{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,6]],"date-time":"2026-10-06T20:39:56Z","timestamp":1791319196202,"version":"4.3.1"},"reference-count":161,"publisher":"MDPI AG","issue":"5","license":[{"start":{"date-parts":[[2021,5,12]],"date-time":"2021-05-12T00:00:00Z","timestamp":1620777600000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Biomolecules"],"abstract":"<jats:p>The pentose phosphate pathway (PPP) is a route that can work in parallel to glycolysis in glucose degradation in most living cells. It has a unidirectional oxidative part with glucose-6-phosphate dehydrogenase as a key enzyme generating NADPH, and a non-oxidative part involving the reversible transketolase and transaldolase reactions, which interchange PPP metabolites with glycolysis. While the oxidative branch is vital to cope with oxidative stress, the non-oxidative branch provides precursors for the synthesis of nucleic, fatty and aromatic amino acids. For glucose catabolism in the baker\u2019s yeast Saccharomyces cerevisiae, where its components were first discovered and extensively studied, the PPP plays only a minor role. In contrast, PPP and glycolysis contribute almost equally to glucose degradation in other yeasts. We here summarize the data available for the PPP enzymes focusing on S. cerevisiae and Kluyveromyces lactis, and describe the phenotypes of gene deletions and the benefits of their overproduction and modification. Reference to other yeasts and to the importance of the PPP in their biotechnological and medical applications is briefly being included. We propose future studies on the PPP in K. lactis to be of special interest for basic science and as a host for the expression of human disease genes.<\/jats:p>","DOI":"10.3390\/biom11050725","type":"journal-article","created":{"date-parts":[[2021,5,12]],"date-time":"2021-05-12T10:59:12Z","timestamp":1620817152000},"page":"725","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":132,"title":["The Pentose Phosphate Pathway in Yeasts\u2013More Than a Poor Cousin of Glycolysis"],"prefix":"10.3390","volume":"11","author":[{"given":"Laura-Katharina","family":"Bertels","sequence":"first","affiliation":[{"name":"Department of Genetics, Faculty of Biology\/Chemistry, University of Osnabr\u00fcck, Barbarastrasse 11, D-49076 Osnabr\u00fcck, Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-9281-8296","authenticated-orcid":false,"given":"Luc\u00eda","family":"Fern\u00e1ndez Murillo","sequence":"additional","affiliation":[{"name":"Department of Genetics, Faculty of Biology\/Chemistry, University of Osnabr\u00fcck, Barbarastrasse 11, D-49076 Osnabr\u00fcck, Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-4197-4285","authenticated-orcid":false,"given":"J\u00fcrgen J.","family":"Heinisch","sequence":"additional","affiliation":[{"name":"Department of Genetics, Faculty of Biology\/Chemistry, University of Osnabr\u00fcck, Barbarastrasse 11, D-49076 Osnabr\u00fcck, Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2021,5,12]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"1511","DOI":"10.1021\/acs.biochem.8b01236","article-title":"Synthetic Biology of Yeast","volume":"58","author":"Liu","year":"2019","journal-title":"Biochemistry"},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"e1800421","DOI":"10.1002\/biot.201800421","article-title":"Yeast systems biology: Model organism and cell factory","volume":"14","author":"Nielsen","year":"2019","journal-title":"Biotechnol. J."},{"key":"ref_3","doi-asserted-by":"crossref","first-page":"695","DOI":"10.1534\/genetics.111.130765","article-title":"Yeast: An Experimental Organism for 21st Century Biology","volume":"189","author":"Botstein","year":"2011","journal-title":"Genetics"},{"key":"ref_4","doi-asserted-by":"crossref","first-page":"33","DOI":"10.1534\/genetics.114.163188","article-title":"Budding Yeast for Budding Geneticists: A Primer on the Saccharomyces cerevisiae Model System","volume":"197","author":"Duina","year":"2014","journal-title":"Genetics"},{"key":"ref_5","doi-asserted-by":"crossref","unstructured":"Lacerda, M.P., Oh, E.J., and Eckert, C. (2020). The Model System Saccharomyces cerevisiae versus Emerging Non-Model Yeasts for the Production of Biofuels. Life, 10.","DOI":"10.3390\/life10110299"},{"key":"ref_6","doi-asserted-by":"crossref","first-page":"107695","DOI":"10.1016\/j.biotechadv.2021.107695","article-title":"Recent advances in systems and synthetic biology approaches for developing novel cell-factories in non-conventional yeasts","volume":"47","author":"Patra","year":"2021","journal-title":"Biotechnol. Adv."},{"key":"ref_7","doi-asserted-by":"crossref","first-page":"126","DOI":"10.1016\/j.fgb.2015.12.001","article-title":"Synthetic biology and molecular genetics in non-conventional yeasts: Current tools and future advances","volume":"89","author":"Wagner","year":"2016","journal-title":"Fungal Genet. Biol."},{"key":"ref_8","doi-asserted-by":"crossref","first-page":"165","DOI":"10.1002\/yea.2954","article-title":"Yeast on the milky way: Genetics, physiology and biotechnology of Kluyveromyces lactis","volume":"30","author":"Rodicio","year":"2013","journal-title":"Yeast"},{"key":"ref_9","doi-asserted-by":"crossref","first-page":"183","DOI":"10.1111\/j.1462-5822.2008.01259.x","article-title":"Responses to hypoxia in fungal pathogens","volume":"11","author":"Ernst","year":"2009","journal-title":"Cell. Microbiol."},{"key":"ref_10","doi-asserted-by":"crossref","first-page":"7","DOI":"10.1016\/j.mib.2020.05.006","article-title":"The gut, the bad and the harmless: Candida albicans as a commensal and opportunistic pathogen in the intestine","volume":"56","author":"Kumamoto","year":"2020","journal-title":"Curr. Opin. Microbiol."},{"key":"ref_11","doi-asserted-by":"crossref","first-page":"927","DOI":"10.1111\/brv.12140","article-title":"The return of metabolism: Biochemistry and physiology of the pentose phosphate pathway","volume":"90","author":"Stincone","year":"2015","journal-title":"Biol. Rev."},{"key":"ref_12","doi-asserted-by":"crossref","first-page":"826","DOI":"10.1111\/1567-1364.12161","article-title":"Why, when, and how did yeast evolve alcoholic fermentation?","volume":"14","author":"Dashko","year":"2014","journal-title":"FEMS Yeast Res."},{"key":"ref_13","first-page":"507","article-title":"Carbohydrate and energy-yielding metabolism in non-conventional yeasts","volume":"24","author":"Flores","year":"2000","journal-title":"FEMS Microbiol. Rev."