메뉴 건너뛰기




Volumn 32, Issue , 2015, Pages 55-65

Metabolic engineering of Escherichia coli for the production of phenylpyruvate derivatives

Author keywords

Escherichia coli; Phenylglycine; Phenylpropanoids; Phenylpyruvate; Styrene; Synthetic biology

Indexed keywords

AMINO ACIDS; ESCHERICHIA COLI; METABOLISM; STYRENE;

EID: 84942616025     PISSN: 10967176     EISSN: 10967184     Source Type: Journal    
DOI: 10.1016/j.ymben.2015.09.007     Document Type: Review
Times cited : (31)

References (136)
  • 4
    • 0031990783 scopus 로고    scopus 로고
    • 4-Coumarate: coenzyme A ligase in hybrid poplar properties of native enzymes, cDNA cloning, and analysis of recombinant enzymes
    • Allina S.M., Pri-Hadash A., Theilmann D.A., Ellis B.E., Douglas C.J. 4-Coumarate: coenzyme A ligase in hybrid poplar properties of native enzymes, cDNA cloning, and analysis of recombinant enzymes. Plant Physiol. 1998, 116:743-754.
    • (1998) Plant Physiol. , vol.116 , pp. 743-754
    • Allina, S.M.1    Pri-Hadash, A.2    Theilmann, D.A.3    Ellis, B.E.4    Douglas, C.J.5
  • 5
    • 77950920131 scopus 로고    scopus 로고
    • Production of novel antioxidative phenolic amides through heterologous expression of the plant's chlorogenic acid biosynthesis genes in yeast
    • Andrea M., Cinzia C., Sergio L., van Beek Teris A., Luca G., Francesco R.S., Jules B. Production of novel antioxidative phenolic amides through heterologous expression of the plant's chlorogenic acid biosynthesis genes in yeast. Metab. Eng. 2010, 12:223-232.
    • (2010) Metab. Eng. , vol.12 , pp. 223-232
    • Andrea, M.1    Cinzia, C.2    Sergio, L.3    van Beek Teris, A.4    Luca, G.5    Francesco, R.S.6    Jules, B.7
  • 6
    • 0028083417 scopus 로고
    • Structural and catalytic properties of the four phenylalanine ammonia-lyase isoenzymes from parsley (Petroselinum crispum Nym.)
    • Appert C., Logemann E., Hahlbrock K., Schmid J., Amrhein N. Structural and catalytic properties of the four phenylalanine ammonia-lyase isoenzymes from parsley (Petroselinum crispum Nym.). Eur. J. Biochem. 1994, 225:491-499.
    • (1994) Eur. J. Biochem. , vol.225 , pp. 491-499
    • Appert, C.1    Logemann, E.2    Hahlbrock, K.3    Schmid, J.4    Amrhein, N.5
  • 9
    • 4344573757 scopus 로고    scopus 로고
    • Metabolic engineering and protein directed evolution increase the yield of L-phenylalanine synthesized from glucose in Escherichia coli
    • Baez-Viveros J.L., Osuna J., Hernandez-Chavez G., Soberon X., Bolivar F., Gosset G. Metabolic engineering and protein directed evolution increase the yield of L-phenylalanine synthesized from glucose in Escherichia coli. Biotechnol. Bioeng. 2004, 87:516-524.
    • (2004) Biotechnol. Bioeng. , vol.87 , pp. 516-524
    • Baez-Viveros, J.L.1    Osuna, J.2    Hernandez-Chavez, G.3    Soberon, X.4    Bolivar, F.5    Gosset, G.6
  • 10
    • 0034461483 scopus 로고    scopus 로고
    • Inducible metabolism of phenolic acids in Pediococcus pentosaceus is encoded by an autoregulated operon which involves a new class of negative transcriptional regulator
    • Barthelmebs L., Lecomte B., Divies C., Cavin J.-F. Inducible metabolism of phenolic acids in Pediococcus pentosaceus is encoded by an autoregulated operon which involves a new class of negative transcriptional regulator. J. Bacteriol. 2000, 182:6724-6731.
    • (2000) J. Bacteriol. , vol.182 , pp. 6724-6731
    • Barthelmebs, L.1    Lecomte, B.2    Divies, C.3    Cavin, J.-F.4
  • 12
    • 2142816910 scopus 로고
    • Involvement of kinases in glucose and fructose uptake by Saccharomyces cerevisiae
    • Bisson L.F., Fraenkel D.G. Involvement of kinases in glucose and fructose uptake by Saccharomyces cerevisiae. Proc. Natl. Acad. Sci. USA 1983, 80:1730-1734.
    • (1983) Proc. Natl. Acad. Sci. USA , vol.80 , pp. 1730-1734
    • Bisson, L.F.1    Fraenkel, D.G.2
  • 13
    • 0030953385 scopus 로고    scopus 로고
    • The molecular genetics of hexose transport in yeasts
    • Boles E., Hollenberg C.P. The molecular genetics of hexose transport in yeasts. FEMS Microbiol. Rev. 1997, 21:85-111.
    • (1997) FEMS Microbiol. Rev. , vol.21 , pp. 85-111
    • Boles, E.1    Hollenberg, C.P.2
  • 14
    • 0035209901 scopus 로고    scopus 로고
    • Metabolic engineering for microbial production of aromatic amino acids and derived compounds
    • Bongaerts J., Kramer M., Muller U., Raeven L., Wubbolts M. Metabolic engineering for microbial production of aromatic amino acids and derived compounds. Metab. Eng. 2001, 3:289-300.
