메뉴 건너뛰기




Volumn 29, Issue 5, 2013, Pages 1124-1130

Metabolic engineering and transhydrogenase effects on NADPH availability in escherichia coli

Author keywords

E. coli; Metabolically engineered strain; Redox; Transhydrogenase

Indexed keywords

E. COLI; ENGINEERED STRAINS; ENZYMATIC REACTION; NADPH AVAILABILITY; REDOX; SYNTHESIS PATHWAYS; TRANSHYDROGENASES; WILD-TYPE CONTROLS;

EID: 84886747287     PISSN: 87567938     EISSN: 15206033     Source Type: Journal    
DOI: 10.1002/btpr.1765     Document Type: Article
Times cited : (34)

References (28)
  • 1
    • 0037313750 scopus 로고    scopus 로고
    • Genome-scale reconstruction of the Saccharomyces cerevisiae metabolic network
    • Forster J, Famili I, Fu P, Palsson BO, Nielsen J. Genome-scale reconstruction of the Saccharomyces cerevisiae metabolic network. Genome Res. 2003;13:244-253.
    • (2003) Genome Res. , vol.13 , pp. 244-253
    • Forster, J.1    Famili, I.2    Fu, P.3    Palsson, B.O.4    Nielsen, J.5
  • 3
    • 14744267181 scopus 로고    scopus 로고
    • Control of fluxes towards antibiotics and the role of primary metabolism in production of antibiotics
    • Gunnarsson N, Eliasson A, Nielsen J. Control of fluxes towards antibiotics and the role of primary metabolism in production of antibiotics. Adv Biochem Eng Biotechnol. 2004;88:137-178.
    • (2004) Adv Biochem Eng Biotechnol. , vol.88 , pp. 137-178
    • Gunnarsson, N.1    Eliasson, A.2    Nielsen, J.3
  • 4
    • 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 AM, Andrews J, Hussein I, Bennett GN, San KY. Effect of overexpression of a soluble pyridine nucleotide transhydrogenase (UdhA) on the production of poly(3-hydroxybutyrate) in Escherichia coli. Biotechnol Prog. 2006;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
  • 5
    • 39549101609 scopus 로고    scopus 로고
    • Engineering poly(3-hydroxybutyrate-co-3-hydroxyvalerate) copolymer composition in E. coli
    • Wong MS, Causey TB, Mantzaris N, Bennett GN, San KY. Engineering poly(3-hydroxybutyrate-co-3-hydroxyvalerate) copolymer composition in E. coli. Biotechnol Bioeng. 2008;99:919-928.
    • (2008) Biotechnol Bioeng. , vol.99 , pp. 919-928
    • Wong, M.S.1    Causey, T.B.2    Mantzaris, N.3    Bennett, G.N.4    San, K.Y.5
  • 6
    • 0030632239 scopus 로고    scopus 로고
    • New alcohol dehydrogenases for the synthesis of chiral compounds
    • Hummel W. New alcohol dehydrogenases for the synthesis of chiral compounds. Adv Biochem Eng Biotechnol. 1997;58:145-184.
    • (1997) Adv Biochem Eng Biotechnol. , vol.58 , pp. 145-184
    • Hummel, W.1
  • 7
    • 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, Canonaco F, Heri S, Perrenoud A, Fischer E. The soluble and membrane-bound transhydrogenases UdhA and PntAB have divergent functions in NADPH metabolism of Escherichia coli. J Biol Chem. 2004;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
  • 8
    • 0021095336 scopus 로고
    • Why are two different types of pyridine nucleotide transhydrogenase found in living organisms?
    • Voordouw G, van der Vies SM, Themmen AP. Why are two different types of pyridine nucleotide transhydrogenase found in living organisms? Eur J Biochem. 1983;131:527-533.
    • (1983) Eur J Biochem. , vol.131 , pp. 527-533
    • Voordouw, G.1    van der Vies, S.M.2    Themmen, A.P.3
  • 9
    • 0032945184 scopus 로고    scopus 로고
    • The udhA gene of Escherichia coli encodes a soluble pyridine nucleotide transhydrogenase
    • Boonstra B, French CE, Wainwright I, Bruce NC. The udhA gene of Escherichia coli encodes a soluble pyridine nucleotide transhydrogenase. J Bacteriol. 1999;181:1030-1034.
    • (1999) J Bacteriol. , vol.181 , pp. 1030-1034
    • Boonstra, B.1    French, C.E.2    Wainwright, I.3    Bruce, N.C.4
  • 10
    • 0022759517 scopus 로고
    • Nucleotide sequence of the pntA and pntB genes encoding the pyridine nucleotide transhydrogenase of Escherichia coli
    • Clarke DM, Loo TW, Gillam S, Bragg PD. Nucleotide sequence of the pntA and pntB genes encoding the pyridine nucleotide transhydrogenase of Escherichia coli. Eur J Biochem. 1986;158:647-653.
