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Volumn 13, Issue 1, 2014, Pages

Engineering of serine-deamination pathway, entner-doudoroff pathway and yruvate dehydrogenase complex to improve poly(3-hydroxybutyrate) production in Escherichia coli

Author keywords

Entner Doudoroff pathway; Escherichia coli; L serine deaminate; poly(3 hydroxybutyrate); Pyruvate dehydrogenase complex

Indexed keywords

POLY(3 HYDROXYBUTYRIC ACID); PYRUVATE DEHYDROGENASE; SERINE; BACTERIAL PROTEIN; HYDROXYBUTYRIC ACID; PHOSPHOGLYCERATE KINASE; POLY-BETA-HYDROXYBUTYRATE; POLYESTER; PYRUVATE DEHYDROGENASE COMPLEX; SERINE DEHYDRATASE;

EID: 84924038713     PISSN: None     EISSN: 14752859     Source Type: Journal    
DOI: 10.1186/s12934-014-0172-6     Document Type: Article
Times cited : (35)

References (42)
  • 1
    • 82755198036 scopus 로고    scopus 로고
    • Polyhydroxyalkanoates as a source of chemicals, polymers, and biofuels
    • Gao X, Chen JC, Wu Q, Chen GQ: Polyhydroxyalkanoates as a source of chemicals, polymers, and biofuels. Curr Opin Biotechnol 2011, 22:768-774.
    • (2011) Curr Opin Biotechnol , vol.22 , pp. 768-774
    • Gao, X.1    Chen, J.C.2    Wu, Q.3    Chen, G.Q.4
  • 2
    • 0039109649 scopus 로고    scopus 로고
    • High-level production of poly(3-hydroxybutyrate-co-3-hydroxyvalerate) by fed-batch culture of recombinant Escherichia coli
    • Choi JI, Lee SY: High-level production of poly(3-hydroxybutyrate-co-3-hydroxyvalerate) by fed-batch culture of recombinant Escherichia coli. Appl Environ Microbiol 1999, 65:4363-4368.
    • (1999) Appl Environ Microbiol , vol.65 , pp. 4363-4368
    • Choi, J.I.1    Lee, S.Y.2
  • 3
    • 0344026322 scopus 로고    scopus 로고
    • Efficient and economical recovery of poly(3-hydroxybutyrate) from recombinant Escherichia coli by simple digestion with chemicals
    • Choi J, Lee SY: Efficient and economical recovery of poly(3-hydroxybutyrate) from recombinant Escherichia coli by simple digestion with chemicals. Biotechnol Bioeng 1999, 62:546-553.
    • (1999) Biotechnol Bioeng , vol.62 , pp. 546-553
    • Choi, J.1    Lee, S.Y.2
  • 5
    • 0141429051 scopus 로고    scopus 로고
    • Gene expression patterns for metabolic pathway in pgi knockout Escherichia coli with and without phb genes based on RT-PCR
    • Kabir MM, Shimizu K: Gene expression patterns for metabolic pathway in pgi knockout Escherichia coli with and without phb genes based on RT-PCR. J Biotechnol 2003, 105:11-31.
    • (2003) J Biotechnol , vol.105 , pp. 11-31
    • Kabir, M.M.1    Shimizu, K.2
  • 6
    • 6944250125 scopus 로고    scopus 로고
    • Role of tktA gene in pentose phosphate pathway on odd-ball biosynthesis of poly-beta-hydroxybutyrate in transformant Escherichia coli harboring phbCAB operon
    • Jung YM, Lee JN, Shin HD, Lee YH: Role of tkt A gene in pentose phosphate pathway on odd-ball biosynthesis of poly-beta-hydroxybutyrate in transformant Escherichia coli harboring phbCAB operon. J Biosci Bioeng 2004, 98:224-227.