    • (2001) Metab. Eng. , vol.3 , pp. 289-300
    • Bongaerts, J.1    Kramer, M.2    Muller, U.3    Raeven, L.4    Wubbolts, M.5
  • 15
    • 84859768457 scopus 로고    scopus 로고
    • Parts plus pipes: synthetic biology approaches to metabolic engineering
    • Boyle P.M., Silver P.A. Parts plus pipes: synthetic biology approaches to metabolic engineering. Metab. Eng. 2012, 14:223-232.
    • (2012) Metab. Eng. , vol.14 , pp. 223-232
    • Boyle, P.M.1    Silver, P.A.2
  • 16
    • 0026012220 scopus 로고
    • Aromatic amino acid biosynthesis in the yeast Saccharomyces cerevisiae: a model system for the regulation of a eukaryotic biosynthetic pathway
    • Braus G.H. Aromatic amino acid biosynthesis in the yeast Saccharomyces cerevisiae: a model system for the regulation of a eukaryotic biosynthetic pathway. Microbiol. Rev. 1991, 55:349-370.
    • (1991) Microbiol. Rev. , vol.55 , pp. 349-370
    • Braus, G.H.1
  • 17
    • 84872151612 scopus 로고    scopus 로고
    • Metabolic engineering of the flavone-C-glycoside pathway using polyprotein technology
    • Brazier-Hicks M., Edwards R. Metabolic engineering of the flavone-C-glycoside pathway using polyprotein technology. Metab. Eng. 2013, 16:11-20.
    • (2013) Metab. Eng. , vol.16 , pp. 11-20
    • Brazier-Hicks, M.1    Edwards, R.2
  • 18
    • 84887997172 scopus 로고    scopus 로고
    • Metabolic engineering of Escherichia coli: a sustainable industrial platform for bio-based chemical production
    • Chen X., Zhou L., Tian K., Kumar A., Singh S., Prior B.A., Wang Z. Metabolic engineering of Escherichia coli: a sustainable industrial platform for bio-based chemical production. Biotechnol. Adv. 2013, 31:1200-1223.
    • (2013) Biotechnol. Adv. , vol.31 , pp. 1200-1223
    • Chen, X.1    Zhou, L.2    Tian, K.3    Kumar, A.4    Singh, S.5    Prior, B.A.6    Wang, Z.7
  • 20
    • 0034616852 scopus 로고    scopus 로고
    • Biosynthesis of the vancomycin group of antibiotics: involvement of an unusual dioxygenase in the pathway to (s)-4-hydroxyphenylglycine
    • Choroba O.W., Williams D.H., Spencer J.B. Biosynthesis of the vancomycin group of antibiotics: involvement of an unusual dioxygenase in the pathway to (s)-4-hydroxyphenylglycine. J. Am. Chem. Soc. 2000, 122:5389-5390.
    • (2000) J. Am. Chem. Soc. , vol.122 , pp. 5389-5390
    • Choroba, O.W.1    Williams, D.H.2    Spencer, J.B.3
  • 21
    • 3242743829 scopus 로고    scopus 로고
    • The Arabidopsis phenylalanine ammonia lyase gene family: kinetic characterization of the four PAL isoforms
    • Cochrane F.C., Davin L.B., Lewis N.G. The Arabidopsis phenylalanine ammonia lyase gene family: kinetic characterization of the four PAL isoforms. Phytochemistry 2004, 65:1557-1564.
    • (2004) Phytochemistry , vol.65 , pp. 1557-1564
    • Cochrane, F.C.1    Davin, L.B.2    Lewis, N.G.3
  • 22
    • 0022483540 scopus 로고
    • Purification and properties of shikimate kinase II from Escherichia coli K-12
    • DeFeyter R.C., Pittard J. Purification and properties of shikimate kinase II from Escherichia coli K-12. J. Bacteriol. 1986, 165:331-333.
    • (1986) J. Bacteriol. , vol.165 , pp. 331-333
    • DeFeyter, R.C.1    Pittard, J.2
  • 23
    • 0242424115 scopus 로고    scopus 로고
    • A transient intermediate in the reaction catalyzed by (S)-mandelate dehydrogenase from Pseudomonas putida
    • Dewanti A.R., Mitra B. A transient intermediate in the reaction catalyzed by (S)-mandelate dehydrogenase from Pseudomonas putida. Biochemistry 2003, 42:12893-12901.
    • (2003) Biochemistry , vol.42 , pp. 12893-12901
    • Dewanti, A.R.1    Mitra, B.2
  • 24
    • 4143117810 scopus 로고    scopus 로고
    • Role of glycine 81 in (S)-mandelate dehydrogenase from Pseudomonas putida in substrate specificity and oxidase activity
    • Dewanti A.R., Xu Y., Mitra B. Role of glycine 81 in (S)-mandelate dehydrogenase from Pseudomonas putida in substrate specificity and oxidase activity. Biochemistry 2004, 43:10692-10700.
    • (2004) Biochemistry , vol.43 , pp. 10692-10700
    • Dewanti, A.R.1    Xu, Y.2    Mitra, B.3
  • 25
    • 0032515892 scopus 로고    scopus 로고
    • Antimicrobial spectrum and target site of d-3-phenyllactic acid
    • Dieuleveux V., Lemarinier S., Guéguen M. Antimicrobial spectrum and target site of d-3-phenyllactic acid. Int. J. Food Microbiol. 1998, 40:177-183.