},{"key":"ref_14","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1111\/j.1365-313X.2005.02427.x","article-title":"New insights into plant transaldolase","volume":"43","author":"Caillau","year":"2005","journal-title":"Plant J."},{"key":"ref_15","doi-asserted-by":"crossref","first-page":"6","DOI":"10.1016\/j.jbiotec.2006.11.021","article-title":"Engineering primary metabolic pathways of industrial micro-organisms","volume":"129","author":"Kern","year":"2007","journal-title":"J. Biotechnol."},{"key":"ref_16","doi-asserted-by":"crossref","first-page":"236","DOI":"10.1016\/S1369-5266(03)00039-6","article-title":"The oxidative pentose phosphate pathway: Structure and organisation","volume":"6","author":"Kruger","year":"2003","journal-title":"Curr. Opin. Plant Biol."},{"key":"ref_17","doi-asserted-by":"crossref","first-page":"50","DOI":"10.1186\/1475-2859-11-50","article-title":"Recent advances in engineering the central carbon metabolism of industrially important bacteria","volume":"11","author":"Papagianni","year":"2012","journal-title":"Microb. Cell Factories"},{"key":"ref_18","doi-asserted-by":"crossref","first-page":"e200012","DOI":"10.20900\/immunometab20200012","article-title":"Metabolic Targets for Treatment of Autoimmune Diseases","volume":"2","author":"Piranavan","year":"2020","journal-title":"Immunometabolism"},{"key":"ref_19","doi-asserted-by":"crossref","unstructured":"Rajas, F., Gautier-Stein, A., and Mithieux, G. (2019). Glucose-6 Phosphate, a Central Hub for Liver Carbohydrate Metabolism. Metabolites, 9.","DOI":"10.3390\/metabo9120282"},{"key":"ref_20","doi-asserted-by":"crossref","first-page":"227","DOI":"10.1007\/BF00420611","article-title":"Construction and physiological characterization of mutants disrupted in the phosphofructokinase genes of Saccharomyces cerevisiae","volume":"11","author":"Heinisch","year":"1986","journal-title":"Curr. Genet."},{"key":"ref_21","doi-asserted-by":"crossref","unstructured":"Alfarouk, K.O., Ahmed, S.B.M., Elliott, R.L., Benoit, A., Alqahtani, S.S., Ibrahim, M.E., Bashir, A.H.H., AlHoufie, S.T.S., Elhassan, G.O., and Wales, C.C. (2020). The Pentose Phosphate Pathway Dynamics in Cancer and Its Dependency on Intracellular pH. Metabolites, 10.","DOI":"10.3390\/metabo10070285"},{"key":"ref_22","doi-asserted-by":"crossref","first-page":"73","DOI":"10.2174\/1871529X11313010008","article-title":"Glucose-6-Phosphate Dehydrogenase Deficiency: Disadvantages and Possible Benefits","volume":"13","author":"Manganelli","year":"2013","journal-title":"Cardiovasc. Hematol. Disord. Drug Targets"},{"key":"ref_23","doi-asserted-by":"crossref","first-page":"347","DOI":"10.1155\/2005\/314760","article-title":"Biosynthesis of ribose-5-phosphate and erythrose-4-phosphate in archaea: A phylogenetic analysis of archaeal genomes","volume":"1","author":"Soderberg","year":"2005","journal-title":"Archaea"},{"key":"ref_24","doi-asserted-by":"crossref","first-page":"1105","DOI":"10.1016\/j.febslet.2015.03.026","article-title":"The oxidative pentose phosphate pathway in the haloarchaeon Haloferax volcanii involves a novel type of glucose-6-phosphate dehydrogenase\u2014The archaeal Zwischenferment","volume":"589","author":"Pickl","year":"2015","journal-title":"FEBS Lett."},{"key":"ref_25","doi-asserted-by":"crossref","first-page":"969","DOI":"10.1016\/j.cell.2011.05.022","article-title":"Riboneogenesis in Yeast","volume":"145","author":"Clasquin","year":"2011","journal-title":"Cell"},{"key":"ref_26","doi-asserted-by":"crossref","unstructured":"Heinisch, J.J., Knuesting, J., and Scheibe, R. (2020). Investigation of Heterologously Expressed Glucose-6-Phosphate Dehydrogenase Genes in a Yeast zwf1 Deletion. Microorganisms, 8.","DOI":"10.3390\/microorganisms8040546"},{"key":"ref_27","doi-asserted-by":"crossref","first-page":"15","DOI":"10.1007\/s002940050171","article-title":"Analysis of a transketolase gene from Kluyveromyces lactis reveals that the yeast enzymes are more related to transketolases of prokaryotic origins than to those of higher eukaryotes","volume":"31","author":"Jacoby","year":"1997","journal-title":"Curr. Genet."},{"key":"ref_28","doi-asserted-by":"crossref","first-page":"456","DOI":"10.1007\/BF02173011","article-title":"Mutants that show increased sensitivity to hydrogen peroxide reveal an important role for the pentose phosphate pathway in protection of yeast against oxidative stress","volume":"252","author":"Juhnke","year":"1996","journal-title":"Mol. Genet. Genom."},{"key":"ref_29","doi-asserted-by":"crossref","first-page":"161","DOI":"10.1016\/0378-1119(90)90248-P","article-title":"Isolation and characterization of the ZWF1 gene of Saccharomyces cerevisiae, encoding glucose-6-phosphate dehydrogenase","volume":"96","author":"Nogae","year":"1990","journal-title":"Gene"},{"key":"ref_30","doi-asserted-by":"crossref","first-page":"547","DOI":"10.1002\/j.1460-2075.1991.tb07981.x","article-title":"Identification of the structural gene for glucose-6-phosphate dehydrogenase in yeast. Inactivation leads to a nutritional requirement for organic sulfur","volume":"10","author":"Thomas","year":"1991","journal-title":"EMBO J."},{"key":"ref_31","doi-asserted-by":"crossref","first-page":"19","DOI":"10.1128\/EC.00189-06","article-title":"Deletion of the Glucose-6-Phosphate Dehydrogenase Gene KlZWF1 Affects both Fermentative and Respiratory Metabolism in Kluyveromyces lactis","volume":"6","author":"Saliola","year":"2006","journal-title":"Eukaryot. Cell"},{"key":"ref_32","doi-asserted-by":"crossref","first-page":"1503","DOI":"10.1128\/EC.00211-12","article-title":"Intracellular NADPH Levels Affect the Oligomeric State of the Glucose 6-Phosphate Dehydrogenase","volume":"11","author":"Saliola","year":"2012","journal-title":"Eukaryot. Cell"},{"key":"ref_33","doi-asserted-by":"crossref","first-page":"R49","DOI":"10.1186\/gb-2005-6-6-r49","article-title":"Large-scale 13C-flux analysis reveals mechanistic principles of metabolic network robustness to null mutations in yeast","volume":"6","author":"Blank","year":"2005","journal-title":"Genome Biol."},{"key":"ref_34","doi-asserted-by":"crossref","first-page":"117","DOI":"10.1534\/genetics.104.030452","article-title":"Division of Labor Among the Yeast Sol Proteins Implicated in tRNA Nuclear Export and Carbohydrate Metabolism","volume":"168","author":"Stanford","year":"2004","journal-title":"Genetics"},{"key":"ref_35","doi-asserted-by":"crossref","unstructured":"He, W., Wang, Y., Liu, W., and Zhou, C.