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Volumn 77, Issue 2, 2011, Pages 706-709

Anaerobic obligatory xylitol production in Escherichia coli strains devoid of native fermentation pathways

Author keywords

[No Author keywords available]

Indexed keywords

ANAEROBIC GLUCOSE; MEMBRANE-BOUND; THEORETICAL YIELD; TRANSHYDROGENASES; XYLOSE REDUCTASE;

EID: 79551491573     PISSN: 00992240     EISSN: 10985336     Source Type: Journal    
DOI: 10.1128/AEM.01890-10     Document Type: Article
Times cited : (20)

References (21)
  • 1
    • 55549118196 scopus 로고    scopus 로고
    • Heterologous expression of Dxylulokinase from Pichia stipitis enables high levels of xylitol production by engineered Escherichia coli growing on xylose
    • Akinterinwa, O., and P. C. Cirino. 2009. Heterologous expression of Dxylulokinase from Pichia stipitis enables high levels of xylitol production by engineered Escherichia coli growing on xylose. Metab. Eng. 11:48-55.
    • (2009) Metab. Eng. , vol.11 , pp. 48-55
    • Akinterinwa, O.1    Cirino, P.C.2
  • 2
    • 31544450286 scopus 로고    scopus 로고
    • Construction of Escherichia coli K-12 in-frame, singlegene knockout mutants: The Keio collection
    • Baba, T., et al. 2006. Construction of Escherichia coli K-12 in-frame, singlegene knockout mutants: The Keio collection. Mol. Syst. Biol. 2:2006.
    • (2006) Mol. Syst. Biol. , vol.2 , pp. 2006
    • Baba, T.1
  • 3
    • 48649109598 scopus 로고    scopus 로고
    • Metabolic capacity estimation of Escherichia coli as a platform for redox biocatalysis: Constraint-based modeling and experimental verification
    • Blank, L. M., B. E. Ebert, B. Buhler, and A. Schmid. 2008. Metabolic capacity estimation of Escherichia coli as a platform for redox biocatalysis: Constraint-based modeling and experimental verification. Biotechnol. Bioeng. 100:1050-1065.
    • (2008) Biotechnol. Bioeng. , vol.100 , pp. 1050-1065
    • Blank, L.M.1    Ebert, B.E.2    Buhler, B.3    Schmid, A.4
  • 4
    • 40549093298 scopus 로고    scopus 로고
    • NADH availability limits asymmetric biocatalytic epoxidation in a growing recombinant Escherichia coli strain
    • Buhler, B., J. B. Park, L. M. Blank, and A. Schmid. 2008. NADH availability limits asymmetric biocatalytic epoxidation in a growing recombinant Escherichia coli strain. Appl. Environ. Microbiol. 74:1436-1446.
    • (2008) Appl. Environ. Microbiol. , vol.74 , pp. 1436-1446
    • Buhler, B.1    Park, J.B.2    Blank, L.M.3    Schmid, A.4
  • 5
    • 0037417864 scopus 로고    scopus 로고
    • Engineering the metabolism of Escherichia coli W3110 for the conversion of sugar to redox-neutral and oxidized products: Homoacetate production
    • Causey, T. B., S. Zhou, K. T. Shanmugam, and L. O. Ingram. 2003. Engineering the metabolism of Escherichia coli W3110 for the conversion of sugar to redox-neutral and oxidized products: Homoacetate production. Proc. Natl. Acad. Sci. U. S. A. 100:825-832.
    • (2003) Proc. Natl. Acad. Sci. U. S. A. , vol.100 , pp. 825-832
    • Causey, T.B.1    Zhou, S.2    Shanmugam, K.T.3    Ingram, L.O.4
  • 6
    • 58149238062 scopus 로고    scopus 로고
    • Analysis of NADPH supply during xylitol production by engineered Escherichia coli
    • Chin, J. W., R. Khankal, C. A. Monroe, C. D. Maranas, and P. C. Cirino. 2009. Analysis of NADPH supply during xylitol production by engineered Escherichia coli. Biotechnol. Bioeng. 102:209-220.
    • (2009) Biotechnol. Bioeng. , vol.102 , pp. 209-220
    • Chin, J.W.1    Khankal, R.2    Monroe, C.A.3    Maranas, C.D.4    Cirino, P.C.5
  • 7
    • 33845441711 scopus 로고    scopus 로고
    • Engineering Escherichia coli for xylitol production from glucose-xylose mixtures
    • Cirino, P. C., J. W. Chin, and L. O. Ingram. 2006. Engineering Escherichia coli for xylitol production from glucose-xylose mixtures. Biotechnol. Bioeng. 95:1167-1176.
    • (2006) Biotechnol. Bioeng. , vol.95 , pp. 1167-1176
    • Cirino, P.C.1    Chin, J.W.2    Ingram, L.O.3
  • 8
    • 0034612342 scopus 로고    scopus 로고
    • One-step inactivation of chromosomal genes in Escherichia coli K-12 using PCR products
    • Datsenko, K. A., and B. L. Wanner. 2000. One-step inactivation of chromosomal genes in Escherichia coli K-12 using PCR products. Proc. Natl. Acad. Sci. U. S. A. 97:6640-6645.
    • (2000) Proc. Natl. Acad. Sci. U. S. A. , vol.97 , pp. 6640-6645
    • Datsenko, K.A.1    Wanner, B.L.2
  • 9
    • 0032906898 scopus 로고    scopus 로고
    • The steady-state internal redox state (NADH/NAD) reflects the external redox state and is correlated with catabolic adaptation in Escherichia coli