    • (2004) J Biosci Bioeng , vol.98 , pp. 224-227
    • Jung, Y.M.1    Lee, J.N.2    Shin, H.D.3    Lee, Y.H.4
  • 7
    • 33749835786 scopus 로고    scopus 로고
    • Modulation of talA gene in pentose phosphate pathway for overproduction of poly-beta-hydroxybutyrate in transformant Escherichia coli harboring phbCAB operon
    • Song BG, Kim TK, Jung YM, Lee YH: Modulation of talA gene in pentose phosphate pathway for overproduction of poly-beta-hydroxybutyrate in transformant Escherichia coli harboring phbCAB operon. J Biosci Bioeng 2006, 102:237-240.
    • (2006) J Biosci Bioeng , vol.102 , pp. 237-240
    • Song, B.G.1    Kim, T.K.2    Jung, Y.M.3    Lee, Y.H.4
  • 8
    • 0036305048 scopus 로고    scopus 로고
    • Amplification of the NADPH-related genes zwf and gnd for the oddball biosynthesis of PHB in an E. coli transformant harboring a cloned phbCAB operon
    • Lim SJ, Jung YM, Shin HD, Lee YH: Amplification of the NADPH-related genes zwf and gnd for the oddball biosynthesis of PHB in an E. coli transformant harboring a cloned phbCAB operon. J Biosci Bioeng 2002, 93:543-549.
    • (2002) J Biosci Bioeng , vol.93 , pp. 543-549
    • Lim, S.J.1    Jung, Y.M.2    Shin, H.D.3    Lee, Y.H.4
  • 9
    • 84896489949 scopus 로고    scopus 로고
    • Improving poly-3-hydroxybutyrate production in Escherichia coli by combining the increase in the NADPH pool and acetyl-CoA availability
    • Centeno-Leija S, Huerta-Beristain G, Giles-Gomez M, Bolivar F, Gosset G, Martinez A: Improving poly-3-hydroxybutyrate production in Escherichia coli by combining the increase in the NADPH pool and acetyl-CoA availability. Antonie Van Leeuwenhoek 2014, 105:687-696.
    • (2014) Antonie Van Leeuwenhoek , vol.105 , pp. 687-696
    • Centeno-Leija, S.1    Huerta-Beristain, G.2    Giles-Gomez, M.3    Bolivar, F.4    Gosset, G.5    Martinez, A.6
  • 10
    • 0027291428 scopus 로고
    • Phosphoenolpyruvate:carbohydrate phosphotransferase systems of bacteria
    • Postma PW, Lengeler JW, Jacobson GR: Phosphoenolpyruvate:carbohydrate phosphotransferase systems of bacteria. Microbiol Rev 1993, 57:543-594.
    • (1993) Microbiol Rev , vol.57 , pp. 543-594
    • Postma, P.W.1    Lengeler, J.W.2    Jacobson, G.R.3
  • 11
    • 0035191291 scopus 로고    scopus 로고
    • Proteome analysis of metabolically engineered Escherichia coli producing Poly(3-hydroxybutyrate)
    • Han MJ, Yoon SS, Lee SY: Proteome analysis of metabolically engineered Escherichia coli producing Poly(3-hydroxybutyrate). J Bacteriol 2001, 183:301-308.
    • (2001) J Bacteriol , vol.183 , pp. 301-308
    • Han, M.J.1    Yoon, S.S.2    Lee, S.Y.3
  • 12
    • 0042932494 scopus 로고    scopus 로고
    • In silico prediction and validation of the importance of the Entner-Doudoroff pathway in poly(3-hydroxybutyrate) production by metabolically engineered Escherichia coli
    • Hong SH, Park SJ, Moon SY, Park JP, Lee SY: In silico prediction and validation of the importance of the Entner-Doudoroff pathway in poly(3-hydroxybutyrate) production by metabolically engineered Escherichia coli. Biotechnol Bioeng 2003, 83:854-863.
    • (2003) Biotechnol Bioeng , vol.83 , pp. 854-863
    • Hong, S.H.1    Park, S.J.2    Moon, S.Y.3    Park, J.P.4    Lee, S.Y.5
  • 13
    • 0024730743 scopus 로고
    • L-serine degradation in Escherichia coli K-12: cloning and sequencing of the sdaA gene
    • Su HS, Lang BF, Newman EB: L-serine degradation in Escherichia coli K-12: cloning and sequencing of the sdaA gene. J Bacteriol 1989, 171:5095-5102.