-Z. (2007). Crystal structure of Saccharomyces cerevisiae 6-phosphogluconate dehydrogenase Gnd1. BMC Struct. Biol., 7.","DOI":"10.1186\/1472-6807-7-38"},{"key":"ref_36","doi-asserted-by":"crossref","first-page":"367","DOI":"10.1007\/BF00330815","article-title":"Pentose phosphate pathway mutants of yeast","volume":"185","author":"Lobo","year":"1982","journal-title":"Mol. Genet. Genom."},{"key":"ref_37","doi-asserted-by":"crossref","first-page":"1241","DOI":"10.1002\/yea.320091111","article-title":"Lysine144 is essential for the catalytic activity of Saccharomyces cerevisiae transaldolase","volume":"9","author":"Miosga","year":"1993","journal-title":"Yeast"},{"key":"ref_38","doi-asserted-by":"crossref","first-page":"65","DOI":"10.1042\/bj20031268","article-title":"Pyridoxine biosynthesis in yeast: Participation of ribose 5-phosphate ketol-isomerase","volume":"379","author":"Kondo","year":"2004","journal-title":"Biochem. J."},{"key":"ref_39","doi-asserted-by":"crossref","first-page":"47965","DOI":"10.1074\/jbc.X200007200","article-title":"The Pentose Phosphate Pathway","volume":"277","author":"Horecker","year":"2002","journal-title":"J. Biol. Chem."},{"key":"ref_40","doi-asserted-by":"crossref","first-page":"2373","DOI":"10.1002\/j.1460-2075.1992.tb05301.x","article-title":"Three-dimensional structure of transketolase, a thiamine diphosphate dependent enzyme, at 2.5 A resolution","volume":"11","author":"Lindqvist","year":"1992","journal-title":"EMBO J."},{"key":"ref_41","doi-asserted-by":"crossref","first-page":"597","DOI":"10.1111\/j.1432-1033.1990.tb15440.x","article-title":"Molecular analysis of the structural gene for yeast transaldolase","volume":"188","author":"Schaaff","year":"1990","journal-title":"Eur. J. Biochem."},{"key":"ref_42","doi-asserted-by":"crossref","first-page":"487","DOI":"10.1111\/j.1432-1033.1993.tb18268.x","article-title":"TKL2, a second transketolase gene of Saccharomyces cerevisiae. Cloning, sequence and deletion analysis of the gene","volume":"217","author":"Mannhaupt","year":"1993","journal-title":"Eur. J. Biochem."},{"key":"ref_43","doi-asserted-by":"crossref","first-page":"373","DOI":"10.1007\/BF00351843","article-title":"Pentose-phosphate pathway in Saccharomyces cerevisiae: Analysis of deletion mutants for transketolase, transaldolase, and glucose 6-phosphate dehydrogenase","volume":"24","author":"Zimmermann","year":"1993","journal-title":"Curr. Genet."},{"key":"ref_44","doi-asserted-by":"crossref","first-page":"867","DOI":"10.1111\/j.1365-2958.1993.tb00957.x","article-title":"Transaldolase mutants in the yeast Kluyveromyces lactis provide evidence that glucose can be metabolized through the pentose phosphate pathway","volume":"10","author":"Jacoby","year":"1993","journal-title":"Mol. Microbiol."},{"key":"ref_45","doi-asserted-by":"crossref","first-page":"267","DOI":"10.1016\/j.bcmd.2008.12.005","article-title":"The global prevalence of glucose-6-phosphate dehydrogenase deficiency: A systematic review and meta-analysis","volume":"42","author":"Nkhoma","year":"2009","journal-title":"Blood Cells Mol. Dis."},{"key":"ref_46","unstructured":"Richardson, S.R., and O\u2019Malley, G.F. (2021). Glucose-6-Phosphate Dehydrogenase Deficiency, StatPearls."},{"key":"ref_47","doi-asserted-by":"crossref","first-page":"283","DOI":"10.1002\/yea.3461","article-title":"Vitamin requirements and biosynthesis in Saccharomyces cerevisiae","volume":"37","author":"Perli","year":"2020","journal-title":"Yeast"},{"key":"ref_48","doi-asserted-by":"crossref","first-page":"97","DOI":"10.1002\/9780470122938.ch3","article-title":"Glucose-6-Phosphate Dehydrogenases","volume":"48","author":"Levy","year":"1979","journal-title":"Adv. Enzymol. Relat. Areas Mol. Biol."},{"key":"ref_49","doi-asserted-by":"crossref","first-page":"16040","DOI":"10.1074\/jbc.274.23.16040","article-title":"Yap1 and Skn7 Control Two Specialized Oxidative Stress Response Regulons in Yeast","volume":"274","author":"Lee","year":"1999","journal-title":"J. Biol. Chem."},{"key":"ref_50","doi-asserted-by":"crossref","first-page":"39890","DOI":"10.1074\/jbc.M509461200","article-title":"Sources of NADPH in Yeast Vary with Carbon Source","volume":"280","author":"Minard","year":"2005","journal-title":"J. Biol. Chem."},{"key":"ref_51","doi-asserted-by":"crossref","first-page":"543","DOI":"10.1089\/ars.2015.6516","article-title":"Methionine Metabolism Alters Oxidative Stress Resistanceviathe Pentose Phosphate Pathway","volume":"24","author":"Campbell","year":"2016","journal-title":"Antioxid. Redox Signal."},{"key":"ref_52","doi-asserted-by":"crossref","first-page":"13984","DOI":"10.1074\/jbc.M210076200","article-title":"The ALD6 Gene Product Is Indispensable for Providing NADPH in Yeast Cells Lacking Glucose-6-phosphate Dehydrogenase Activity","volume":"278","author":"Grabowska","year":"2003","journal-title":"J. Biol. Chem."},{"key":"ref_53","doi-asserted-by":"crossref","first-page":"241","DOI":"10.1007\/BF00418587","article-title":"The Pasteur effect and catabolite repression in an oxidative yeast, Kluyveromyces lactis","volume":"45","author":"Royt","year":"1979","journal-title":"Antonie Leeuwenhoek"},{"key":"ref_54","first-page":"17","article-title":"An evolutionary perspective on the Crabtree effect","volume":"1","author":"Epfeiffer","year":"2014","journal-title":"Front. Mol. Biosci."},{"key":"ref_55","doi-asserted-by":"crossref","first-page":"61","DOI":"10.1111\/j.1567-1364.2011.00761.x","article-title":"Alternative splicing directs dual localization of Candida albicans 6-phosphogluconate dehydrogenase to cytosol and peroxisomes","volume":"12","author":"Strijbis","year":"2011","journal-title":"FEMS Yeast Res."},{"key":"ref_56","doi-asserted-by":"crossref","first-page":"e00913-19","DOI":"10.1128\/mSphere.00913-19","article-title":"Metabolic Reprogramming in the Opportunistic Yeast Candida albicans in Response to Hypoxia","volume":"5","author":"Burgain","year":"2020","journal-title":"mSphere"},{"key":"ref_57","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1007\/s00253-020-10808-4","article-title":"Functional analysis of PGI1 and ZWF1 in thermotolerant yeast Kluyveromyces marxianus","volume":"104","author":"Zhang","year":"2020","journal-title":"Appl. Microbiol. Biotechnol."