    • de Graef, M. R., S. Alexeeva, J. L. Snoep, and M. J. Teixeira de Mattos. 1999. The steady-state internal redox state (NADH/NAD) reflects the external redox state and is correlated with catabolic adaptation in Escherichia coli. J. Bacteriol. 181:2351-2357.
    • (1999) J. Bacteriol. , vol.181 , pp. 2351-2357
    • De Graef, M.R.1    Alexeeva, S.2    Snoep, J.L.3    De Mattos, M.J.T.4
  • 10
    • 0032537589 scopus 로고    scopus 로고
    • The pyruvate dehydrogenase multi-enzyme complex from gram-negative bacteria
    • de Kok, A., A. F. Hengeveld, A. Martin, and A. H. Westphal. 1998. The pyruvate dehydrogenase multi-enzyme complex from gram-negative bacteria. Biochim. Biophys. Acta 1385:353-366.
    • (1998) Biochim. Biophys. Acta , vol.1385 , pp. 353-366
    • De Kok, A.1    Hengeveld, A.F.2    Martin, A.3    Westphal, A.H.4
  • 11
    • 0035682064 scopus 로고    scopus 로고
    • Conditional-replication, integration, excision, and retrieval plasmid-host systems for gene structure-function studies of bacteria
    • Haldimann, A., and B. L. Wanner. 2001. Conditional-replication, integration, excision, and retrieval plasmid-host systems for gene structure-function studies of bacteria. J. Bacteriol. 183:6384-6393.
    • (2001) J. Bacteriol. , vol.183 , pp. 6384-6393
    • Haldimann, A.1    Wanner, B.L.2
  • 12
    • 0014010920 scopus 로고
    • Regulation of pyruvate dehydrogenase activity in Escherichia coli K12
    • Hansen, R. G., and U. Henning. 1966. Regulation of pyruvate dehydrogenase activity in Escherichia coli K12. Biochim. Biophys. Acta 12:355-358.
    • (1966) Biochim. Biophys. Acta , vol.12 , pp. 355-358
    • Hansen, R.G.1    Henning, U.2
  • 13
    • 0038748286 scopus 로고    scopus 로고
    • Molecular characterization of a gene for aldose reductase (CbXYL1) from Candida boidinii and its expression in Saccharomyces cerevisiae
    • Kang, M. H., H. Y. Ni, and T. W. Jeffries. 2003. Molecular characterization of a gene for aldose reductase (CbXYL1) from Candida boidinii and its expression in Saccharomyces cerevisiae. Appl. Biochem. Biotech. 105:265-276.
    • (2003) Appl. Biochem. Biotech. , vol.105 , pp. 265-276
    • Kang, M.H.1    Ni, H.Y.2    Jeffries, T.W.3
  • 14
    • 33947357776 scopus 로고    scopus 로고
    • Construction of an Escherichia coli K-12 mutant for homoethanologenic fermentation of glucose or xylose without foreign genes
    • Kim, Y., L. O. Ingram, and K. T. Shanmugam. 2007. Construction of an Escherichia coli K-12 mutant for homoethanologenic fermentation of glucose or xylose without foreign genes. Appl. Environ. Microbiol. 73:1766-1771.
    • (2007) Appl. Environ. Microbiol. , vol.73 , pp. 1766-1771
    • Kim, Y.1    Ingram, L.O.2    Shanmugam, K.T.3
  • 15
    • 44349173795 scopus 로고    scopus 로고
    • Dihydrolipoamide dehydrogenase mutation alters the NADH sensitivity of pyruvate dehydrogenase complex of Escherichia coli K-12
    • Kim, Y., L. O. Ingram, and K. T. Shanmugam. 2008. Dihydrolipoamide dehydrogenase mutation alters the NADH sensitivity of pyruvate dehydrogenase complex of Escherichia coli K-12. J. Bacteriol. 190:3851-3858.
    • (2008) J. Bacteriol. , vol.190 , pp. 3851-3858
    • Kim, Y.1    Ingram, L.O.2    Shanmugam, K.T.3
  • 19
    • 33646045867 scopus 로고    scopus 로고
    • Effect of overexpression of a soluble pyridine nucleotide transhydrogenase (UdhA) on the production of poly(3-hydroxybutyrate) in Escherichia coli
    • Sanchez, A. M., J. Andrews, I. Hussein, G. N. Bennett, and K. Y. San. 2006. Effect of overexpression of a soluble pyridine nucleotide transhydrogenase (UdhA) on the production of poly(3-hydroxybutyrate) in Escherichia coli. Biotechnol. Prog. 22:420-425.
    • (2006) Biotechnol. Prog. , vol.22 , pp. 420-425
    • Sanchez, A.M.1    Andrews, J.2    Hussein, I.3    Bennett, G.N.4    San, K.Y.5
  • 20
    • 1342325419 scopus 로고    scopus 로고
    • The soluble and membrane-bound transhydrogenases UdhA and PntAB have divergent functions in NADPH metabolism of Escherichia coli
    • Sauer, U., F. Canonaco, S. Heri, A. Perrenoud, and E. Fischer. 2004. The soluble and membrane-bound transhydrogenases UdhA and PntAB have divergent functions in NADPH metabolism of Escherichia coli. J. Biol. Chem. 279:6613-6619.
    • (2004) J. Biol. Chem. , vol.279 , pp. 6613-6619
    • Sauer, U.1    Canonaco, F.2    Heri, S.3    Perrenoud, A.4    Fischer, E.5
  • 21
    • 1842762173 scopus 로고    scopus 로고
    • Understanding and improving NADPH-dependent reactions by nongrowing Escherichia coli cells
    • Walton, A. Z., and J. D. Stewart. 2004. Understanding and improving NADPH-dependent reactions by nongrowing Escherichia coli cells. Biotechnol. Prog. 20:403-411.
    • (2004) Biotechnol. Prog. , vol.20 , pp. 403-411
    • Walton, A.Z.1    Stewart, J.D.2


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