    • (1998) Int. J. Food Microbiol. , vol.40 , pp. 177-183
    • Dieuleveux, V.1    Lemarinier, S.2    Guéguen, M.3
  • 28
    • 0030157380 scopus 로고    scopus 로고
    • Phenylpropanoid metabolism and lignin biosynthesis: from weeds to trees
    • Douglas C.J. Phenylpropanoid metabolism and lignin biosynthesis: from weeds to trees. Trends Plant. Sci. 1996, 1:171-178.
    • (1996) Trends Plant. Sci. , vol.1 , pp. 171-178
    • Douglas, C.J.1
  • 30
    • 84867322381 scopus 로고    scopus 로고
    • Current knowledge of the Escherichia coli phosphoenolpyruvate-carbohydrate phosphotransferase system: peculiarities of regulation and impact on growth and product formation
    • Escalante A., Cervantes A.S., Gosset G., Bolívar F. Current knowledge of the Escherichia coli phosphoenolpyruvate-carbohydrate phosphotransferase system: peculiarities of regulation and impact on growth and product formation. Appl. Microbiol. Biotechnol. 2012, 94:1483-1494.
    • (2012) Appl. Microbiol. Biotechnol. , vol.94 , pp. 1483-1494
    • Escalante, A.1    Cervantes, A.S.2    Gosset, G.3    Bolívar, F.4
  • 31
    • 0036372095 scopus 로고    scopus 로고
    • Hydroxycinnamic acid amide metabolism: physiology and biochemistry
    • Facchini P.J., Hagel J., Zulak K.G. Hydroxycinnamic acid amide metabolism: physiology and biochemistry. Can. J. Bot. 2002, 80:577-589.
    • (2002) Can. J. Bot. , vol.80 , pp. 577-589
    • Facchini, P.J.1    Hagel, J.2    Zulak, K.G.3
  • 32
    • 0038819942 scopus 로고    scopus 로고
    • In vivo imaging of the dynamics of glucose uptake in the cytosol of COS-7 cells by fluorescent nanosensors
    • Fehr M., Lalonde S., Lager I., Wolff M.W., Frommer W.B. In vivo imaging of the dynamics of glucose uptake in the cytosol of COS-7 cells by fluorescent nanosensors. J. Biol. Chem. 2003, 278:19127-19133.
    • (2003) J. Biol. Chem. , vol.278 , pp. 19127-19133
    • Fehr, M.1    Lalonde, S.2    Lager, I.3    Wolff, M.W.4    Frommer, W.B.5
  • 33
    • 67650685038 scopus 로고    scopus 로고
    • Biosynthesis and biotechnological production of flavanones: current state and perspectives
    • Fowler Z.L., Koffas M.A. Biosynthesis and biotechnological production of flavanones: current state and perspectives. Appl. Microbiol. Biotechnol. 2009, 83:799-808.
    • (2009) Appl. Microbiol. Biotechnol. , vol.83 , pp. 799-808
    • Fowler, Z.L.1    Koffas, M.A.2
  • 34
    • 0028054686 scopus 로고
    • The fadD gene of Escherichia coli K12 is located close to rnd at 39.6min of the chromosomal-map and is a new member of the AMP-binding protein family
    • Fulda M., Heinz E., Wolter F.P. The fadD gene of Escherichia coli K12 is located close to rnd at 39.6min of the chromosomal-map and is a new member of the AMP-binding protein family. Mol. Gen. Genet. 1994, 242:241-249.
    • (1994) Mol. Gen. Genet. , vol.242 , pp. 241-249
    • Fulda, M.1    Heinz, E.2    Wolter, F.P.3
  • 35
    • 26844512919 scopus 로고    scopus 로고
    • Improvement of Escherichia coli production strains by modification of the phosphoenolpyruvate:sugar phosphotransferase system
    • Gosset G. Improvement of Escherichia coli production strains by modification of the phosphoenolpyruvate:sugar phosphotransferase system. Microb. Cell Fact. 2005, 4:14.
    • (2005) Microb. Cell Fact. , vol.4 , pp. 14
    • Gosset, G.1
  • 36
    • 0037413687 scopus 로고    scopus 로고
    • Directed evolution of an extremely fast phosphotriesterase by in vitro compartmentalization
    • Griffiths A.D., Tawfik D.S. Directed evolution of an extremely fast phosphotriesterase by in vitro compartmentalization. Embo J. 2003, 22:24-35.
    • (2003) Embo J. , vol.22 , pp. 24-35
    • Griffiths, A.D.1    Tawfik, D.S.2
  • 37
    • 80053581937 scopus 로고    scopus 로고
    • Functional characterization of evolutionarily divergent 4-coumarate: coenzyme A ligases in rice
    • Gui J., Shen J., Li L. Functional characterization of evolutionarily divergent 4-coumarate: coenzyme A ligases in rice. Plant Physiol. 2011, 157:574-586.
    • (2011) Plant Physiol. , vol.157 , pp. 574-586
    • Gui, J.1    Shen, J.2    Li, L.3
  • 39
    • 78650804716 scopus 로고    scopus 로고
    • Expression of aspartic protease from Neurospora crassa in industrial ethanol-producing yeast and its application in ethanol production
    • Guo Z.P., Qiu C.Y., Zhang L., Ding Z.Y., Wang Z.X., Shi G.Y. Expression of aspartic protease from Neurospora crassa in industrial ethanol-producing yeast and its application in ethanol production. Enzyme Microb. Technol. 2011, 48:148-154.