},{"key":"ref_58","doi-asserted-by":"crossref","first-page":"645","DOI":"10.1139\/o98-001","article-title":"Regulation of D-glucose-6-phosphate dehydrogenase from Schizosaccharomyces pombe","volume":"76","author":"Tsai","year":"1998","journal-title":"Biochem. Cell Biol."},{"key":"ref_59","doi-asserted-by":"crossref","first-page":"41","DOI":"10.1111\/j.1432-1033.1993.tb17630.x","article-title":"Glucose-6-phosphate dehydrogenase. Structure-function relationships and the Pichia jadinii enzyme structure","volume":"212","author":"Jeffery","year":"1993","journal-title":"Eur. J. Biochem."},{"key":"ref_60","doi-asserted-by":"crossref","first-page":"2006-0001","DOI":"10.1038\/msb4100043","article-title":"Global analysis of gene function in yeast by quantitative phenotypic profiling","volume":"2","author":"Brown","year":"2006","journal-title":"Mol. Syst. Biol."},{"key":"ref_61","doi-asserted-by":"crossref","first-page":"1456","DOI":"10.1101\/gr.3672305","article-title":"The Yeast Gene Order Browser: Combining curated homology and syntenic context reveals gene fate in polyploid species","volume":"15","author":"Byrne","year":"2005","journal-title":"Genome Res."},{"key":"ref_62","doi-asserted-by":"crossref","first-page":"1865","DOI":"10.1099\/00221287-138-9-1865","article-title":"Induction of specific enzymes of the oxidative pentose phosphate pathway by glucono-lactone in Saccharomyces cerevisiae","volume":"138","author":"Sinha","year":"1992","journal-title":"J. Gen. Microbiol."},{"key":"ref_63","doi-asserted-by":"crossref","first-page":"2036","DOI":"10.1021\/bi00059a021","article-title":"Overall kinetic mechanism of 6-phosphogluconate dehydrogenase from Candida utilis","volume":"32","author":"Berdis","year":"1993","journal-title":"Biochemistry"},{"key":"ref_64","doi-asserted-by":"crossref","first-page":"637","DOI":"10.1139\/o98-083","article-title":"Purification and kinetic characterization of 6-phosphogluconate dehydrogenase from Schizosaccharomyces pombe","volume":"76","author":"Tsai","year":"1998","journal-title":"Biochem. Cell Biol."},{"key":"ref_65","doi-asserted-by":"crossref","first-page":"404","DOI":"10.1007\/s002940050149","article-title":"Cloning and characterization of the first two genes of the non-oxidative part of the Saccharomyces cerevisiae pentose-phosphate pathway","volume":"30","author":"Miosga","year":"1996","journal-title":"Curr. Genet."},{"key":"ref_66","doi-asserted-by":"crossref","first-page":"1326","DOI":"10.1111\/j.1742-4658.2005.04562.x","article-title":"Effect of coenzyme modification on the structural and catalytic properties of wild-type transketolase and of the variant E418A from Saccharomyces cerevisiae","volume":"272","author":"Golbik","year":"2005","journal-title":"FEBS J."},{"key":"ref_67","doi-asserted-by":"crossref","first-page":"229","DOI":"10.1016\/0014-5793(92)81197-T","article-title":"Three-dimensional structure of apotransketolase flexible loops at the active site enable cofactor binding","volume":"313","author":"Lindqvist","year":"1992","journal-title":"FEBS Lett."},{"key":"ref_68","doi-asserted-by":"crossref","first-page":"1131","DOI":"10.1016\/j.freeradbiomed.2007.12.008","article-title":"Adaptation to hydrogen peroxide in Saccharomyces cerevisiae: The role of NADPH-generating systems and the SKN7 transcription factor","volume":"44","author":"Ng","year":"2008","journal-title":"Free. Radic. Biol. Med."},{"key":"ref_69","doi-asserted-by":"crossref","first-page":"16","DOI":"10.1016\/j.enzmictec.2012.03.008","article-title":"Characterization of non-oxidative transaldolase and transketolase enzymes in the pentose phosphate pathway with regard to xylose utilization by recombinant Saccharomyces cerevisiae","volume":"51","author":"Matsushika","year":"2012","journal-title":"Enzym. Microb. Technol."},{"key":"ref_70","doi-asserted-by":"crossref","first-page":"125","DOI":"10.1007\/s00438-010-0592-x","article-title":"Genome-wide screen for inositol auxotrophy in Saccharomyces cerevisiae implicates lipid metabolism in stress response signaling","volume":"285","author":"Choi","year":"2011","journal-title":"Mol. Genet. Genom."},{"key":"ref_71","doi-asserted-by":"crossref","first-page":"69","DOI":"10.1016\/0003-9861(77)90172-2","article-title":"Purification and crystallization of transaldolase isozyme I and evidence for different genetic origin of isozymes I and III in Candida utilis","volume":"178","author":"Sun","year":"1977","journal-title":"Arch. Biochem. Biophys."},{"key":"ref_72","doi-asserted-by":"crossref","first-page":"5689","DOI":"10.1093\/jxb\/erx367","article-title":"Octulose: A forgotten metabolite?","volume":"68","author":"Zhang","year":"2017","journal-title":"J. Exp. Bot."},{"key":"ref_73","doi-asserted-by":"crossref","first-page":"1867","DOI":"10.1074\/jbc.RA119.011239","article-title":"The pentose phosphate pathway of cellulolytic clostridia relies on 6-phosphofructokinase instead of transaldolase","volume":"295","author":"Koendjbiharie","year":"2020","journal-title":"J. Biol. Chem."},{"key":"ref_74","first-page":"288","article-title":"Characterization of recombinant PPi-dependent 6-phosphofructokinases from Methylosinus trichosporium OB3b and Methylobacterium nodulans ORS 2060","volume":"77","author":"Rozova","year":"2012","journal-title":"Biochemistry"},{"key":"ref_75","doi-asserted-by":"crossref","first-page":"536","DOI":"10.1007\/BF00341459","article-title":"Genetic and physiological evidence for the existence of a second glycolytic pathway in yeast parallel to the phosphofructokinase-aldolase reaction sequence","volume":"195","author":"Schmitt","year":"1984","journal-title":"Mol. Genet. Genom."},{"key":"ref_76","doi-asserted-by":"crossref","first-page":"90","DOI":"10.1111\/j.1432-1033.1973.tb02961.x","article-title":"Reduced Pyridine-Nucleotides Balance in Glucose-Growing Saccharomyces cerevisiae","volume":"37","author":"Lagunas","year":"1973","journal-title":"Eur. J. Biochem."},{"key":"ref_77","doi-asserted-by":"crossref","first-page":"152","DOI":"10.1128\/jb.139.1.152-160.1979","article-title":"Physiological Effects of Seven Different Blocks in Glycolysis in Saccharomyces cerevisiae","volume":"139","author":"Ciriacy","year":"1979","journal-title":"J. Bacteriol."},{"key":"ref_78","doi-asserted-by":"crossref","first-page":"401","DOI":"10.1007\/BF00260633","article-title":"A phosphoglucose isomerase gene is involved in the Rag phenotype of the yeast Kluyveromyces lactis","volume":"228","author":"Goffrini","year":"1991","journal-title":"Mol. Genet. Genom."