    • (1989) J Bacteriol , vol.171 , pp. 5095-5102
    • Su, H.S.1    Lang, B.F.2    Newman, E.B.3
  • 14
    • 47749129257 scopus 로고    scopus 로고
    • Deficiency in L-serine deaminase results in abnormal growth and cell division of Escherichia coli K-12
    • Zhang X, Newman E: Deficiency in L-serine deaminase results in abnormal growth and cell division of Escherichia coli K-12. Mol Microbiol 2008, 69:870-881.
    • (2008) Mol Microbiol , vol.69 , pp. 870-881
    • Zhang, X.1    Newman, E.2
  • 15
    • 0028177225 scopus 로고
    • The pdhR-aceEF-lpd operon of Escherichia coli expresses the pyruvate dehydrogenase complex
    • Quail MA, Haydon DJ, Guest JR: The pdhR-aceEF-lpd operon of Escherichia coli expresses the pyruvate dehydrogenase complex. Mol Microbiol 1994, 12:95-104.
    • (1994) Mol Microbiol , vol.12 , pp. 95-104
    • Quail, M.A.1    Haydon, D.J.2    Guest, J.R.3
  • 16
    • 0016294957 scopus 로고
    • Pyruvate formate-lyase of Escherichia coli: the acetyl-enzyme intermediate
    • Knappe J, Blaschkowski HP, Grobner P, Schmitt T: Pyruvate formate-lyase of Escherichia coli: the acetyl-enzyme intermediate. Eur J Biochem 1974, 50:253-263.
    • (1974) Eur J Biochem , vol.50 , pp. 253-263
    • Knappe, J.1    Blaschkowski, H.P.2    Grobner, P.3    Schmitt, T.4
  • 17
    • 10444221880 scopus 로고    scopus 로고
    • Cometabolism of a nongrowth substrate: L-serine utilization by Corynebacterium glutamicum
    • Netzer R, Peters-Wendisch P, Eggeling L, Sahm H: Cometabolism of a nongrowth substrate: L-serine utilization by Corynebacterium glutamicum. Appl Environ Microbiol 2004, 70:7148-7155.
    • (2004) Appl Environ Microbiol , vol.70 , pp. 7148-7155
    • Netzer, R.1    Peters-Wendisch, P.2    Eggeling, L.3    Sahm, H.4
  • 18
    • 0037213337 scopus 로고    scopus 로고
    • 3-Phosphoglycerate dehydrogenase from Corynebacterium glutamicum: the C-terminal domain is not essential for activity but is required for inhibition by L-serine
    • Peters-Wendisch P, Netzer R, Eggeling L, Sahm H: 3-Phosphoglycerate dehydrogenase from Corynebacterium glutamicum: the C-terminal domain is not essential for activity but is required for inhibition by L-serine. Appl Microbiol Biotechnol 2002, 60:437-441.
    • (2002) Appl Microbiol Biotechnol , vol.60 , pp. 437-441
    • Peters-Wendisch, P.1    Netzer, R.2    Eggeling, L.3    Sahm, H.4
  • 20
    • 0041731698 scopus 로고    scopus 로고
    • Role of proline residues in the folding of serine hydroxymethyltransferase
    • Fu TF, Boja ES, Safo MK, Schirch V: Role of proline residues in the folding of serine hydroxymethyltransferase. J Biol Chem 2003, 278:31088-31094.
    • (2003) J Biol Chem , vol.278 , pp. 31088-31094
    • Fu, T.F.1    Boja, E.S.2    Safo, M.K.3    Schirch, V.4
  • 21
    • 0015965111 scopus 로고
    • Control of serine transhydroxymethylase synthesis in Escherichia coli K12
    • Miller BA, Newman EB: Control of serine transhydroxymethylase synthesis in Escherichia coli K12. Can J Microbiol 1974, 20:41-47.