    • (2011) Enzyme Microb. Technol. , vol.48 , pp. 148-154
    • Guo, Z.P.1    Qiu, C.Y.2    Zhang, L.3    Ding, Z.Y.4    Wang, Z.X.5    Shi, G.Y.6
  • 40
    • 78649800037 scopus 로고    scopus 로고
    • Improving the performance of industrial ethanol-producing yeast by expressing the aspartyl protease on the cell surface
    • Guo Z.P., Zhang L., Ding Z.Y., Wang Z.X., Shi G.Y. Improving the performance of industrial ethanol-producing yeast by expressing the aspartyl protease on the cell surface. Yeast 2010, 27:1017-1027.
    • (2010) Yeast , vol.27 , pp. 1017-1027
    • Guo, Z.P.1    Zhang, L.2    Ding, Z.Y.3    Wang, Z.X.4    Shi, G.Y.5
  • 41
    • 1242296765 scopus 로고    scopus 로고
    • The 4-coumarate: CoA ligase gene family in Arabidopsis thaliana comprises one rare, sinapate-activating and three commonly occurring isoenzymes
    • Hamberger B., Hahlbrock K. The 4-coumarate: CoA ligase gene family in Arabidopsis thaliana comprises one rare, sinapate-activating and three commonly occurring isoenzymes. Proc. Natl. Acad. Sci. USA 2004, 101:2209-2214.
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 2209-2214
    • Hamberger, B.1    Hahlbrock, K.2
  • 43
    • 22244465913 scopus 로고    scopus 로고
    • Evolution of 3-deoxy-D-arabino-heptulosonate-7-phosphate synthase-encoding genes in the yeast Saccharomyces cerevisiae
    • Helmstaedt K., Strittmatter A., Lipscomb W.N., Braus G.H. Evolution of 3-deoxy-D-arabino-heptulosonate-7-phosphate synthase-encoding genes in the yeast Saccharomyces cerevisiae. Proc. Natl. Acad. Sci. USA 2005, 102:9784-9789.
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 9784-9789
    • Helmstaedt, K.1    Strittmatter, A.2    Lipscomb, W.N.3    Braus, G.H.4
  • 44
    • 83255164998 scopus 로고    scopus 로고
    • Cell-free synthetic biology: thinking outside the cell
    • Hodgman C.E., Jewett M.C. Cell-free synthetic biology: thinking outside the cell. Metab. Eng. 2012, 14:261-269.
    • (2012) Metab. Eng. , vol.14 , pp. 261-269
    • Hodgman, C.E.1    Jewett, M.C.2
  • 46
    • 0028786298 scopus 로고
    • 450 proteins as translational fusions with P450 reductase in Escherichia coli
    • 450 proteins as translational fusions with P450 reductase in Escherichia coli. FEBS Lett. 1995, 374:345-350.
    • (1995) FEBS Lett. , vol.374 , pp. 345-350
    • Hotze, M.1    Schröder, G.2    Schröder, J.3
  • 47
    • 78049459077 scopus 로고    scopus 로고
    • Crystal structures of a Populus tomentosa 4-coumarate: CoA ligase shed light on its enzymatic mechanisms
    • Hu Y., Gai Y., Yin L., Wang X., Feng C., Feng L., Li D., Jiang X.-N., Wang D.-C. Crystal structures of a Populus tomentosa 4-coumarate: CoA ligase shed light on its enzymatic mechanisms. Plant Cell Online 2010, 22:3093-3104.
    • (2010) Plant Cell Online , vol.22 , pp. 3093-3104
    • Hu, Y.1    Gai, Y.2    Yin, L.3    Wang, X.4    Feng, C.5    Feng, L.6    Li, D.7    Jiang, X.-N.8    Wang, D.-C.9
  • 48
    • 77954293821 scopus 로고    scopus 로고
    • Enhanced 2-phenylethanol production from L-phenylalanine via in situ product adsorption
    • Hua D., Lin S., Li Y., Chen H., Zhang Z., Du Y., Zhang X., Xu P. Enhanced 2-phenylethanol production from L-phenylalanine via in situ product adsorption. Biocatal. Biotransform. 2010, 28:259-266.
    • (2010) Biocatal. Biotransform. , vol.28 , pp. 259-266
    • Hua, D.1    Lin, S.2    Li, Y.3    Chen, H.4    Zhang, Z.5    Du, Y.6    Zhang, X.7    Xu, P.8
  • 49
    • 0034523992 scopus 로고    scopus 로고
    • Biosynthesis of L-p-hydroxyphenylglycine, a non-proteinogenic amino acid constituent of peptide antibiotics
    • Hubbard B.K., Thomas M.G., Walsh C.T. Biosynthesis of L-p-hydroxyphenylglycine, a non-proteinogenic amino acid constituent of peptide antibiotics. Chem. Biol. 2000, 7:931-942.
    • (2000) Chem. Biol. , vol.7 , pp. 931-942
    • Hubbard, B.K.1    Thomas, M.G.2    Walsh, C.T.3
  • 50
    • 20444422841 scopus 로고    scopus 로고
    • Metabolic engineering of the phenylpropanoid pathway in Saccharomyces cerevisiae
    • Jiang H., Wood K.V., Morgan J.A. Metabolic engineering of the phenylpropanoid pathway in Saccharomyces cerevisiae. Appl. Environ. Microbiol. 2005, 71:2962-2969.