},{"key":"ref_79","doi-asserted-by":"crossref","first-page":"559","DOI":"10.1111\/j.1365-2958.1993.tb01600.x","article-title":"Molecular genetics of phosphofructokinase in the yeast Kluyveromyces lactis","volume":"8","author":"Heinisch","year":"1993","journal-title":"Mol. Microbiol."},{"key":"ref_80","first-page":"469","article-title":"The role of the NAD-dependent glutamate dehydrogenase in restoring growth on glucose of a Saccharomyces cerevisiae phosphoglucose isomerase mutant","volume":"217","author":"Boles","year":"1993","journal-title":"JBIC J. Biol. Inorg. Chem."},{"key":"ref_81","doi-asserted-by":"crossref","first-page":"813","DOI":"10.1002\/yea.878","article-title":"Two mechanisms for oxidation of cytosolic NADPH by Kluyveromyces lactis mitochondria","volume":"19","author":"Overkamp","year":"2002","journal-title":"Yeast"},{"key":"ref_82","doi-asserted-by":"crossref","first-page":"199","DOI":"10.1016\/j.bbabio.2004.12.008","article-title":"The nuclear genes encoding the internal (KlNDI1) and external (KlNDE1) alternative NAD(P)H:ubiquinone oxidoreductases of mitochondria from Kluyveromyces lactis","volume":"1707","author":"Prado","year":"2005","journal-title":"Biochim. Biophys. Acta (BBA) Bioenerg."},{"key":"ref_83","doi-asserted-by":"crossref","first-page":"1441","DOI":"10.1128\/JB.183.4.1441-1451.2001","article-title":"Network Identification and Flux Quantification in the Central Metabolism of Saccharomyces cerevisiae under Different Conditions of Glucose Repression","volume":"183","author":"Gombert","year":"2001","journal-title":"J. Bacteriol."},{"key":"ref_84","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1007\/s11306-019-1584-4","article-title":"Metabolic switches from quiescence to growth in synchronized Saccharomyces cerevisiae","volume":"15","author":"Zhang","year":"2019","journal-title":"Metabolomics"},{"key":"ref_85","doi-asserted-by":"crossref","first-page":"4970","DOI":"10.1111\/j.1742-4658.2005.04907.x","article-title":"Revisiting the 13C-label distribution of the non-oxidative branch of the pentose phosphate pathway based upon kinetic and genetic evidence","volume":"272","author":"Kleijn","year":"2005","journal-title":"FEBS J."},{"key":"ref_86","doi-asserted-by":"crossref","first-page":"545","DOI":"10.1016\/j.femsyr.2004.09.008","article-title":"Metabolic-flux and network analysis in fourteen hemiascomycetous yeasts","volume":"5","author":"Blank","year":"2005","journal-title":"FEMS Yeast Res."},{"key":"ref_87","doi-asserted-by":"crossref","first-page":"311","DOI":"10.1089\/ars.2010.3797","article-title":"The Pentose Phosphate Pathway Is a Metabolic Redox Sensor and Regulates Transcription During the Antioxidant Response","volume":"15","author":"Wamelink","year":"2011","journal-title":"Antioxid. Redox Signal."},{"key":"ref_88","doi-asserted-by":"crossref","first-page":"10","DOI":"10.1186\/jbiol61","article-title":"Dynamic rerouting of the carbohydrate flux is key to counteracting oxidative stress","volume":"6","author":"Ralser","year":"2007","journal-title":"J. Biol."},{"key":"ref_89","doi-asserted-by":"crossref","first-page":"519","DOI":"10.1016\/j.molcel.2015.08.002","article-title":"Metabolic Remodeling in Times of Stress: Who Shoots Faster than His Shadow?","volume":"59","author":"Dick","year":"2015","journal-title":"Mol. Cell"},{"key":"ref_90","doi-asserted-by":"crossref","first-page":"359","DOI":"10.1016\/j.molcel.2015.06.017","article-title":"Acute Activation of Oxidative Pentose Phosphate Pathway as First-Line Response to Oxidative Stress in Human Skin Cells","volume":"59","author":"Kuehne","year":"2015","journal-title":"Mol. Cell"},{"key":"ref_91","doi-asserted-by":"crossref","first-page":"877","DOI":"10.1182\/blood.V41.6.877.877","article-title":"Regulation of glucose-6-phosphate dehydrogenase activity in red blood cells from hemolytic and non-hemolytic variant subjects","volume":"41","author":"Yoshida","year":"1973","journal-title":"Blood"},{"key":"ref_92","doi-asserted-by":"crossref","unstructured":"R\u00f8st, L.M., Thorfinnsdottir, L.B., Kumar, K., Fuchino, K., Lang\u00f8rgen, I.E., Bartosova, Z., Kristiansen, K.A., and Bruheim, P. (2020). Absolute Quantification of the Central Carbon Metabolome in Eight Commonly Applied Prokaryotic and Eukaryotic Model Systems. Metabolites, 10.","DOI":"10.3390\/metabo10020074"},{"key":"ref_93","doi-asserted-by":"crossref","first-page":"3","DOI":"10.1093\/femsyr\/foz027","article-title":"Effects of overexpression of STB5 in Saccharomyces cerevisiae on fatty acid biosynthesis, physiology and transcriptome","volume":"19","author":"Bergman","year":"2019","journal-title":"FEMS Yeast Res."},{"key":"ref_94","doi-asserted-by":"crossref","first-page":"1251","DOI":"10.1038\/nbt.1499","article-title":"Activity motifs reveal principles of timing in transcriptional control of the yeast metabolic network","volume":"26","author":"Chechik","year":"2008","journal-title":"Nat. Biotechnol."},{"key":"ref_95","doi-asserted-by":"crossref","first-page":"6690","DOI":"10.1128\/MCB.02450-05","article-title":"Oxidative Stress-Activated Zinc Cluster Protein Stb5 Has Dual Activator\/Repressor Functions Required for Pentose Phosphate Pathway Regulation and NADPH Production","volume":"26","author":"LaRochelle","year":"2006","journal-title":"Mol. Cell. Biol."},{"key":"ref_96","doi-asserted-by":"crossref","first-page":"509","DOI":"10.1002\/yea.986","article-title":"A history of research on yeasts 5: The fermentation pathway","volume":"20","author":"Barnett","year":"2003","journal-title":"Yeast"},{"key":"ref_97","doi-asserted-by":"crossref","first-page":"379","DOI":"10.1128\/MMBR.00025-07","article-title":"Progress in Metabolic Engineering of Saccharomyces cerevisiae","volume":"72","author":"Nevoigt","year":"2008","journal-title":"Microbiol. Mol. Biol. Rev."},{"key":"ref_98","doi-asserted-by":"crossref","first-page":"937","DOI":"10.1016\/j.foodchem.2015.11.063","article-title":"The bio refinery; producing feed and fuel from grain","volume":"197","author":"Scholey","year":"2016","journal-title":"Food Chem."},{"key":"ref_99","doi-asserted-by":"crossref","first-page":"fox044","DOI":"10.1093\/femsyr\/fox044","article-title":"Saccharomyces cerevisiae strains for second-generation ethanol production: From academic exploration to industrial implementation","volume":"17","author":"Jansen","year":"2017","journal-title":"FEMS Yeast Res."