메뉴 건너뛰기




Volumn 74, Issue 4, 2008, Pages 950-958

Suppressing posttranslational gluconoylation of heterologous proteins by metabolic engineering of Escherichia coli

Author keywords

[No Author keywords available]

Indexed keywords

GLUCONOYLATION; METABOLIC FLUX ANALYSIS; METABOLIC PATHWAY ENGINEERING; PENTOSE PHOSPHATE PATHWAY; POSTTRANSLATIONAL MODIFICATION;

EID: 39649092097     PISSN: 00992240     EISSN: None     Source Type: Journal    
DOI: 10.1128/AEM.01790-07     Document Type: Article
Times cited : (40)

References (27)
  • 1
    • 0032884573 scopus 로고    scopus 로고
    • Recombinant protein expression in Escherichia coli
    • Baneyx, F. 1999. Recombinant protein expression in Escherichia coli. Curr. Opin. Biotechnol. 10:411-421.
    • (1999) Curr. Opin. Biotechnol , vol.10 , pp. 411-421
    • Baneyx, F.1
  • 2
    • 0035069009 scopus 로고    scopus 로고
    • Inhibitory effect of glycation on catalytic activity of alanine aminotransferase
    • Beranek, M., J. Drsata, and V. Palicka. 2001. Inhibitory effect of glycation on catalytic activity of alanine aminotransferase. Mol. Cell. Biochem. 218:35-39.
    • (2001) Mol. Cell. Biochem , vol.218 , pp. 35-39
    • Beranek, M.1    Drsata, J.2    Palicka, V.3
  • 3
    • 0031260036 scopus 로고    scopus 로고
    • Affinity purification and elimination of methionine oxidation in recombinant human cystatin C
    • Berti, P. J., I. Ekiel, P. Lindahl, M. Abrahamson, and A. C. Storer. 1997. Affinity purification and elimination of methionine oxidation in recombinant human cystatin C. Protein Expr. Purif. 11:111-118.
    • (1997) Protein Expr. Purif , vol.11 , pp. 111-118
    • Berti, P.J.1    Ekiel, I.2    Lindahl, P.3    Abrahamson, M.4    Storer, A.C.5
  • 4
    • 0029099002 scopus 로고
    • Role of glycine1 and lysine2 in the glycation of bovine gamma-B-crystallin
    • Casey, E. B., H. R. Zhao, and E. C. Abraham. 1995. Role of glycine1 and lysine2 in the glycation of bovine gamma-B-crystallin. J. Biol. Chem. 270:20781-20786.
    • (1995) J. Biol. Chem , vol.270 , pp. 20781-20786
    • Casey, E.B.1    Zhao, H.R.2    Abraham, E.C.3
  • 5
    • 0029329218 scopus 로고
    • Fluxes of carbon, phosphorylation, and redox intermediates during growth of Saccharomyces cerevisiae on different carbon sources
    • Cortassa, S., J. C. Aon, and M. A. Aon. 1995. Fluxes of carbon, phosphorylation, and redox intermediates during growth of Saccharomyces cerevisiae on different carbon sources. Biotechnol. Bioeng. 47:193-208.
    • (1995) Biotechnol. Bioeng , vol.47 , pp. 193-208
    • Cortassa, S.1    Aon, J.C.2    Aon, M.A.3
  • 6
    • 0034623222 scopus 로고    scopus 로고
    • Molecular characterization of the first two enzymes of the pentose-phosphate pathway of Trypanosoma brucei
    • Duffieux, F., J. van Roy, P. Michels, and F. R. Opperdoes. 2000. Molecular characterization of the first two enzymes of the pentose-phosphate pathway of Trypanosoma brucei. J. Biol. Chem. 275:27559-27565.
    • (2000) J. Biol. Chem , vol.275 , pp. 27559-27565
    • Duffieux, F.1    van Roy, J.2    Michels, P.3    Opperdoes, F.R.4
  • 8
    • 84886462579 scopus 로고    scopus 로고
    • Methods for preventing gluconoylation of proteins
    • September, U.S. patent 04006507
    • Gardner, A. R., T. D. Sweitzer, A. H. Taylor, and P. S. Patel. September 2004. Methods for preventing gluconoylation of proteins. U.S. patent 04006507.
    • (2004)
    • Gardner, A.R.1    Sweitzer, T.D.2    Taylor, A.H.3    Patel, P.S.4
  • 9
    • 0033080755 scopus 로고    scopus 로고
    • Geoghegan, K. F., H. B. F. Dixon, P. J. Rosner, L. R. Hoth, A. J. Lanzetti, K. A. Borzilleri, E. S. Marr, L. H. Pezullo, L. B. Martin, P. K. LeMotte, A. S. McColl, A. V. Kamath, and J. G. Stroh. 1999. Spontaneous alpha-N-6-phosphogluconoylation of a His tag in Escherichia coli: the cause of extra mass of 258 or 178 Da in fusion proteins. Anal. Biochem. 267:169-184.