    • (2005) Appl. Environ. Microbiol. , vol.71 , pp. 2962-2969
    • Jiang, H.1    Wood, K.V.2    Morgan, J.A.3
  • 51
    • 0035822553 scopus 로고    scopus 로고
    • Characterization of a new feedback-resistant 3-deoxy-D-arabino-heptulosonate 7-phosphate synthase AroF of Escherichia coli
    • Jossek R., Bongaerts J., Sprenger G.A. Characterization of a new feedback-resistant 3-deoxy-D-arabino-heptulosonate 7-phosphate synthase AroF of Escherichia coli. FEMS Microbiol. Lett. 2001, 202:145-148.
    • (2001) FEMS Microbiol. Lett. , vol.202 , pp. 145-148
    • Jossek, R.1    Bongaerts, J.2    Sprenger, G.A.3
  • 52
    • 55549141496 scopus 로고    scopus 로고
    • Production of phenylpropanoid amides in recombinant Escherichia coli
    • Kang K., Back K. Production of phenylpropanoid amides in recombinant Escherichia coli. Metab. Eng. 2009, 11:64-68.
    • (2009) Metab. Eng. , vol.11 , pp. 64-68
    • Kang, K.1    Back, K.2
  • 53
    • 63049124712 scopus 로고    scopus 로고
    • Ectopic expression of serotonin N-hydroxycinnamoyltransferase and differential production of phenylpropanoid amides in transgenic tomato tissues
    • Kang K., Lee K., Sohn S.-O., Park S., Lee S., Kim S.Y., Kim Y.S., Back K. Ectopic expression of serotonin N-hydroxycinnamoyltransferase and differential production of phenylpropanoid amides in transgenic tomato tissues. Sci. Hortic. 2009, 120:504-510.
    • (2009) Sci. Hortic. , vol.120 , pp. 504-510
    • Kang, K.1    Lee, K.2    Sohn, S.-O.3    Park, S.4    Lee, S.5    Kim, S.Y.6    Kim, Y.S.7    Back, K.8
  • 54
    • 33646075412 scopus 로고    scopus 로고
    • Enriched production of N-hydroxycinnamic acid amides and biogenic amines in pepper (Capsicum annuum) flowers
    • Kang S., Back K. Enriched production of N-hydroxycinnamic acid amides and biogenic amines in pepper (Capsicum annuum) flowers. Sci. Hortic. 2006, 108:337-341.
    • (2006) Sci. Hortic. , vol.108 , pp. 337-341
    • Kang, S.1    Back, K.2
  • 55
    • 84859772410 scopus 로고    scopus 로고
    • Synthetic biology and the development of tools for metabolic engineering
    • Keasling J.D. Synthetic biology and the development of tools for metabolic engineering. Metab. Eng. 2012, 14:189-195.
    • (2012) Metab. Eng. , vol.14 , pp. 189-195
    • Keasling, J.D.1
  • 56
    • 84865987785 scopus 로고    scopus 로고
    • Substrate channelling
    • Khan D. Substrate channelling. Resonance 2012, 17:791-796.
    • (2012) Resonance , vol.17 , pp. 791-796
    • Khan, D.1
  • 57
    • 0031001311 scopus 로고    scopus 로고
    • Mutational analysis of the feedback sites of phenylalanine-sensitive 3-deoxy-D-arabino-heptulosonate-7-phosphate synthase of Escherichia coli
    • Kikuchi Y., Tsujimoto K., Kurahashi O. Mutational analysis of the feedback sites of phenylalanine-sensitive 3-deoxy-D-arabino-heptulosonate-7-phosphate synthase of Escherichia coli. Appl. Environ. Microbiol. 1997, 63:761-762.
    • (1997) Appl. Environ. Microbiol. , vol.63 , pp. 761-762
    • Kikuchi, Y.1    Tsujimoto, K.2    Kurahashi, O.3
  • 58
    • 84866285573 scopus 로고    scopus 로고
    • Production of aromatic compounds by metabolically engineered Escherichia coli with an expanded shikimate pathway
    • Koma D., Yamanaka H., Moriyoshi K., Ohmoto T., Sakai K. Production of aromatic compounds by metabolically engineered Escherichia coli with an expanded shikimate pathway. Appl Environ. Microbiol. 2012, 78:6203-6216.
    • (2012) Appl Environ. Microbiol. , vol.78 , pp. 6203-6216
    • Koma, D.1    Yamanaka, H.2    Moriyoshi, K.3    Ohmoto, T.4    Sakai, K.5
  • 59
    • 0025860534 scopus 로고
    • Physiologically motivated strategies for control of the fed-batch cultivation of recombinant Escherichia coli for phenylalanine production
    • Konstantinov K.B., Nishio N., Seki T., Yoshida T. Physiologically motivated strategies for control of the fed-batch cultivation of recombinant Escherichia coli for phenylalanine production. J. Ferment. Bioeng. 1991, 71:350-355.
    • (1991) J. Ferment. Bioeng. , vol.71 , pp. 350-355
    • Konstantinov, K.B.1    Nishio, N.2    Seki, T.3    Yoshida, T.4
  • 62
    • 39849084210 scopus 로고    scopus 로고
    • Combinatorial pathway analysis for improved L-tyrosine production in Escherichia coli: identification of enzymatic bottlenecks by systematic gene overexpression
    • Lütke-Eversloh T., Stephanopoulos G. Combinatorial pathway analysis for improved L-tyrosine production in Escherichia coli: identification of enzymatic bottlenecks by systematic gene overexpression. Metab. Eng. 2008, 10:69-77.
    • (2008) Metab. Eng. , vol.10 , pp. 69-77
    • Lütke-Eversloh, T.1    Stephanopoulos, G.2
  • 63
    • 84859780045 scopus 로고    scopus 로고
    • Spatial organization of enzymes for metabolic engineering
    • Lee H., DeLoache W.C., Dueber J.E. Spatial organization of enzymes for metabolic engineering. Metab. Eng. 2012, 14:242-251.