},{"key":"ref_100","doi-asserted-by":"crossref","first-page":"883","DOI":"10.1080\/21655979.2020.1801178","article-title":"Engineered Saccharomyces cerevisiae for lignocellulosic valorization: A review and perspectives on bioethanol production","volume":"11","author":"Cunha","year":"2020","journal-title":"Bioengineered"},{"key":"ref_101","doi-asserted-by":"crossref","first-page":"89","DOI":"10.1016\/0378-1119(91)90592-Y","article-title":"Cloning and expression in Saccharomyces cerevisiae of the NAD(P)H-dependent xylose reductase-encoding gene (XYL1) from the xylose-assimilating yeast Pichia stipitis","volume":"109","author":"Amore","year":"1991","journal-title":"Gene"},{"key":"ref_102","doi-asserted-by":"crossref","first-page":"493","DOI":"10.1007\/BF00327019","article-title":"Isolation and characterization of the Pichia stipitis xylitol dehydrogenase gene, XYL2, and construction of a xylose-utilizing Saccharomyces cerevisiae transformant","volume":"18","author":"Amore","year":"1990","journal-title":"Curr. Genet."},{"key":"ref_103","doi-asserted-by":"crossref","first-page":"7796","DOI":"10.1128\/AEM.01505-10","article-title":"Increased Ethanol Productivity in Xylose-Utilizing Saccharomyces cerevisiae via a Randomly Mutagenized Xylose Reductase","volume":"76","author":"Runquist","year":"2010","journal-title":"Appl. Environ. Microbiol."},{"key":"ref_104","doi-asserted-by":"crossref","first-page":"2304","DOI":"10.1128\/AEM.02522-08","article-title":"Functional Expression of a Bacterial Xylose Isomerase in Saccharomyces cerevisiae","volume":"75","author":"Brat","year":"2009","journal-title":"Appl. Environ. Microbiol."},{"key":"ref_105","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1186\/s13568-018-0670-8","article-title":"Systematic optimization of gene expression of pentose phosphate pathway enhances ethanol production from a glucose\/xylose mixed medium in a recombinant Saccharomyces cerevisiae","volume":"8","author":"Kobayashi","year":"2018","journal-title":"AMB Express"},{"key":"ref_106","doi-asserted-by":"crossref","first-page":"399","DOI":"10.1016\/j.femsyr.2004.09.010","article-title":"Metabolic engineering of a xylose-isomerase-expressing Saccharomyces cerevisiae strain for rapid anaerobic xylose fermentation","volume":"5","author":"Kuyper","year":"2005","journal-title":"FEMS Yeast Res."},{"key":"ref_107","doi-asserted-by":"crossref","first-page":"1165","DOI":"10.3389\/fmicb.2015.01165","article-title":"Heterologous xylose isomerase pathway and evolutionary engineering improve xylose utilization in Saccharomyces cerevisiae","volume":"6","author":"Qi","year":"2015","journal-title":"Front. Microbiol."},{"key":"ref_108","doi-asserted-by":"crossref","first-page":"611","DOI":"10.1016\/j.ymben.2012.07.011","article-title":"Xylose isomerase overexpression along with engineering of the pentose phosphate pathway and evolutionary engineering enable rapid xylose utilization and ethanol production by Saccharomyces cerevisiae","volume":"14","author":"Zhou","year":"2012","journal-title":"Metab. Eng."},{"key":"ref_109","doi-asserted-by":"crossref","first-page":"12","DOI":"10.1186\/s13068-019-1641-2","article-title":"Improved simultaneous co-fermentation of glucose and xylose by Saccharomyces cerevisiae for efficient lignocellulosic biorefinery","volume":"13","author":"Tran","year":"2020","journal-title":"Biotechnol. Biofuels"},{"key":"ref_110","doi-asserted-by":"crossref","first-page":"38","DOI":"10.1186\/1754-6834-4-38","article-title":"Improving L-arabinose utilization of pentose fermenting Saccharomyces cerevisiae cells by heterologous expression of L-arabinose transporting sugar transporters","volume":"4","author":"Subtil","year":"2011","journal-title":"Biotechnol. Biofuels"},{"key":"ref_111","doi-asserted-by":"crossref","first-page":"464","DOI":"10.3389\/fbioe.2019.00464","article-title":"Engineering of Pentose Transport in Saccharomyces cerevisiae for Biotechnological Applications","volume":"7","author":"Nijland","year":"2020","journal-title":"Front. Bioeng. Biotechnol."},{"key":"ref_112","doi-asserted-by":"crossref","first-page":"3311","DOI":"10.1128\/AEM.02651-10","article-title":"Functional Survey for Heterologous Sugar Transport Proteins, Using Saccharomyces cerevisiae as a Host","volume":"77","author":"Young","year":"2011","journal-title":"Appl. Environ. Microbiol."},{"key":"ref_113","doi-asserted-by":"crossref","first-page":"98","DOI":"10.1016\/j.ymben.2018.11.010","article-title":"Yeast chemogenomic screen identifies distinct metabolic pathways required to tolerate exposure to phenolic fermentation inhibitors ferulic acid, 4-hydroxybenzoic acid and coniferyl aldehyde","volume":"52","author":"Fletcher","year":"2019","journal-title":"Metab. Eng."},{"key":"ref_114","doi-asserted-by":"crossref","first-page":"56","DOI":"10.1016\/j.copbio.2019.01.006","article-title":"Harnessing xylose pathways for biofuels production","volume":"57","author":"Li","year":"2019","journal-title":"Curr. Opin. Biotechnol."},{"key":"ref_115","doi-asserted-by":"crossref","first-page":"39","DOI":"10.1016\/j.copbio.2017.10.002","article-title":"Engineering microbial fatty acid metabolism for biofuels and biochemicals","volume":"50","author":"Marella","year":"2018","journal-title":"Curr. Opin. Biotechnol."},{"key":"ref_116","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/j.ymben.2015.01.009","article-title":"Metabolic engineering strategies for microbial synthesis of oleochemicals","volume":"29","author":"Pfleger","year":"2015","journal-title":"Metab. Eng."},{"key":"ref_117","doi-asserted-by":"crossref","first-page":"627","DOI":"10.1016\/j.copbio.2011.01.002","article-title":"Pathway engineering for functional isoprenoids","volume":"22","author":"Misawa","year":"2011","journal-title":"Curr. Opin. Biotechnol."},{"key":"ref_118","doi-asserted-by":"crossref","first-page":"355","DOI":"10.1038\/nrmicro3240","article-title":"Semi-synthetic artemisinin: A model for the use of synthetic biology in pharmaceutical development","volume":"12","author":"Paddon","year":"2014","journal-title":"Nat. Rev. Microbiol."},{"key":"ref_119","doi-asserted-by":"crossref","first-page":"e1900173","DOI":"10.1002\/biot.201900173","article-title":"Redirection of the Glycolytic Flux Enhances Isoprenoid Production in Saccharomyces cerevisiae","volume":"15","author":"Kwak","year":"2019","journal-title":"Biotechnol. J."