    • (1974) Can J Microbiol , vol.20 , pp. 41-47
    • Miller, B.A.1    Newman, E.B.2
  • 22
    • 4244126317 scopus 로고
    • The Relation of Serine-Glycine Metabolism to the Formation of Single-Carbon Units
    • Newman EB, Magasanik B: The Relation of Serine-Glycine Metabolism to the Formation of Single-Carbon Units. Biochim Biophys Acta 1963, 78:437-448.
    • (1963) Biochim Biophys Acta , vol.78 , pp. 437-448
    • Newman, E.B.1    Magasanik, B.2
  • 23
    • 84860728385 scopus 로고    scopus 로고
    • Metabolic engineering and flux analysis of Corynebacterium glutamicum for L-serine production
    • Lai S, Zhang Y, Liu S, Liang Y, Shang X, Chai X, Wen T: Metabolic engineering and flux analysis of Corynebacterium glutamicum for L-serine production. Sci China Life Sci 2012, 55:283-290.
    • (2012) Sci China Life Sci , vol.55 , pp. 283-290
    • Lai, S.1    Zhang, Y.2    Liu, S.3    Liang, Y.4    Shang, X.5    Chai, X.6    Wen, T.7
  • 24
    • 2342653439 scopus 로고    scopus 로고
    • Plasmid copy number and plasmid stability
    • Friehs K: Plasmid copy number and plasmid stability. Adv Biochem Eng Biotechnol 2004, 86:47-82.
    • (2004) Adv Biochem Eng Biotechnol , vol.86 , pp. 47-82
    • Friehs, K.1
  • 25
    • 0034496492 scopus 로고    scopus 로고
    • Low-copy plasmids can perform as well as or better than high-copy plasmids for metabolic engineering of bacteria
    • Jones KL, Kim SW, Keasling JD: Low-copy plasmids can perform as well as or better than high-copy plasmids for metabolic engineering of bacteria. Metab Eng 2000, 2:328-338.
    • (2000) Metab Eng , vol.2 , pp. 328-338
    • Jones, K.L.1    Kim, S.W.2    Keasling, J.D.3
  • 26
    • 0027908930 scopus 로고
    • Yield of poly-D(-)-3-hydroxybutyrate from various carbon sources: a theoretical study
    • Yamane T: Yield of poly-D(-)-3-hydroxybutyrate from various carbon sources: a theoretical study. Biotechnol Bioeng 1993, 41:165-170.
    • (1993) Biotechnol Bioeng , vol.41 , pp. 165-170
    • Yamane, T.1
  • 27
    • 0014082204 scopus 로고
    • Glucose and gluconate metabolism in an Escherichia coli mutant lacking phosphoglucose isomerase
    • Fraenkel DG, Levisohn SR: Glucose and gluconate metabolism in an Escherichia coli mutant lacking phosphoglucose isomerase. J Bacteriol 1967, 93:1571-1578.
    • (1967) J Bacteriol , vol.93 , pp. 1571-1578
    • Fraenkel, D.G.1    Levisohn, S.R.2
  • 28
    • 1842582933 scopus 로고    scopus 로고
    • Transcription levels of key metabolic genes are the cause for different glucose utilization pathways in E. coli B (BL21) and E. coli K (JM109)
    • Phue JN, Shiloach J: Transcription levels of key metabolic genes are the cause for different glucose utilization pathways in E. coli B (BL21) and E. coli K (JM109). J Biotechnol 2004, 109:21-30.
    • (2004) J Biotechnol , vol.109 , pp. 21-30
    • Phue, J.N.1    Shiloach, J.2
  • 29
    • 0034965129 scopus 로고    scopus 로고
    • Pyruvate oxidase contributes to the aerobic growth efficiency of Escherichia coli
    • Abdel-Hamid AM, Attwood MM, Guest JR: Pyruvate oxidase contributes to the aerobic growth efficiency of Escherichia coli. Microbiology 2001, 147:1483-1498.
