Engineering the glycolytic pathway: A potential approach for improvement of biocatalyst performance

References

• Borodina I, Nielsen J. Advances in metabolic engineering of yeast Saccharomyces cerevisiae for production of chemicals. Biotechnol J 2014; 9:609-20; PMID:24677744; http://dx.doi.org/10.1002/biot.201300445
   PubMed Web of Science ®Google Scholar
• Otte KB, Hauer B. Enzyme engineering in the context of novel pathways and products. Curr Opin Biotechnol 2015; 35C:16-22; http://dx.doi.org/10.1016/j.copbio.2014.12.011
   Web of Science ®Google Scholar
• Uhlenbusch I, Sahm H, Sprenger GA. Expression of an L-alanine dehydrogenase gene in Zymomonas mobilis and excretion of L-alanine. Appl Environ Microbiol 1991; 57:1360-6; PMID:1854197
   PubMed Web of Science ®Google Scholar
• Colón GE, Nguyen TT, Jetten MSM, Sinskey AJ, Stephanopoulos G. Production of isoleucine by overexpression of ilvA in a Corynebacterium lactofermentum threonine producer. Appl Microbiol Biotechnol 1995; 43:482-8; http://dx.doi.org/10.1007/BF00218453
   PubMed Web of Science ®Google Scholar
• Platteeuw C, Hugenholtz J, Starrenburg M, van Alen-Boerrigter I, de Vos WM. Metabolic engineering of Lactococcus lactis: influence of the overproduction of α-acetolactate synthase in strains deficient in lactate dehydrogenase as a function of culture conditions. Appl Environ Microbiol 1995; 61:3967-71; PMID:8526510
   PubMed Web of Science ®Google Scholar
• Bakker BM, Michels PAM, Opperdoes FR, Westerhoff HV. What controls glycolysis in bloodstream form Trypanosoma brucei? J Biol Chem 1999; 274:14551-9; PMID:10329645; http://dx.doi.org/10.1074/jbc.274.21.14551
   PubMed Web of Science ®Google Scholar
• Hauf J, Zimmermann FK, Müller S. Simultaneous genomic overexpression of seven glycolytic enzymes in the yeast Saccharomyces cerevisiae. Enzyme Microb Technol 2000; 26:688-98; PMID:10862874; http://dx.doi.org/10.1016/S0141-0229(00)00160-5
   PubMed Web of Science ®Google Scholar
• Snoep JL, Yomano LP, Westerhoff HV, Ingram LO. Protein burden in Zymomonas mobilis: negative flux and growth control due to overproduction of glycolytic enzymes. Microbiology 1995; 141:2329-37; http://dx.doi.org/10.1099/13500872-141-9-2329
   Web of Science ®Google Scholar
• Peter Smits H, Hauf J, Müller S, Hobley TJ, Zimmermann FK, Hahn-Hägerdal B, Nielsen J, Olsson L. Simultaneous overexpression of enzymes of the lower part of glycolysis can enhance the fermentative capacity of Saccharomyces cerevisiae. Yeast 2000; 16:1325-34; PMID:11015729; http://dx.doi.org/10.1002/1097-0061(200010)16:14<1325::AID-YEA627>3.0.CO;2-E
   PubMed Web of Science ®Google Scholar
• Schaaff I, Heinisch J, Zimmermann FK. Overproduction of glycolytic enzymes in yeast. Yeast 1989; 5:285-90; PMID:2528863; http://dx.doi.org/10.1002/yea.320050408
   PubMed Web of Science ®Google Scholar
• Ikeda M, Takeno S. Amino acid production by Corynebacterium glutamicum. In: Yukawa H, Inui M, eds. Corynebacterium glutamicum: Springer Berlin Heidelberg, 2013:107-47
   Google Scholar
• Inui M, Murakami S, Okino S, Kawaguchi H, Vertès AA, Yukawa H. Metabolic analysis of Corynebacterium glutamicum during lactate and succinate productions under oxygen deprivation conditions. J Mol Microbiol Biotechnol 2004; 7:182-96; PMID:15383716; http://dx.doi.org/10.1159/000079827
   PubMed Web of Science ®Google Scholar
• Okino S, Inui M, Yukawa H. Production of organic acids by Corynebacterium glutamicum under oxygen deprivation. Appl Microbiol Biotechnol 2005; 68:475-80; PMID:15672268; http://dx.doi.org/10.1007/s00253-005-1900-y
   PubMed Web of Science ®Google Scholar