},{"key":"ref_120","doi-asserted-by":"crossref","first-page":"e2972","DOI":"10.1002\/btpr.2972","article-title":"Exploiting the NADPH pool for xylitol production using recombinant Saccharomyces cerevisiae","volume":"36","author":"Reshamwala","year":"2020","journal-title":"Biotechnol. Prog."},{"key":"ref_121","doi-asserted-by":"crossref","first-page":"346","DOI":"10.1021\/acssynbio.8b00388","article-title":"Metabolic Engineering of Saccharomyces cerevisiae for Production of Shinorine, a Sunscreen Material, from Xylose","volume":"8","author":"Park","year":"2019","journal-title":"ACS Synth. Biol."},{"key":"ref_122","doi-asserted-by":"crossref","first-page":"664","DOI":"10.1021\/acssynbio.7b00397","article-title":"Photosynthetic Production of Sunscreen Shinorine Using an Engineered Cyanobacterium","volume":"7","author":"Yang","year":"2018","journal-title":"ACS Synth. Biol."},{"key":"ref_123","doi-asserted-by":"crossref","first-page":"55","DOI":"10.1016\/j.ymben.2012.10.003","article-title":"Metabolic engineering of muconic acid production in Saccharomyces cerevisiae","volume":"15","author":"Curran","year":"2013","journal-title":"Metab. Eng."},{"key":"ref_124","doi-asserted-by":"crossref","first-page":"165","DOI":"10.1016\/j.ymben.2019.09.011","article-title":"Connecting central carbon and aromatic amino acid metabolisms to improve de novo 2-phenylethanol production in Saccharomyces cerevisiae","volume":"56","author":"Hassing","year":"2019","journal-title":"Metab. Eng."},{"key":"ref_125","doi-asserted-by":"crossref","first-page":"134","DOI":"10.1016\/j.ymben.2017.06.008","article-title":"Multilevel engineering of the upstream module of aromatic amino acid biosynthesis in Saccharomyces cerevisiae for high production of polymer and drug precursors","volume":"42","author":"Ng","year":"2017","journal-title":"Metab. Eng."},{"key":"ref_126","doi-asserted-by":"crossref","first-page":"2520","DOI":"10.1021\/acsomega.9b04046","article-title":"Erythritol: Another C4 Platform Chemical in Biomass Refinery","volume":"5","author":"Nakagawa","year":"2020","journal-title":"ACS Omega"},{"key":"ref_127","doi-asserted-by":"crossref","first-page":"793","DOI":"10.1111\/j.1567-1364.2009.00525.x","article-title":"Pichia stipitis genomics, transcriptomics, and gene clusters","volume":"9","author":"Jeffries","year":"2009","journal-title":"FEMS Yeast Res."},{"key":"ref_128","first-page":"fuaa069","article-title":"Pentose metabolism and conversion to biofuels and high-value chemicals in yeasts","volume":"10","author":"Ruchala","year":"2020","journal-title":"FEMS Microbiol. Rev."},{"key":"ref_129","doi-asserted-by":"crossref","first-page":"191","DOI":"10.2217\/fmb.12.133","article-title":"Pichia pastoris: Protein production host and model organism for biomedical research","volume":"8","author":"Gasser","year":"2013","journal-title":"Futur. Microbiol."},{"key":"ref_130","doi-asserted-by":"crossref","first-page":"5955","DOI":"10.1007\/s00253-016-7363-5","article-title":"Increasing pentose phosphate pathway flux enhances recombinant protein production in Pichia pastoris","volume":"100","author":"Nocon","year":"2016","journal-title":"Appl. Microbiol. Biotechnol."},{"key":"ref_131","doi-asserted-by":"crossref","first-page":"475","DOI":"10.1007\/s00253-019-10224-3","article-title":"Integration of comprehensive data and biotechnological tools for industrial applications of Kluyveromyces marxianus","volume":"104","author":"Nurcholis","year":"2019","journal-title":"Appl. Microbiol. Biotechnol."},{"key":"ref_132","doi-asserted-by":"crossref","first-page":"94","DOI":"10.3389\/fgene.2018.00094","article-title":"Ploidy Variation in Kluyveromyces marxianus Separates Dairy and Non-dairy Isolates","volume":"9","author":"Varela","year":"2018","journal-title":"Front. Genet."},{"key":"ref_133","doi-asserted-by":"crossref","first-page":"553","DOI":"10.1016\/j.biortech.2016.11.110","article-title":"Engineered Kluyveromyces marxianus for pyruvate production at elevated temperature with simultaneous consumption of xylose and glucose","volume":"224","author":"Zhang","year":"2017","journal-title":"Bioresour. Technol."},{"key":"ref_134","doi-asserted-by":"crossref","first-page":"9251","DOI":"10.1007\/s00253-019-10200-x","article-title":"Yarrowia lipolytica: More than an oleaginous workhorse","volume":"103","author":"Miller","year":"2019","journal-title":"Appl. Microbiol. Biotechnol."},{"key":"ref_135","doi-asserted-by":"crossref","first-page":"64","DOI":"10.1016\/S0140-6736(08)60073-2","article-title":"Glucose-6-phosphate dehydrogenase deficiency","volume":"371","author":"Cappellini","year":"2008","journal-title":"Lancet"},{"key":"ref_136","doi-asserted-by":"crossref","first-page":"365","DOI":"10.3389\/fendo.2020.00365","article-title":"The Role of the Pentose Phosphate Pathway in Diabetes and Cancer","volume":"11","author":"Ge","year":"2020","journal-title":"Front. Endocrinol."},{"key":"ref_137","doi-asserted-by":"crossref","first-page":"167","DOI":"10.1016\/j.ccell.2020.06.001","article-title":"Oxidative Stress in Cancer","volume":"38","author":"Hayes","year":"2020","journal-title":"Cancer Cell"},{"key":"ref_138","doi-asserted-by":"crossref","first-page":"2289","DOI":"10.1007\/s11033-020-05243-7","article-title":"d-ribose and pathogenesis of Alzheimer\u2019s disease","volume":"47","author":"Javed","year":"2020","journal-title":"Mol. Biol. Rep."},{"key":"ref_139","doi-asserted-by":"crossref","first-page":"14285","DOI":"10.1002\/jcb.29004","article-title":"Neuroprotection by glucose-6-phosphate dehydrogenase and the pentose phosphate pathway","volume":"120","author":"Tang","year":"2019","journal-title":"J. Cell. Biochem."},{"key":"ref_140","doi-asserted-by":"crossref","first-page":"703","DOI":"10.1007\/s10545-008-1015-6","article-title":"The biochemistry, metabolism and inherited defects of the pentose phosphate pathway: A review","volume":"31","author":"Wamelink","year":"2008","journal-title":"J. Inherit. Metab. Dis."},{"key":"ref_141","first-page":"1","article-title":"Differential Site-Based Expression of Pentose Phosphate Pathway-Related Proteins among Breast Cancer Metastases","volume":"2017","author":"Cha","year":"2017","journal-title":"Dis. Markers"},{"key":"ref_142","doi-asserted-by":"crossref","first-page":"103708","DOI":"10.1016\/j.ejmg.2019.103708","article-title":"Confirmation of a Rare Genetic Leukoencephalopathy due to a Novel Bi-allelic Variant in RPIA","volume":"62","author":"Kaur","year":"2019","journal-title":"Eur. J. Med. Genet."