    • (2001) Microbiology , vol.147 , pp. 1483-1498
    • Abdel-Hamid, A.M.1    Attwood, M.M.2    Guest, J.R.3
  • 30
    • 78649717393 scopus 로고    scopus 로고
    • Elimination of D-lactate synthesis increases poly(3-hydroxybutyrate) and ethanol synthesis from glycerol and affects cofactor distribution in recombinant Escherichia coli
    • Nikel PI, Giordano AM, de Almeida A, Godoy MS, Pettinari MJ: Elimination of D-lactate synthesis increases poly(3-hydroxybutyrate) and ethanol synthesis from glycerol and affects cofactor distribution in recombinant Escherichia coli. Appl Environ Microbiol 2010, 76:7400-7406.
    • (2010) Appl Environ Microbiol , vol.76 , pp. 7400-7406
    • Nikel, P.I.1    Giordano, A.M.2    Almeida, A.3    Godoy, M.S.4    Pettinari, M.J.5
  • 31
    • 84871416564 scopus 로고    scopus 로고
    • Effectiveness of xylose utilization for high yield production of lactate-enriched P(lactate-co-3-hydroxybutyrate) using a lactate-overproducing strain of Escherichia coli and an evolved lactate-polymerizing enzyme
    • Nduko JM, Matsumoto K, Ooi T, Taguchi S: Effectiveness of xylose utilization for high yield production of lactate-enriched P(lactate-co-3-hydroxybutyrate) using a lactate-overproducing strain of Escherichia coli and an evolved lactate-polymerizing enzyme. Metab Eng 2013, 15:159-166.
    • (2013) Metab Eng , vol.15 , pp. 159-166
    • Nduko, J.M.1    Matsumoto, K.2    Ooi, T.3    Taguchi, S.4
  • 32
    • 84889863555 scopus 로고    scopus 로고
    • Poly(4-hydroxybutyrate) (P4HB) production in recombinant Escherichia coli: P4HB synthesis is uncoupled with cell growth
    • Le Meur S, Zinn M, Egli T, Thony-Meyer L, Ren Q: Poly(4-hydroxybutyrate) (P4HB) production in recombinant Escherichia coli: P4HB synthesis is uncoupled with cell growth. Microb Cell Fact 2013, 12:123.
    • (2013) Microb Cell Fact , vol.12 , pp. 123
    • Meur, S.1    Zinn, M.2    Egli, T.3    Thony-Meyer, L.4    Ren, Q.5
  • 33
    • 79551667941 scopus 로고    scopus 로고
    • Circular polymerase extension cloning for high-throughput cloning of complex and combinatorial DNA libraries
    • Quan J, Tian J: Circular polymerase extension cloning for high-throughput cloning of complex and combinatorial DNA libraries. Nat Protoc 2011, 6:242-251.
    • (2011) Nat Protoc , vol.6 , pp. 242-251
    • Quan, J.1    Tian, J.2
  • 34
    • 0033037037 scopus 로고    scopus 로고
    • A sensitive, viable-colony staining method using Nile red for direct screening of bacteria that accumulate polyhydroxyalkanoic acids and other lipid storage compounds
    • Spiekermann P, Rehm BH, Kalscheuer R, Baumeister D, Steinbuchel A: A sensitive, viable-colony staining method using Nile red for direct screening of bacteria that accumulate polyhydroxyalkanoic acids and other lipid storage compounds. Arch Microbiol 1999, 171:73-80.
    • (1999) Arch Microbiol , vol.171 , pp. 73-80
    • Spiekermann, P.1    Rehm, B.H.2    Kalscheuer, R.3    Baumeister, D.4    Steinbuchel, A.5
  • 35
    • 77951278557 scopus 로고    scopus 로고
    • Site-specific chromosomal integration of large synthetic constructs
    • Kuhlman TE, Cox EC: Site-specific chromosomal integration of large synthetic constructs. Nucleic Acids Res 2010, 38:e92.
    • (2010) Nucleic Acids Res , vol.38 , pp. e92
    • Kuhlman, T.E.1    Cox, E.C.2
  • 36
    • 84923925548 scopus 로고    scopus 로고
    • Metabolic engineering of Escherichia coli for the production of riboflavin
    • Lin Z, Xu Z, Li Y, Wang Z, Chen T, Zhao X: Metabolic engineering of Escherichia coli for the production of riboflavin. Microbial Cell Factories 2014, 13:104.