    • (1986) Eur J Biochem. , vol.158 , pp. 647-653
    • Clarke, D.M.1    Loo, T.W.2    Gillam, S.3    Bragg, P.D.4
  • 11
    • 0018866929 scopus 로고
    • Effects of an insertion mutation in a locus affecting pyridine nucleotide transhydrogenase (pnt::Tn5) on the growth of Escherichia coli
    • Hanson RL, Rose C. Effects of an insertion mutation in a locus affecting pyridine nucleotide transhydrogenase (pnt::Tn5) on the growth of Escherichia coli. J Bacteriol. 1980;141:401-404.
    • (1980) J Bacteriol. , vol.141 , pp. 401-404
    • Hanson, R.L.1    Rose, C.2
  • 12
    • 0035856579 scopus 로고    scopus 로고
    • Metabolic flux response to phosphoglucose isomerase knock-out in Escherichia coli and impact of overexpression of the soluble transhydrogenase UdhA
    • Canonaco F, Hess TA, Heri S, Wang T, Szyperski T, Sauer U. Metabolic flux response to phosphoglucose isomerase knock-out in Escherichia coli and impact of overexpression of the soluble transhydrogenase UdhA. FEMS Microbiol Lett. 2001;204:247-252.
    • (2001) FEMS Microbiol Lett. , vol.204 , pp. 247-252
    • Canonaco, F.1    Hess, T.A.2    Heri, S.3    Wang, T.4    Szyperski, T.5    Sauer, U.6
  • 13
  • 14
    • 23744487493 scopus 로고    scopus 로고
    • Escherichia coli phosphoglucose isomerase can be substituted by members of the PGI family, the PGI/PMI family, and the cPGI family
    • Hansen T, Schonheit P. Escherichia coli phosphoglucose isomerase can be substituted by members of the PGI family, the PGI/PMI family, and the cPGI family. FEMS Microbiol Lett. 2005;250:49-53.
    • (2005) FEMS Microbiol Lett. , vol.250 , pp. 49-53
    • Hansen, T.1    Schonheit, P.2
  • 15
    • 0023681148 scopus 로고
    • Physiological roles of nicotinamide nucleotide transhydrogenase
    • Hoek JB, Rydstrom J. Physiological roles of nicotinamide nucleotide transhydrogenase. Biochem J. 1988;254:1-10.
    • (1988) Biochem J. , vol.254 , pp. 1-10
    • Hoek, J.B.1    Rydstrom, J.2
  • 17
    • 77955429093 scopus 로고    scopus 로고
    • High NADPH/NADP+ ratio improves thymidine production by a metabolically engineered Escherichia coli strain
    • Lee HC, Kim JS, Jang W, Kim SY. High NADPH/NADP+ ratio improves thymidine production by a metabolically engineered Escherichia coli strain. J Biotechnol. 2010;149:24-32.
    • (2010) J Biotechnol. , vol.149 , pp. 24-32
    • Lee, H.C.1    Kim, J.S.2    Jang, W.3    Kim, S.Y.4
  • 18
    • 43549109862 scopus 로고    scopus 로고
    • Production of (S)-2-chloropropionate by asymmetric reduction of 2-chloroacrylate with 2-haloacrylate reductase coupled with glucose dehydrogenase
    • Kurata A, Fujita M, Mowafy AM, Kamachi H, Kurihara T, Esaki N. Production of (S)-2-chloropropionate by asymmetric reduction of 2-chloroacrylate with 2-haloacrylate reductase coupled with glucose dehydrogenase. J Biosci Bioeng. 2008;105:429-431.
    • (2008) J Biosci Bioeng. , vol.105 , pp. 429-431
    • Kurata, A.1    Fujita, M.2    Mowafy, A.M.3    Kamachi, H.4    Kurihara, T.5    Esaki, N.6
  • 19
    • 20144374483 scopus 로고    scopus 로고
    • 2-Haloacrylate reductase, a novel enzyme of the medium chain dehydrogenase/reductase superfamily that catalyzes the reduction of a carbon-carbon double bond of unsaturated organohalogen compounds
    • Kurata A, Kurihara T, Kamachi H, Esaki N. 2-Haloacrylate reductase, a novel enzyme of the medium chain dehydrogenase/reductase superfamily that catalyzes the reduction of a carbon-carbon double bond of unsaturated organohalogen compounds. J Biol Chem. 2005;280:20286-20291.
    • (2005) J Biol Chem. , vol.280 , pp. 20286-20291
    • Kurata, A.1    Kurihara, T.2    Kamachi, H.3    Esaki, N.4
  • 20
    • 0034612342 scopus 로고    scopus 로고
    • One-step inactivation of chromosomal genes in Escherichia coli K-12 using PCR products
    • Datsenko KA, Wanner BL. One-step inactivation of chromosomal genes in Escherichia coli K-12 using PCR products. Proc Natl Acad Sci USA. 2000;97:6640-6645.
    • (2000) Proc Natl Acad Sci USA. , vol.97 , pp. 6640-6645