    • (2012) Metab. Eng. , vol.14 , pp. 242-251
    • Lee, H.1    DeLoache, W.C.2    Dueber, J.E.3
  • 64
    • 34250849659 scopus 로고    scopus 로고
    • Engineering central metabolic pathways for high-level flavonoid production in Escherichia coli
    • Leonard E., Lim K.-H., Saw P.-N., Koffas M.A. Engineering central metabolic pathways for high-level flavonoid production in Escherichia coli. Appl. Environ. Microb. 2007, 73:3877-3886.
    • (2007) Appl. Environ. Microb. , vol.73 , pp. 3877-3886
    • Leonard, E.1    Lim, K.-H.2    Saw, P.-N.3    Koffas, M.A.4
  • 65
    • 33644816925 scopus 로고    scopus 로고
    • Functional expression of a P450 flavonoid hydroxylase for the biosynthesis of plant-specific hydroxylated flavonols in Escherichia coli
    • Leonard E., Yan Y., Koffas M.A. Functional expression of a P450 flavonoid hydroxylase for the biosynthesis of plant-specific hydroxylated flavonols in Escherichia coli. Metab. Eng. 2006, 8:172-181.
    • (2006) Metab. Eng. , vol.8 , pp. 172-181
    • Leonard, E.1    Yan, Y.2    Koffas, M.A.3
  • 66
    • 84876281017 scopus 로고    scopus 로고
    • Purification, characterization and cloning of a thermotolerant isoamylase produced from Bacillus sp. CICIM 304
    • Li Y., Niu D., Zhang L., Wang Z., Shi G. Purification, characterization and cloning of a thermotolerant isoamylase produced from Bacillus sp. CICIM 304. J. Ind. Microbiol. Biotechnol. 2013, 40:437-446.
    • (2013) J. Ind. Microbiol. Biotechnol. , vol.40 , pp. 437-446
    • Li, Y.1    Niu, D.2    Zhang, L.3    Wang, Z.4    Shi, G.5
  • 67
    • 84868599824 scopus 로고    scopus 로고
    • Cloning, expression, characterization, and biocatalytic investigation of a novel bacilli thermostable type I pullulanase from Bacillus sp. CICIM 263
    • Li Y., Zhang L., Niu D., Wang Z., Shi G. Cloning, expression, characterization, and biocatalytic investigation of a novel bacilli thermostable type I pullulanase from Bacillus sp. CICIM 263. J. Agric. Food Chem. 2012, 60:11164-11172.
    • (2012) J. Agric. Food Chem. , vol.60 , pp. 11164-11172
    • Li, Y.1    Zhang, L.2    Niu, D.3    Wang, Z.4    Shi, G.5
  • 69
    • 84942572201 scopus 로고    scopus 로고
    • Screening, characterization and utilization of D-amino acid aminotransferase to obtain D-phenylalanine
    • Liu R.X., Liu S.P., Cheng S., Zhang L., Ding Z.Y., Gu Z.H., Shi G.Y. Screening, characterization and utilization of D-amino acid aminotransferase to obtain D-phenylalanine. Appl. Biochem. Microbiol.+ 2015, 51:695-703.
    • (2015) Appl. Biochem. Microbiol.+ , vol.51 , pp. 695-703
    • Liu, R.X.1    Liu, S.P.2    Cheng, S.3    Zhang, L.4    Ding, Z.Y.5    Gu, Z.H.6    Shi, G.Y.7
  • 70
    • 84898455322 scopus 로고    scopus 로고
    • A systems level engineered E. coli capable of efficiently producing L-phenylalanine
    • Liu S.P., Liu R.X., Xiao M.R., Zhang L., Ding Z.Y., Gu Z.H., Shi G.Y. A systems level engineered E. coli capable of efficiently producing L-phenylalanine. Process Biochem. 2014, 49:751-757.
    • (2014) Process Biochem. , vol.49 , pp. 751-757
    • Liu, S.P.1    Liu, R.X.2    Xiao, M.R.3    Zhang, L.4    Ding, Z.Y.5    Gu, Z.H.6    Shi, G.Y.7
  • 71
    • 84875892911 scopus 로고    scopus 로고
    • Production of L-phenylalanine from glucose by metabolic engineering of wild type Escherichia coli W3110
    • Liu S.P., Xiao M.R., Zhang L., Xu J., Ding Z.Y., Gu Z.H., Shi G.Y. Production of L-phenylalanine from glucose by metabolic engineering of wild type Escherichia coli W3110. Process Biochem. 2013, 48:413-419.
    • (2013) Process Biochem. , vol.48 , pp. 413-419
    • Liu, S.P.1    Xiao, M.R.2    Zhang, L.3    Xu, J.4    Ding, Z.Y.5    Gu, Z.H.6    Shi, G.Y.7
  • 73
    • 84919625013 scopus 로고    scopus 로고
    • Sequence-based screening and characterization of cytosolic mandelate oxidase using oxygen as electron acceptor
    • Liu S.P., Liu R.X., Zhang L., Shi G.Y. Sequence-based screening and characterization of cytosolic mandelate oxidase using oxygen as electron acceptor. Enzyme Microb. Technol. 2015, 69:24-30.