• Okino S, Suda M, Fujikura K, Inui M, Yukawa H. Production of D-lactic acid by Corynebacterium glutamicum under oxygen deprivation. Appl Microbiol Biotechnol 2008; 78:449-54; PMID:18188553; http://dx.doi.org/10.1007/s00253-007-1336-7
   PubMed Web of Science ®Google Scholar
• Okino S, Noburyu R, Suda M, Jojima T, Inui M, Yukawa H. An efficient succinic acid production process in a metabolically engineered Corynebacterium glutamicum strain. Appl Microbiol Biotechnol 2008; 81:459-64; PMID:18777022; http://dx.doi.org/10.1007/s00253-008-1668-y
   PubMed Web of Science ®Google Scholar
• Jojima T, Fujii M, Mori E, Inui M, Yukawa H. Engineering of sugar metabolism of Corynebacterium glutamicum for production of amino acid L-alanine under oxygen deprivation. Appl Microbiol Biotechnol 2010; 87:159-65; PMID:20217078; http://dx.doi.org/10.1007/s00253-010-2493-7
   PubMed Web of Science ®Google Scholar
• Yamamoto S, Gunji W, Suzuki H, Toda H, Suda M, Jojima T, Inui M, Yukawa H. Overexpression of genes encoding glycolytic enzymes in Corynebacterium glutamicum enhances glucose metabolism and alanine production under oxygen deprivation conditions. Appl Environ Microbiol 2012; 78:4447-57; PMID:22504802; http://dx.doi.org/10.1128/AEM.07998-11
   PubMed Web of Science ®Google Scholar
• Hasegawa S, Uematsu K, Natsuma Y, Suda M, Hiraga K, Jojima T, Inui M, Yukawa H. Improvement of the redox balance increases L-valine production by Corynebacterium glutamicum under oxygen deprivation. Appl Environ Microbiol 2012; 78:865-75; PMID:22138982; http://dx.doi.org/10.1128/AEM.07056-11
   PubMed Web of Science ®Google Scholar
• Hasegawa S, Suda M, Uematsu K, Natsuma Y, Hiraga K, Jojima T, Inui M, Yukawa H. Engineering of Corynebacterium glutamicum for high-yield L-valine production under oxygen deprivation conditions. Appl Environ Microbiol 2013; 79:1250-7; PMID:23241971; http://dx.doi.org/10.1128/AEM.02806-12
   PubMed Web of Science ®Google Scholar
• Inui M, Kawaguchi H, Murakami S, Vertès AA, Yukawa H. Metabolic engineering of Corynebacterium glutamicum for fuel ethanol production under oxygen-deprivation conditions. J Mol Microbiol Biotechnol 2004; 8:243-54; PMID:16179801; http://dx.doi.org/10.1159/000086705
   PubMed Web of Science ®Google Scholar
• Jojima T, Noburyu R, Sasaki M, Tajima T, Suda M, Yukawa H, Inui M. Metabolic engineering for improved production of ethanol by Corynebacterium glutamicum. Appl Microbiol Biotechnol 2015; 99:1165-72; PMID:25421564; http://dx.doi.org/10.1007/s00253-014-6223-4
   PubMed Web of Science ®Google Scholar
• Yamamoto S, Suda M, Niimi S, Inui M, Yukawa H. Strain optimization for efficient isobutanol production using Corynebacterium glutamicum under oxygen deprivation. Biotechnol Bioeng 2013; 110:2938-48; PMID:23737329; http://dx.doi.org/10.1002/bit.24961
   PubMed Web of Science ®Google Scholar
• Jojima T, Inui M, Yukawa H. Biorefinery applications of Corynebacterium glutamicum. In: Yukawa H, Inui M, eds. Corynebacterium glutamicum: Springer Berlin Heidelberg, 2013:149-72
   Google Scholar
• Tsuge Y, Yamamoto S, Suda M, Inui M, Yukawa H. Reactions upstream of glycerate-1,3-bisphosphate drive Corynebacterium glutamicum D-lactate productivity under oxygen deprivation. Appl Microbiol Biotechnol 2013; 97:6693-703; PMID:23712891; http://dx.doi.org/10.1007/s00253-013-4986-7
   PubMed Web of Science ®Google Scholar
• Tsuge Y, Yamamoto S, Kato N, Suda M, Vertès AA, Yukawa H, Inui M. Overexpression of the phosphofructokinase encoding gene is crucial for achieving high production of D-lactate in Corynebacterium glutamicum under oxygen deprivation. Appl Microbiol Biotechnol 2015; 99:4679-89; PMID:25820644; http://dx.doi.org/10.1007/s00253-015-6546-9