    • Datsenko, K.A.1    Wanner, B.L.2
  • 21
    • 31544450286 scopus 로고    scopus 로고
    • Construction of Escherichia coli K-12 in-frame, single-gene knockout mutants: the Keio collection
    • Baba T, Ara T, Hasegawa M, Takai Y, Okumura Y, Baba M, et al. Construction of Escherichia coli K-12 in-frame, single-gene knockout mutants: the Keio collection. Mol Syst Biol. 2006;2:2006-2008.
    • (2006) Mol Syst Biol. , vol.2 , pp. 2006-2008
    • Baba, T.1    Ara, T.2    Hasegawa, M.3    Takai, Y.4    Okumura, Y.5    Baba, M.6
  • 22
    • 0034060604 scopus 로고    scopus 로고
    • High copy number plasmids compatible with commonly used cloning vectors
    • 404, 406 passim.
    • Phillips GJ, Park SK, Huber D. High copy number plasmids compatible with commonly used cloning vectors. Biotechniques. 2000;28:400-402, 404, 406 passim.
    • (2000) Biotechniques. , vol.28 , pp. 400-402
    • Phillips, G.J.1    Park, S.K.2    Huber, D.3
  • 23
    • 34247584154 scopus 로고    scopus 로고
    • Expression of the Escherichia coli pntAB genes encoding a membrane-bound transhydrogenase in Corynebacterium glutamicum improves L-lysine formation
    • Kabus A, Georgi T, Wendisch VF, Bott M. Expression of the Escherichia coli pntAB genes encoding a membrane-bound transhydrogenase in Corynebacterium glutamicum improves L-lysine formation. Appl Microbiol Biotechnol. 2007;75:47-53.
    • (2007) Appl Microbiol Biotechnol. , vol.75 , pp. 47-53
    • Kabus, A.1    Georgi, T.2    Wendisch, V.F.3    Bott, M.4
  • 24
    • 0033565415 scopus 로고    scopus 로고
    • A shift in the equilibrium constant at the catalytic site of proton-translocating transhydrogenase: significance for a 'binding-change' mechanism
    • Venning JD, Jackson JB. A shift in the equilibrium constant at the catalytic site of proton-translocating transhydrogenase: significance for a 'binding-change' mechanism. Biochem J. 1999;341:329-337.
    • (1999) Biochem J. , vol.341 , pp. 329-337
    • Venning, J.D.1    Jackson, J.B.2
  • 25
    • 79954423939 scopus 로고    scopus 로고
    • Improved NADPH supply for xylitol production by engineered Escherichia coli with glycolytic mutations
    • Chin JW, Cirino PC. Improved NADPH supply for xylitol production by engineered Escherichia coli with glycolytic mutations. Biotechnol Prog. 2011;27:333-341.
    • (2011) Biotechnol Prog. , vol.27 , pp. 333-341
    • Chin, J.W.1    Cirino, P.C.2
  • 26
    • 79551491573 scopus 로고    scopus 로고
    • Anaerobic obligatory xylitol production in Escherichia coli strains devoid of native fermentation pathways
    • Akinterinwa O, Cirino PC. Anaerobic obligatory xylitol production in Escherichia coli strains devoid of native fermentation pathways. Appl Environ Microbiol 2011; 77:706-709.
    • (2011) Appl Environ Microbiol , vol.77 , pp. 706-709
    • Akinterinwa, O.1    Cirino, P.C.2
  • 27
    • 0345529074 scopus 로고    scopus 로고
    • Responses of the central metabolism in Escherichia coli to phosphoglucose isomerase and glucose-6-phosphate dehydrogenase knockouts
    • Hua Q, Yang C, Baba T, Mori H, Shimizu K. Responses of the central metabolism in Escherichia coli to phosphoglucose isomerase and glucose-6-phosphate dehydrogenase knockouts. J Bacteriol. 2003;185:7053-7067.
    • (2003) J Bacteriol. , vol.185 , pp. 7053-7067
    • Hua, Q.1    Yang, C.2    Baba, T.3    Mori, H.4    Shimizu, K.5
  • 28
    • 12444320410 scopus 로고    scopus 로고
    • Improved synthesis of chiral alcohols with Escherichia coli cells co-expressing pyridine nucleotide transhydrogenase, NADP+-dependent alcohol dehydrogenase and NAD+-dependent formate dehydrogenase
    • Weckbecker A, Hummel W. Improved synthesis of chiral alcohols with Escherichia coli cells co-expressing pyridine nucleotide transhydrogenase, NADP+-dependent alcohol dehydrogenase and NAD+-dependent formate dehydrogenase. Biotechnol Lett. 2004;26:1739-1744.
    • (2004) Biotechnol Lett. , vol.26 , pp. 1739-1744
    • Weckbecker, A.1    Hummel, W.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.