    • (2015) Enzyme Microb. Technol. , vol.69 , pp. 24-30
    • Liu, S.P.1    Liu, R.X.2    Zhang, L.3    Shi, G.Y.4
  • 74
    • 44749095048 scopus 로고    scopus 로고
    • Alleviation of feedback inhibition in Saccharomyces cerevisiae aromatic amino acid biosynthesis: quantification of metabolic impact
    • Luttik M.A., Vuralhan Z., Suir E., Braus G.H., Pronk J.T., Daran J.M. Alleviation of feedback inhibition in Saccharomyces cerevisiae aromatic amino acid biosynthesis: quantification of metabolic impact. Metab. Eng. 2008, 10:141-153.
    • (2008) Metab. Eng. , vol.10 , pp. 141-153
    • Luttik, M.A.1    Vuralhan, Z.2    Suir, E.3    Braus, G.H.4    Pronk, J.T.5    Daran, J.M.6
  • 75
    • 79961206960 scopus 로고    scopus 로고
    • Identification and functional characterization of phenylglycine biosynthetic genes involved in pristinamycin biosynthesis in Streptomyces pristinaespiralis
    • Mast Y.J., Wohlleben W., Schinko E. Identification and functional characterization of phenylglycine biosynthetic genes involved in pristinamycin biosynthesis in Streptomyces pristinaespiralis. J. Biotechnol. 2011, 155:63-67.
    • (2011) J. Biotechnol. , vol.155 , pp. 63-67
    • Mast, Y.J.1    Wohlleben, W.2    Schinko, E.3
  • 76
    • 31144436098 scopus 로고    scopus 로고
    • Synthesis and biological evaluation of a series of flavone derivatives as potential radioligands for imaging the multidrug resistance-associated protein 1 (ABCC1/MRP1)
    • Mavel S., Dikic B., Palakas S., Emond P., Greguric I., de Gracia A.G., Mattner F., Garrigos M., Guilloteau D., Katsifis A. Synthesis and biological evaluation of a series of flavone derivatives as potential radioligands for imaging the multidrug resistance-associated protein 1 (ABCC1/MRP1). Bioorgan. Med. Chem. 2006, 14:1599-1607.
    • (2006) Bioorgan. Med. Chem. , vol.14 , pp. 1599-1607
    • Mavel, S.1    Dikic, B.2    Palakas, S.3    Emond, P.4    Greguric, I.5    de Gracia, A.G.6    Mattner, F.7    Garrigos, M.8    Guilloteau, D.9    Katsifis, A.10
  • 77
    • 0030943846 scopus 로고    scopus 로고
    • Asparagine 394 in putative helix 11 of the galactose-H+ symport protein (GalP) from Escherichia coli is associated with the internal binding site for cytochalasin B and sugar
    • McDonald T.P., Walmsley A.R., Henderson P.J. Asparagine 394 in putative helix 11 of the galactose-H+ symport protein (GalP) from Escherichia coli is associated with the internal binding site for cytochalasin B and sugar. J. Biol. Chem. 1997, 272:15189-15199.
    • (1997) J. Biol. Chem. , vol.272 , pp. 15189-15199
    • McDonald, T.P.1    Walmsley, A.R.2    Henderson, P.J.3
  • 78
    • 80052027792 scopus 로고    scopus 로고
    • Styrene biosynthesis from glucose by engineered E. coli
    • McKenna R., Nielsen D.R. Styrene biosynthesis from glucose by engineered E. coli. Metab. Eng. 2011, 13:544-554.
    • (2011) Metab. Eng. , vol.13 , pp. 544-554
    • McKenna, R.1    Nielsen, D.R.2
  • 79
    • 84857050180 scopus 로고    scopus 로고
    • Applications of genetically-encoded biosensors for the construction and control of biosynthetic pathways
    • Michener J.K., Thodey K., Liang J.C., Smolke C.D. Applications of genetically-encoded biosensors for the construction and control of biosynthetic pathways. Metab. Eng. 2012, 14:212-222.
    • (2012) Metab. Eng. , vol.14 , pp. 212-222
    • Michener, J.K.1    Thodey, K.2    Liang, J.C.3    Smolke, C.D.4
  • 80
    • 0033617187 scopus 로고    scopus 로고
    • The molecular basis of substrate channeling
    • Miles E.W., Rhee S., Davies D.R. The molecular basis of substrate channeling. J. Biol. Chem. 1999, 274:12193-12196.
    • (1999) J. Biol. Chem. , vol.274 , pp. 12193-12196
    • Miles, E.W.1    Rhee, S.2    Davies, D.R.3
  • 82
    • 48249104039 scopus 로고    scopus 로고
    • Riboswitches: emerging themes in RNA structure and function
    • Montange R.K., Batey R.T. Riboswitches: emerging themes in RNA structure and function. Annu. Rev. Biophys. 2008, 37:117-133.
    • (2008) Annu. Rev. Biophys. , vol.37 , pp. 117-133
    • Montange, R.K.1    Batey, R.T.2
  • 84
    • 79952669657 scopus 로고    scopus 로고
    • Crystallization and preliminary X-ray analysis of 4-coumarate: CoA ligase from Arabidopsis thaliana
    • Morita H., Mori T., Wanibuchi K., Kato R., Sugio S., Abe I. Crystallization and preliminary X-ray analysis of 4-coumarate: CoA ligase from Arabidopsis thaliana. Acta. Crystallogr. F 2011, 67:409-411.
