase (GUT2). Glycerol 92-100 glycerol-3-phosphate dehydrogenase Saccharomyces cerevisiae S288C 325-359 17132142-1 2007 This study focuses on unravelling the carbon and redox metabolism of a previously developed glycerol-overproducing Saccharomyces cerevisiae strain with deletions in the structural genes encoding triosephosphate isomerase (TPI1), the external mitochondrial NADH dehydrogenases (NDE1 and NDE2) and the respiratory chain-linked glycerol-3-phosphate dehydrogenase (GUT2). Glycerol 92-100 glycerol-3-phosphate dehydrogenase Saccharomyces cerevisiae S288C 361-365 11142398-1 2000 Cytosolic glycerol kinase (Gut1p) and mitochondrial glycerol-3-phosphate dehydrogenase (Gut2p) constitute the glycerol utilization pathway in Saccharomyces cerevisiae. Glycerol 10-18 glycerol-3-phosphate dehydrogenase Saccharomyces cerevisiae S288C 88-93 16208474-4 2005 Real time RT-PCR analyses identified severely attenuated transcript levels from GUT1 and GUT2 to be the source of that growth defect, the products of GUT1 and GUT2 are required for glycerol utilization. Glycerol 181-189 glycerol-3-phosphate dehydrogenase Saccharomyces cerevisiae S288C 89-93 16208474-4 2005 Real time RT-PCR analyses identified severely attenuated transcript levels from GUT1 and GUT2 to be the source of that growth defect, the products of GUT1 and GUT2 are required for glycerol utilization. Glycerol 181-189 glycerol-3-phosphate dehydrogenase Saccharomyces cerevisiae S288C 159-163 16049663-1 2005 The role for the gene encoding glycerol 3-phosphate dehydrogenase (DhGPD1) from the osmotolerant yeast Debaryomyces hansenii, in glycerol production and halotolerance, was studied through its heterologous expression in a Saccharomyces cerevisiae strain deficient in glycerol synthesis (gpd1Delta). Glycerol 129-137 glycerol-3-phosphate dehydrogenase Saccharomyces cerevisiae S288C 31-65 15118906-11 2004 Gut2 is associated with the inner membrane, and is essential for growth on glycerol-containing medium. Glycerol 75-83 glycerol-3-phosphate dehydrogenase Saccharomyces cerevisiae S288C 0-4 11676566-2 2001 It was recently shown that the most direct approach for increasing glycerol formation is to overexpress GPD1, which encodes the glycerol-3-phosphate dehydrogenase (GPDH) isoform Gpd1p. Glycerol 67-75 glycerol-3-phosphate dehydrogenase Saccharomyces cerevisiae S288C 128-162 11676566-2 2001 It was recently shown that the most direct approach for increasing glycerol formation is to overexpress GPD1, which encodes the glycerol-3-phosphate dehydrogenase (GPDH) isoform Gpd1p. Glycerol 67-75 glycerol-3-phosphate dehydrogenase Saccharomyces cerevisiae S288C 164-168 14618562-1 2003 Glycerol 3-phosphate dehydrogenase, a key enzyme in the production of glycerol, is encoded by GPD1 and GPD2. Glycerol 70-78 glycerol-3-phosphate dehydrogenase Saccharomyces cerevisiae S288C 0-34 11142398-2 2000 Transcriptional analysis of the GUT2 gene showed that it was repressed by glucose and derepressed on the non-fermentable carbon sources, glycerol, lactate and ethanol. Glycerol 137-145 glycerol-3-phosphate dehydrogenase Saccharomyces cerevisiae S288C 32-36 11068916-6 2000 The strains that produced significant glycerol exhibited efficient expression of the glycerol-3-phosphate dehydrogenase gene GPD1. Glycerol 38-46 glycerol-3-phosphate dehydrogenase Saccharomyces cerevisiae S288C 85-119 16232830-3 2000 During the glycerol-production phase, the NAD+-dependent glycerol-3-phosphate