   PubMed Web of Science ®Google Scholar
• Dominguez H, Nezondet C, Lindley ND, Cocaign M. Modified carbon flux during oxygen limited growth of Corynebacterium glutamicum and the consequences for amino acid overproduction. Biotech Lett 1993; 15:449-54; http://dx.doi.org/10.1007/BF00129316
   Web of Science ®Google Scholar
• Jojima T, Igari T, Gunji W, Suda M, Inui M, Yukawa H. Identification of a HAD superfamily phosphatase, HdpA, involved in 1,3-dihydroxyacetone production during sugar catabolism in Corynebacterium glutamicum. FEBS lett 2012; 586:4228-32; PMID:23108048; http://dx.doi.org/10.1016/j.febslet.2012.10.028
   PubMed Web of Science ®Google Scholar
• Jojima T, Igari T, Moteki Y, Suda M, Yukawa H, Inui M. Promiscuous activity of (S,S)-butanediol dehydrogenase is responsible for glycerol production from 1,3-dihydroxyacetone in Corynebacterium glutamicum under oxygen-deprived conditions. Appl Microbiol Biotechnol 2015; 99:1427-33; PMID:25363556; http://dx.doi.org/10.1007/s00253-014-6170-0
   PubMed Web of Science ®Google Scholar
• Papagianni M, Avramidis N. Lactococcus lactis as a cell factory: a twofold increase in phosphofructokinase activity results in a proportional increase in specific rates of glucose uptake and lactate formation. Enzyme Microb Technol 2011; 49:197-202; PMID:22112409; http://dx.doi.org/10.1016/j.enzmictec.2011.05.002
   PubMed Web of Science ®Google Scholar
• Koebmann B, Solem C, Jensen PR. Control analysis as a tool to understand the formation of the las operon in Lactococcus lactis. FEBS J 2005; 272:2292-303; PMID:15853813; http://dx.doi.org/10.1111/j.1742-4658.2005.04656.x
   PubMed Web of Science ®Google Scholar
• Emmerling M, Bailey JE, Sauer U. Altered regulation of pyruvate kinase or co-overexpression of phosphofructokinase increases glycolytic fluxes in resting Escherichia coli. Biotechnol Bioeng 2000; 67:623-7; PMID:10649237; http://dx.doi.org/10.1002/(SICI)1097-0290(20000305)67:5<623::AID-BIT13>3.0.CO;2-W
   PubMed Web of Science ®Google Scholar
• Davies SE, Brindle KM. Effects of overexpression of phosphofructokinase on glycolysis in the yeast Saccharomyces cerevisiae. Biochemistry 1992; 31:4729-35; PMID:1533788; http://dx.doi.org/10.1021/bi00134a028
   PubMed Web of Science ®Google Scholar
• Rogers PL, Lee KJ, Skotnicki ML, Tribe DE. Ethanol production by Zymomonas mobilis. Microbial Reactions: Springer Berlin Heidelberg, 1982:37-84
   Google Scholar
• Snoep JL, Arfman N, Yomano LP, Westerhoff HV, Conway T, Ingram LO. Control of glycolytic flux in Zymomonas mobilis by glucose 6-phosphate dehydrogenase activity. Biotechnol Bioeng 1996; 51:190-7; PMID: 18624328; http://dx.doi.org/10.1002/(SICI)1097-0290(19960720)51:2<190::AID-BIT8>3.0.CO;2-E
   PubMed Web of Science ®Google Scholar
• Huerta-Beristain G, Utrilla J, Hernández-Chávez G, Bolívar F, Gosset G, Martinez A. Specific ethanol production rate in ethanologenic Escherichia coli strain KO11 is limited by pyruvate decarboxylase. J Mol Microbiol Biotechnol 2008; 15:55-64; PMID: 18349551; http://dx.doi.org/10.1159/000111993
   PubMed Web of Science ®Google Scholar
• Solem C, Koebmann BJ, Jensen PR. Glyceraldehyde-3-phosphate dehydrogenase has no control over glycolytic flux in Lactococcus lactis MG1363. J Bacteriol 2003; 185:1564-71; PMID:12591873; http://dx.doi.org/10.1128/JB.185.5.1564-1571.2003
   PubMed Web of Science ®Google Scholar
• Koebmann B, Solem C, Jensen PR. Control analysis of the importance of phosphoglycerate enolase for metabolic fluxes in Lactococcus lactis subsp. lactis IL1403. Syst Biol (Stevenage) 2006; 153:346-9; PMID:16986314; http://dx.doi.org/10.1049/ip-syb:20060022
   PubMedGoogle Scholar