    • (2014) Microbial Cell Factories , vol.13 , pp. 104
    • Lin, Z.1    Xu, Z.2    Li, Y.3    Wang, Z.4    Chen, T.5    Zhao, X.6
  • 37
    • 84875670791 scopus 로고    scopus 로고
    • Engineering central metabolic modules of Escherichia coli for improving beta-carotene production
    • Zhao J, Li Q, Sun T, Zhu X, Xu H, Tang J, Zhang X, Ma Y: Engineering central metabolic modules of Escherichia coli for improving beta-carotene production. Metab Eng 2013, 17:42-50.
    • (2013) Metab Eng , vol.17 , pp. 42-50
    • Zhao, J.1    Li, Q.2    Sun, T.3    Zhu, X.4    Xu, H.5    Tang, J.6    Zhang, X.7    Ma, Y.8
  • 38
    • 67650691481 scopus 로고    scopus 로고
    • Overexpression of NAD kinase in recombinant Escherichia coli harboring the phbCAB operon improves poly(3-hydroxybutyrate) production
    • Li ZJ, Cai L, Wu Q, Chen GQ: Overexpression of NAD kinase in recombinant Escherichia coli harboring the phbCAB operon improves poly(3-hydroxybutyrate) production. Appl Microbiol Biotechnol 2009, 83:939-947.
    • (2009) Appl Microbiol Biotechnol , vol.83 , pp. 939-947
    • Li, Z.J.1    Cai, L.2    Wu, Q.3    Chen, G.Q.4
  • 39
    • 84875981840 scopus 로고    scopus 로고
    • Engineering of acetate recycling and citrate synthase to improve aerobic succinate production in Corynebacterium glutamicum
    • Zhu N, Xia H, Wang Z, Zhao X, Chen T: Engineering of acetate recycling and citrate synthase to improve aerobic succinate production in Corynebacterium glutamicum. PLoS One 2013, 8:e60659.
    • (2013) PLoS One , vol.8
    • Zhu, N.1    Xia, H.2    Wang, Z.3    Zhao, X.4    Chen, T.5
  • 40
    • 0028084344 scopus 로고
    • Intracellular concentrations of coenzyme A and its derivatives from Clostridium acetobutylicum ATCC 824 and their roles in enzyme regulation
    • Boynton ZL, Bennett GN, Rudolph FB: Intracellular concentrations of coenzyme A and its derivatives from Clostridium acetobutylicum ATCC 824 and their roles in enzyme regulation. Appl Environ Microbiol 1994, 60:39-44.
    • (1994) Appl Environ Microbiol , vol.60 , pp. 39-44
    • Boynton, Z.L.1    Bennett, G.N.2    Rudolph, F.B.3
  • 41
    • 84906779771 scopus 로고    scopus 로고
    • NADH plays the vital role for chiral pure D-(-)-2,3-butanediol production in Bacillus subtilis under limited oxygen conditions
    • Fu J, Wang Z, Chen T, Liu W, Shi T, Wang G, Tang YJ, Zhao X: NADH plays the vital role for chiral pure D-(-)-2,3-butanediol production in Bacillus subtilis under limited oxygen conditions. Biotechnol Bioeng 2014, 111(10):2126-2131.
    • (2014) Biotechnol Bioeng , vol.111 , Issue.10 , pp. 2126-2131
    • Fu, J.1    Wang, Z.2    Chen, T.3    Liu, W.4    Shi, T.5    Wang, G.6    Tang, Y.J.7    Zhao, X.8
  • 42
    • 0035710746 scopus 로고    scopus 로고
    • Analysis of relative gene expression data using real-time quantitative PCR and the 2(-Delta Delta C(T)) Method
    • Livak KJ, Schmittgen TD: Analysis of relative gene expression data using real-time quantitative PCR and the 2(-Delta Delta C(T)) Method. Methods 2001, 25:402-408.
    • (2001) Methods , vol.25 , pp. 402-408
    • Livak, K.J.1    Schmittgen, T.D.2


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