dehydrogenase (GPDH) activity of heat-shock-treated cells was much higher than that of control cells, suggesting that a higher GPDH activity enhances glycerol production. Glycerol 11-19 glycerol-3-phosphate dehydrogenase Saccharomyces cerevisiae S288C 57-91 16232830-3 2000 During the glycerol-production phase, the NAD+-dependent glycerol-3-phosphate dehydrogenase (GPDH) activity of heat-shock-treated cells was much higher than that of control cells, suggesting that a higher GPDH activity enhances glycerol production. Glycerol 11-19 glycerol-3-phosphate dehydrogenase Saccharomyces cerevisiae S288C 93-97 16232830-3 2000 During the glycerol-production phase, the NAD+-dependent glycerol-3-phosphate dehydrogenase (GPDH) activity of heat-shock-treated cells was much higher than that of control cells, suggesting that a higher GPDH activity enhances glycerol production. Glycerol 11-19 glycerol-3-phosphate dehydrogenase Saccharomyces cerevisiae S288C 205-209 16232830-3 2000 During the glycerol-production phase, the NAD+-dependent glycerol-3-phosphate dehydrogenase (GPDH) activity of heat-shock-treated cells was much higher than that of control cells, suggesting that a higher GPDH activity enhances glycerol production. Glycerol 57-65 glycerol-3-phosphate dehydrogenase Saccharomyces cerevisiae S288C 93-97 16232830-3 2000 During the glycerol-production phase, the NAD+-dependent glycerol-3-phosphate dehydrogenase (GPDH) activity of heat-shock-treated cells was much higher than that of control cells, suggesting that a higher GPDH activity enhances glycerol production. Glycerol 57-65 glycerol-3-phosphate dehydrogenase Saccharomyces cerevisiae S288C 205-209 10536147-1 1999 In Saccharomyces cerevisiae glycerol utilization is mediated by two enzymes, glycerol kinase (Gut1p) and mitochondrial glycerol-3-phosphate dehydrogenase (Gut2p). Glycerol 28-36 glycerol-3-phosphate dehydrogenase Saccharomyces cerevisiae S288C 119-153 10536147-1 1999 In Saccharomyces cerevisiae glycerol utilization is mediated by two enzymes, glycerol kinase (Gut1p) and mitochondrial glycerol-3-phosphate dehydrogenase (Gut2p). Glycerol 28-36 glycerol-3-phosphate dehydrogenase Saccharomyces cerevisiae S288C 155-160 9446611-10 1998 Glycerol is synthesized from glucose, and a rate-limiting enzyme in glycerol biosynthesis is glycerol-3-phosphate dehydrogenase (GPD1 gene product), which catalyzes reduction of dihydroxyacetone phosphate to glycerol 3-phosphate. Glycerol 0-8 glycerol-3-phosphate dehydrogenase Saccharomyces cerevisiae S288C 93-127 9872772-1 1999 Overexpression of the GPD1 gene, encoding a glycerol-3-phosphate dehydrogenase, resulted in a 1.5- to 2.5-fold increase in glycerol production and a slight decrease in ethanol formation under conditions simulating wine fermentation. Glycerol 124-132 glycerol-3-phosphate dehydrogenase Saccharomyces cerevisiae S288C 45-79 9559543-10 1998 Our results also demonstrated that of the two isoforms of NAD-dependent glycerol 3-phosphate dehydrogenase, only the enzyme encoded by GPD1 appeared important for the shuttle, since the enhanced glycerol production that occurs in a gut2 delta strain proved dependent on GPD1 but not on GPD2. Glycerol 72-80 glycerol-3-phosphate dehydrogenase Saccharomyces cerevisiae S288C 232-236 9446611-10 1998 Glycerol is synthesized from glucose, and a rate-limiting enzyme in glycerol biosynthesis is glycerol-3-phosphate dehydrogenase (GPD1 gene product), which