    • Geoghegan, K. F., H. B. F. Dixon, P. J. Rosner, L. R. Hoth, A. J. Lanzetti, K. A. Borzilleri, E. S. Marr, L. H. Pezullo, L. B. Martin, P. K. LeMotte, A. S. McColl, A. V. Kamath, and J. G. Stroh. 1999. Spontaneous alpha-N-6-phosphogluconoylation of a "His tag" in Escherichia coli: the cause of extra mass of 258 or 178 Da in fusion proteins. Anal. Biochem. 267:169-184.
  • 10
    • 0033932518 scopus 로고    scopus 로고
    • The Pseudomonas aeruginosa devB/SOL homolog, pgl, is a member of the hex regulon and encodes 6-phosphogluconolactonase
    • Hager, P. W., M. W. Calfee, and P. Phibbs. 2000. The Pseudomonas aeruginosa devB/SOL homolog, pgl, is a member of the hex regulon and encodes 6-phosphogluconolactonase. J. Bacteriol. 182:3934-3941.
    • (2000) J. Bacteriol , vol.182 , pp. 3934-3941
    • Hager, P.W.1    Calfee, M.W.2    Phibbs, P.3
  • 11
    • 0004212736 scopus 로고
    • Chemical synthesis of the bacterial cell: Polymerization, biosynthesis, fueling reactions, and transport
    • Sinauer Associates, Sunderland, MA
    • Ingraham, J. L., O. Maaloe, and F. C. Neidhardt. 1983. Chemical synthesis of the bacterial cell: polymerization, biosynthesis, fueling reactions, and transport, p. 87-174. In Growth of the bacterial cell. Sinauer Associates, Sunderland, MA.
    • (1983) Growth of the bacterial cell , pp. 87-174
    • Ingraham, J.L.1    Maaloe, O.2    Neidhardt, F.C.3
  • 12
    • 0037324340 scopus 로고    scopus 로고
    • Reciprocal regulation of inflammation and lipid metabolism by liver X receptors
    • Joseph, S. B., A. Castrillo, B. A. Laffitte, D. J. Mangelsdorf, and P. Tontonoz. 2003. Reciprocal regulation of inflammation and lipid metabolism by liver X receptors. Nat. Med. 9:213-219.
    • (2003) Nat. Med , vol.9 , pp. 213-219
    • Joseph, S.B.1    Castrillo, A.2    Laffitte, B.A.3    Mangelsdorf, D.J.4    Tontonoz, P.5
  • 13
    • 0035007293 scopus 로고    scopus 로고
    • Post-translational modification of the N-terminal His tag interferes with the crystallization of the wild-type and mutant SH3 domains from chicken src tyrosine kinase
    • Kim, K. M., E. C. Yi, D. Baker, and K. Y. J. Zhang. 2001. Post-translational modification of the N-terminal His tag interferes with the crystallization of the wild-type and mutant SH3 domains from chicken src tyrosine kinase. Acta Crystallogr. Sect. D 57:759-762.
    • (2001) Acta Crystallogr. Sect. D , vol.57 , pp. 759-762
    • Kim, K.M.1    Yi, E.C.2    Baker, D.3    Zhang, K.Y.J.4
  • 14
    • 0030789847 scopus 로고    scopus 로고
    • The effect of delta-gluconolactone, an oxidised analogue of glucose, on the nonenzymatic glycation of human and rat haemoglobin
    • Lindsay, R. M., W. Smith, W. K. Lee, M. H. Dominiczak, and J. D. Baird. 1997. The effect of delta-gluconolactone, an oxidised analogue of glucose, on the nonenzymatic glycation of human and rat haemoglobin. Clin. Chim. Acta 263:239-247.
    • (1997) Clin. Chim. Acta , vol.263 , pp. 239-247
    • Lindsay, R.M.1    Smith, W.2    Lee, W.K.3    Dominiczak, M.H.4    Baird, J.D.5
  • 15
    • 0347065359 scopus 로고    scopus 로고
    • Glycation and post-translational processing of human interferon-gamma expressed in Escherichia coli
    • Mironova, R., T. Niwa, R. Dimitrova, M. Bosanova, and I. Ivanov. 2003. Glycation and post-translational processing of human interferon-gamma expressed in Escherichia coli. J. Biol. Chem. 278:51068-51074.
    • (2003) J. Biol. Chem , vol.278 , pp. 51068-51074
    • Mironova, R.1    Niwa, T.2    Dimitrova, R.3    Bosanova, M.4    Ivanov, I.5
  • 17
    • 19944421092 scopus 로고    scopus 로고
    • Glucose metabolism at high cell density growth of Escherichia coli B and Escherichia coli K
    • Phue, J., S. B. Noronha, R. Hattacharyya, A. J. Wolfe, and J. Shiloach. 2005. Glucose metabolism at high cell density growth of Escherichia coli B and Escherichia coli K. Biotechnol. Bioeng. 90:805-820.
    • (2005) Biotechnol. Bioeng , vol.90 , pp. 805-820
    • Phue, J.1    Noronha, S.B.2    Hattacharyya, R.3    Wolfe, A.J.4    Shiloach, J.5
  • 18
    • 0029550860 scopus 로고
    • Reactivity of 6-phosphogluconolactone with hydroxylamine: The possible involvement of glucose-6-phosphate dehydrogenase in endogenous glycation reactions