},{"key":"ref_143","doi-asserted-by":"crossref","first-page":"931","DOI":"10.1007\/s00109-010-0634-1","article-title":"The difference between rare and exceptionally rare: Molecular characterization of ribose 5-phosphate isomerase deficiency","volume":"88","author":"Wamelink","year":"2010","journal-title":"J. Mol. Med."},{"key":"ref_144","doi-asserted-by":"crossref","first-page":"1235","DOI":"10.1016\/j.ajhg.2016.03.030","article-title":"Mutations in TKT are the cause of a syndrome including short stature, developmental delay, and congenital heart defects","volume":"98","author":"Boyle","year":"2016","journal-title":"Am. J. Hum. Genet."},{"key":"ref_145","doi-asserted-by":"crossref","first-page":"139","DOI":"10.1177\/0036933013496944","article-title":"The effect of magnesium administration on erythrocyte transketolase activity in alcoholic patients treated with thiamine","volume":"58","author":"Peake","year":"2013","journal-title":"Scott. Med. J."},{"key":"ref_146","doi-asserted-by":"crossref","first-page":"1297","DOI":"10.1016\/S1357-2725(98)00095-8","article-title":"Properties and functions of the thiamin diphosphate dependent enzyme transketolase","volume":"30","author":"Schenk","year":"1998","journal-title":"Int. J. Biochem. Cell Biol."},{"key":"ref_147","doi-asserted-by":"crossref","unstructured":"Lafc\u0131, N.G., Colak, F.K., Sahin, G., Sakar, M., \u00c7etinkaya, S., and Savas-Erdeve, S. (2020). Hypergonadotrophic hypogonadism in a patient with transaldolase deficiency: Novel mutation in the pentose phosphate pathway. Hormones, 1\u20135.","DOI":"10.1007\/s42000-020-00252-4"},{"key":"ref_148","doi-asserted-by":"crossref","first-page":"496","DOI":"10.1002\/jimd.12197","article-title":"Transaldolase haploinsufficiency in subjects with acetaminophen-induced liver failure","volume":"43","author":"Oaks","year":"2020","journal-title":"J. Inherit. Metab. Dis."},{"key":"ref_149","doi-asserted-by":"crossref","first-page":"1482","DOI":"10.1016\/j.biocel.2009.02.001","article-title":"Transaldolase: From biochemistry to human disease","volume":"41","author":"Samland","year":"2009","journal-title":"Int. J. Biochem. Cell Biol."},{"key":"ref_150","doi-asserted-by":"crossref","first-page":"147","DOI":"10.1002\/jimd.12036","article-title":"Clinical, biochemical, and molecular overview of transaldolase deficiency and evaluation of the endocrine function: Update of 34 patients","volume":"42","author":"Williams","year":"2019","journal-title":"J. Inherit. Metab. Dis."},{"key":"ref_151","doi-asserted-by":"crossref","first-page":"347","DOI":"10.1016\/j.tibs.2014.06.005","article-title":"The pentose phosphate pathway and cancer","volume":"39","author":"Patra","year":"2014","journal-title":"Trends Biochem. Sci."},{"key":"ref_152","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1186\/s12974-019-1659-1","article-title":"The pentose phosphate pathway regulates chronic neuroinflammation and dopaminergic neurodegeneration","volume":"16","author":"Tu","year":"2019","journal-title":"J. Neuroinflammation"},{"key":"ref_153","doi-asserted-by":"crossref","first-page":"2000205","DOI":"10.1002\/bies.202000205","article-title":"Why do cancer cells break from host circadian rhythm? Insights from unicellular organisms","volume":"43","author":"Alamoudi","year":"2021","journal-title":"BioEssays"},{"key":"ref_154","doi-asserted-by":"crossref","first-page":"462","DOI":"10.1016\/j.cmet.2016.07.024","article-title":"The Pentose Phosphate Pathway Regulates the Circadian Clock","volume":"24","author":"Rey","year":"2016","journal-title":"Cell Metab."},{"key":"ref_155","doi-asserted-by":"crossref","first-page":"1047","DOI":"10.1080\/10715762.2016.1223296","article-title":"What has passed is prolog: New cellular and physiological roles of G6PD","volume":"50","author":"Yang","year":"2016","journal-title":"Free. Radic. Res."},{"key":"ref_156","unstructured":"Aziz, H., and Mohiuddin, S.S. (2021). Biochemistry, Hexose Monophosphate Pathway, StatPearls."},{"key":"ref_157","doi-asserted-by":"crossref","first-page":"115","DOI":"10.1038\/s41586-019-1847-2","article-title":"Metabolic heterogeneity confers differences in melanoma metastatic potential","volume":"577","author":"Tasdogan","year":"2020","journal-title":"Nature"},{"key":"ref_158","doi-asserted-by":"crossref","first-page":"124","DOI":"10.1016\/j.bcmd.2003.11.001","article-title":"A novel mutation in the glucose-6-phosphate dehydrogenase gene in a subject with chronic nonspherocytic hemolytic anemia\u2014Characterization of enzyme using yeast expression system and molecular modeling","volume":"32","author":"Grabowska","year":"2004","journal-title":"Blood Cells Mol. Dis."},{"key":"ref_159","doi-asserted-by":"crossref","first-page":"723","DOI":"10.1016\/j.jmgm.2008.11.005","article-title":"Homology modeling of human Transketolase: Description of critical sites useful for drug design and study of the cofactor binding mode","volume":"27","year":"2009","journal-title":"J. Mol. Graph. Model."},{"key":"ref_160","first-page":"131","article-title":"Functional expression of human mutant phosphofructokinase in yeast: Genetic defects in French Canadian and Swiss patients with phosphofructokinase deficiency","volume":"56","author":"Raben","year":"1995","journal-title":"Am. J. Hum. Genet."},{"key":"ref_161","doi-asserted-by":"crossref","first-page":"333","DOI":"10.1111\/j.1567-1364.2009.00604.x","article-title":"A tool kit for molecular genetics of Kluyveromyces lactis comprising a congenic strain series and a set of versatile vectors","volume":"10","author":"Heinisch","year":"2010","journal-title":"FEMS Yeast Res."}],"container-title":["Biomolecules"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/2218-273X\/11\/5\/725\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,10,11]],"date-time":"2025-10-11T05:59:39Z","timestamp":1760162379000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/2218-273X\/11\/5\/725"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2021,5,12]]},"references-count":161,"journal-issue":{"issue":"5","published-online":{"date-parts":[[2021,5]]}},"alternative-id":["biom11050725"],"URL":"https:\/\/doi.org\/10.3390\/biom11050725","relation":{},"ISSN":["2218-273X"],"issn-type":[{"value":"2218-273X","type":"electronic"}],"subject":[],"published":{"date-parts":[[2021,5,12]]}}}