catalyzes reduction of dihydroxyacetone phosphate to glycerol 3-phosphate. Glycerol 68-76 glycerol-3-phosphate dehydrogenase Saccharomyces cerevisiae S288C 93-127 8923738-3 1996 The glycerol yield was 4.7 times (a pdc mutant exhibiting 19% of normal PDC activity) and 6.5 times (a strain exhibiting 20-fold increased GPD activity resulting from overexpression of GPD1 gene) that of the wild type. Glycerol 4-12 glycerol-3-phosphate dehydrogenase Saccharomyces cerevisiae S288C 139-142 9234667-2 1997 Variations in the glycerol 3-phosphate dehydrogenase (GPDH) level and similar trends for alcohol dehydrogenase (ADH), pyruvate decarboxylase and glycerol-3-phosphatase were found when low and high glycerol-forming wine yeast strains were compared. Glycerol 18-26 glycerol-3-phosphate dehydrogenase Saccharomyces cerevisiae S288C 54-58 9234667-3 1997 GPDH is thus a limiting enzyme for glycerol production. Glycerol 35-43 glycerol-3-phosphate dehydrogenase Saccharomyces cerevisiae S288C 0-4 8923738-8 1996 The experimental work clearly demonstrates the rate-limiting role of GPD in glycerol formation in S. cerevisiae. Glycerol 76-84 glycerol-3-phosphate dehydrogenase Saccharomyces cerevisiae S288C 69-72 8196651-2 1994 We have cloned a gene encoding the key enzyme of glycerol synthesis, the NADH-dependent cytosolic glycerol-3-phosphate dehydrogenase, and we named it GPD1. Glycerol 49-57 glycerol-3-phosphate dehydrogenase Saccharomyces cerevisiae S288C 98-132 7729414-3 1995 Enhanced glycerol production caused by overexpression of GPD1 encoding glycerol-3-phosphate dehydrogenase also suppressed the growth defect of ggs1/tps1 delta mutants, suggesting a novel role for glycerol production in the control of glycolysis. Glycerol 9-17 glycerol-3-phosphate dehydrogenase Saccharomyces cerevisiae S288C 71-105 8082159-7 1994 We have investigated in more detail the enzymes of glycerol metabolism and found that only the cytoplasmic glycerol-3-phosphate dehydrogenase was strongly induced. Glycerol 51-59 glycerol-3-phosphate dehydrogenase Saccharomyces cerevisiae S288C 107-141 8256521-1 1993 A gut2 mutant of Saccharomyces cerevisiae is deficient in the mitochondrial glycerol 3-phosphate dehydrogenase and hence cannot utilize glycerol. Glycerol 76-84 glycerol-3-phosphate dehydrogenase Saccharomyces cerevisiae S288C 2-6 2644223-3 1989 During this conditioning, the rate of formation of glycerol, the main compatible solute in S. cerevisiae, increased threefold and the specific activity of glycerol-3-phosphate dehydrogenase (NAD+) (GPDH) (EC 1.1.1.8) was enhanced sixfold. Glycerol 51-59 glycerol-3-phosphate dehydrogenase Saccharomyces cerevisiae S288C 155-189 1772344-6 1991 It is suggested that inhibition of glycerol production during the initial period of adaptation could be due to either the inhibition of glycerol-3-phosphate dehydrogenase by increased cation content or the inhibition of glycolysis, glycerol being produced glycolytically in S. cerevisiae. Glycerol 35-43 glycerol-3-phosphate dehydrogenase Saccharomyces cerevisiae S288C 136-170 1772344-7 1991 The increased accumulation of glycerol towards the end of the 8-h period suggests that the osmoregulatory response of S. cerevisiae involves complex sets of adjustments in which inhibition of glycerol-3-phosphate dehydrogenase must be relieved before glycerol functions as a major osmoregulator. Glycerol 30-38 glycerol-3-phosphate dehydrogenase Saccharomyces cerevisiae S288C 192-226