    • Rakitzis, E. T., and P. Papandreou. 1995. Reactivity of 6-phosphogluconolactone with hydroxylamine: the possible involvement of glucose-6-phosphate dehydrogenase in endogenous glycation reactions. Biochem. Int. 37:747-755.
    • (1995) Biochem. Int , vol.37 , pp. 747-755
    • Rakitzis, E.T.1    Papandreou, P.2
  • 19
    • 0031780918 scopus 로고    scopus 로고
    • Kinetic analysis of 6-phosphogluconolactone hydrolysis in hemolysates
    • Rakitzis, E. T., and P. Papandreou. 1998. Kinetic analysis of 6-phosphogluconolactone hydrolysis in hemolysates. Chem.-Biol. Interact. 113:205-216.
    • (1998) Chem.-Biol. Interact , vol.113 , pp. 205-216
    • Rakitzis, E.T.1    Papandreou, P.2
  • 20
    • 0026782586 scopus 로고
    • Induction of specific enzymes of the oxidative pentose pathway by glucono-delta-lactone in Saccharomyces cerevisiae
    • Sinha, A., and P. K. Maitra. 1992. Induction of specific enzymes of the oxidative pentose pathway by glucono-delta-lactone in Saccharomyces cerevisiae. J. Gen. Microbiol. 138:1865-1873.
    • (1992) J. Gen. Microbiol , vol.138 , pp. 1865-1873
    • Sinha, A.1    Maitra, P.K.2
  • 21
    • 23744476305 scopus 로고    scopus 로고
    • Maillard reaction in eye disease
    • Stitt, A. W. 2005. Maillard reaction in eye disease. Ann. N. Y. Acad. Sci. 1043:582-597.
    • (2005) Ann. N. Y. Acad. Sci , vol.1043 , pp. 582-597
    • Stitt, A.W.1
  • 22
    • 0029146299 scopus 로고
    • 13C-labeling of proteinogenic amino acids: An efficient analytical tool to investigate intermediary metabolism
    • 13C-labeling of proteinogenic amino acids: an efficient analytical tool to investigate intermediary metabolism. Eur. J. Biochem. 232:433-448.
    • (1995) Eur. J. Biochem , vol.232 , pp. 433-448
    • Szyperski, T.1
  • 23
    • 26644440190 scopus 로고    scopus 로고
    • Proteomic profiling of Escherichia coli proteins under high-cell density fed-batch cultivation with overexpression of phosphogluconolactonase
    • Wang, Y., S. L. Wu, W. S. Hancock, R. Trala, M. Kessler, A. H. Taylor, P. S. Patel, and J. C. Aon. 2005. Proteomic profiling of Escherichia coli proteins under high-cell density fed-batch cultivation with overexpression of phosphogluconolactonase. Biotechnol. Prog. 21:1401-1411.
    • (2005) Biotechnol. Prog , vol.21 , pp. 1401-1411
    • Wang, Y.1    Wu, S.L.2    Hancock, W.S.3    Trala, R.4    Kessler, M.5    Taylor, A.H.6    Patel, P.S.7    Aon, J.C.8
  • 24
    • 0023259759 scopus 로고
    • Glucose autooxidation and protein modification. The potential role of autoxidative glycosylation in diabetes
    • Wolff, S. P., and R. T. Dean. 1897. Glucose autooxidation and protein modification. The potential role of autoxidative glycosylation in diabetes. Biochem. J. 245:243-250.
    • (1897) Biochem. J , vol.245 , pp. 243-250
    • Wolff, S.P.1    Dean, R.T.2
  • 26
    • 0033533509 scopus 로고    scopus 로고
    • Identification of a gluconic acid derivative attached to the N-terminus of histidine-tagged proteins expressed in bacteria
    • Yan, Z., G. W. Caldwell, and P. A. McDonell. 1999. Identification of a gluconic acid derivative attached to the N-terminus of histidine-tagged proteins expressed in bacteria. Biochem. Biophys. Res. Commun. 262:793-800.
    • (1999) Biochem. Biophys. Res. Commun , vol.262 , pp. 793-800
    • Yan, Z.1    Caldwell, G.W.2    McDonell, P.A.3
  • 27
    • 0033532587 scopus 로고    scopus 로고
    • Mass spectrometry determination of a novel modification of the N-terminus of histidine-tagged proteins expressed in bacteria
    • Yan, Z., G. W. Caldwell, P. A. McDonell, W. J. Jones, A. August, and J. A. Masucci. 1999. Mass spectrometry determination of a novel modification of the N-terminus of histidine-tagged proteins expressed in bacteria. Biochem. Biophys. Res. Commun. 259:271-282.
    • (1999) Biochem. Biophys. Res. Commun , vol.259 , pp. 271-282
    • Yan, Z.1    Caldwell, G.W.2    McDonell, P.A.3    Jones, W.J.4    August, A.5    Masucci, J.A.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.