• Solem C, Koebmann B, Jensen PR. Control analysis of the role of triosephosphate isomerase in glucose metabolism in Lactococcus lactis. IET Syst Biol 2008; 2:64-72; PMID:18397117; http://dx.doi.org/10.1049/iet-syb:20070002
   PubMed Web of Science ®Google Scholar
• Solem C, Petranovic D, Koebmann B, Mijakovic I, Jensen PR. Phosphoglycerate mutase is a highly efficient enzyme without flux control in Lactococcus lactis. J Mol Microbiol Biotechnol 2010; 18:174-80; PMID:20530968; http://dx.doi.org/10.1159/000315458
   PubMed Web of Science ®Google Scholar
• Litsanov B, Brocker M, Bott M. Toward homosuccinate fermentation: metabolic engineering of Corynebacterium glutamicum for anaerobic production of succinate from glucose and formate. Appl Environ Microbiol 2012; 78:3325-37; PMID:22389371; http://dx.doi.org/10.1128/AEM.07790-11
   PubMed Web of Science ®Google Scholar
• Andersen HW, Solem C, Hammer K, Jensen PR. Twofold reduction of phosphofructokinase activity in Lactococcus lactis results in strong decreases in growth rate and in glycolytic flux. J Bacteriol 2001; 183:3458-67; PMID:11344154; http://dx.doi.org/10.1128/JB.183.11.3458-3467.2001
   PubMed Web of Science ®Google Scholar
• Smallbone K, Messiha HL, Carroll KM, Winder CL, Malys N, Dunn WB, Murabito E, Swainston N, Dada JO, Khan F, et al. A model of yeast glycolysis based on a consistent kinetic characterisation of all its enzymes. FEBS lett 2013; 587:2832-41; PMID:23831062; http://dx.doi.org/10.1016/j.febslet.2013.06.043
   PubMed Web of Science ®Google Scholar
• Bro C, Knudsen S, Regenberg B, Olsson L, Nielsen J. Improvement of galactose uptake in Saccharomyces cerevisiae through overexpression of phosphoglucomutase: example of transcript analysis as a tool in inverse metabolic engineering. Appl Environ Microbiol 2005; 71:6465-72; PMID:16269670; http://dx.doi.org/10.1128/AEM.71.11.6465-6472.2005
   PubMed Web of Science ®Google Scholar
• Koebmann BJ, Westerhoff HV, Snoep JL, Nilsson D, Jensen PR. The glycolytic flux in Escherichia coli is controlled by the demand for ATP. J Bacteriol 2002; 184:3909-16; PMID:12081962; http://dx.doi.org/10.1128/JB.184.14.3909-3916.2002
   PubMed Web of Science ®Google Scholar
• Nielsen DR, Leonard E, Yoon SH, Tseng HC, Yuan C, Prather KL. Engineering alternative butanol production platforms in heterologous bacteria. Metab Eng 2009; 11:262-73; PMID:19464384; http://dx.doi.org/10.1016/j.ymben.2009.05.003
   PubMed Web of Science ®Google Scholar
• Takeno S, Murata R, Kobayashi R, Mitsuhashi S, Ikeda M. Engineering of Corynebacterium glutamicum with an NADPH-generating glycolytic pathway for L-lysine production. Appl Environ Microbiol 2010; 76:7154-60; PMID:20851994; http://dx.doi.org/10.1128/AEM.01464-10
   PubMed Web of Science ®Google Scholar
• Komati Reddy G, Lindner SN, Wendisch VF. Metabolic engineering of an ATP-neutral Embden-Meyerhof-Parnas pathway in Corynebacterium glutamicum: growth restoration by an adaptive point mutation in NADH dehydrogenase. Appl Environ Microbiol 2015; 81:1996-2005; PMID:25576602; http://dx.doi.org/10.1128/AEM.03116-14
   PubMed Web of Science ®Google Scholar
• Benisch F, Boles E. The bacterial Entner-Doudoroff pathway does not replace glycolysis in Saccharomyces cerevisiae due to the lack of activity of iron-sulfur cluster enzyme 6-phosphogluconate dehydratase. J Biotechnol 2014; 171:45-55; PMID:24333129; http://dx.doi.org/10.1016/j.jbiotec.2013.11.025
   PubMed Web of Science ®Google Scholar
• Abengoa. Press release. 2014:http://static.abengoabiotech.com/wp-content/uploads/2014/09/Abengoa-Hugoton-plant-grand-opening-press-release_final_10.17.14.pdf
   Google Scholar