    • (2011) Acta. Crystallogr. F , vol.67 , pp. 409-411
    • Morita, H.1    Mori, T.2    Wanibuchi, K.3    Kato, R.4    Sugio, S.5    Abe, I.6
  • 87
    • 31544449418 scopus 로고    scopus 로고
    • Heterologous production of epothilone C and D in Escherichia coli
    • Mutka S.C., Carney J.R., Liu Y., Kennedy J. Heterologous production of epothilone C and D in Escherichia coli. Biochemistry 2006, 45:1321-1330.
    • (2006) Biochemistry , vol.45 , pp. 1321-1330
    • Mutka, S.C.1    Carney, J.R.2    Liu, Y.3    Kennedy, J.4
  • 88
    • 0026643267 scopus 로고
    • Novel mutations in the pheA gene of Escherichia coli K-12 which result in highly feedback inhibition-resistant variants of chorismate mutase/prephenate dehydratase
    • Nelms J., Edwards R., Warwick J., Fotheringham I. Novel mutations in the pheA gene of Escherichia coli K-12 which result in highly feedback inhibition-resistant variants of chorismate mutase/prephenate dehydratase. Appl. Environ. Microb. 1992, 58:2592-2598.
    • (1992) Appl. Environ. Microb. , vol.58 , pp. 2592-2598
    • Nelms, J.1    Edwards, R.2    Warwick, J.3    Fotheringham, I.4
  • 89
    • 10044287191 scopus 로고    scopus 로고
    • Stimulation, monitoring, and analysis of pathway dynamics by metabolic profiling in the aromatic amino acid pathway
    • Oldiges M., Kunze M., Degenring D., Sprenger G., Takors R. Stimulation, monitoring, and analysis of pathway dynamics by metabolic profiling in the aromatic amino acid pathway. Biotechnol. Prog. 2004, 20:1623-1633.
    • (2004) Biotechnol. Prog. , vol.20 , pp. 1623-1633
    • Oldiges, M.1    Kunze, M.2    Degenring, D.3    Sprenger, G.4    Takors, R.5
  • 90
    • 0032865543 scopus 로고    scopus 로고
    • Function and regulation of yeast hexose transporters
    • Özcan S., Johnston M. Function and regulation of yeast hexose transporters. Microbiol. Mol. Biol. Rev. 1999, 63:554-569.
    • (1999) Microbiol. Mol. Biol. Rev. , vol.63 , pp. 554-569
    • Özcan, S.1    Johnston, M.2
  • 91
    • 77950906711 scopus 로고    scopus 로고
    • Synthesis of empty bacterial microcompartments, directed organelle protein incorporation, and evidence of filament-associated organelle movement
    • Parsons J.B., Frank S., Bhella D., Liang M., Prentice M.B., Mulvihill D.P., Warren M.J. Synthesis of empty bacterial microcompartments, directed organelle protein incorporation, and evidence of filament-associated organelle movement. Mol. Cell 2010, 38:305-315.
    • (2010) Mol. Cell , vol.38 , pp. 305-315
    • Parsons, J.B.1    Frank, S.2    Bhella, D.3    Liang, M.4    Prentice, M.B.5    Mulvihill, D.P.6    Warren, M.J.7
  • 92
    • 77952806661 scopus 로고    scopus 로고
    • Production and characterization of an antifungal compound (3-phenyllactic acid) produced by Lactobacillus plantarum strain
    • Prema P., Smila D., Palavesam A., Immanuel G. Production and characterization of an antifungal compound (3-phenyllactic acid) produced by Lactobacillus plantarum strain. Food Bioprocess. Technol. 2010, 3:379-386.
    • (2010) Food Bioprocess. Technol. , vol.3 , pp. 379-386
    • Prema, P.1    Smila, D.2    Palavesam, A.3    Immanuel, G.4
  • 93
    • 34249686497 scopus 로고    scopus 로고
    • Functional expression of prokaryotic and eukaryotic genes in Escherichia coli for conversion of glucose to p-hydroxystyrene
    • Qi W.W., Vannelli T., Breinig S., Ben-Bassat A., Gatenby A.A., Haynie S.L., Sariaslani F.S. Functional expression of prokaryotic and eukaryotic genes in Escherichia coli for conversion of glucose to p-hydroxystyrene. Metab. Eng. 2007, 9:268-276.
    • (2007) Metab. Eng. , vol.9 , pp. 268-276
    • Qi, W.W.1    Vannelli, T.2    Breinig, S.3    Ben-Bassat, A.4    Gatenby, A.A.5    Haynie, S.L.6    Sariaslani, F.S.7
  • 94
    • 0024255488 scopus 로고
    • Mutational analysis of the catalytic and feedback sites of the tryptophan-sensitive 3-deoxy-D-arabino-heptulosonate-7- phosphate synthase of Escherichia coli
    • Ray J.M., Yanofsky C., Bauerle R. Mutational analysis of the catalytic and feedback sites of the tryptophan-sensitive 3-deoxy-D-arabino-heptulosonate-7- phosphate synthase of Escherichia coli. . J. Bacteriol. 1988, 170:5500-5506.
    • (1988) . J. Bacteriol. , vol.170 , pp. 5500-5506
    • Ray, J.M.1    Yanofsky, C.2    Bauerle, R.3
  • 96
    • 1842287997 scopus 로고    scopus 로고
    • Maize phenylalanine ammonia-lyase has tyrosine ammonia-lyase activity
    • Rosler J., Krekel F., Amrhein N., Schmid J. Maize phenylalanine ammonia-lyase has tyrosine ammonia-lyase activity. Plant Physiol. 1997, 113:175-179.
    • (1997) Plant Physiol. , vol.113 , pp. 175-179
    • Rosler, J.1    Krekel, F.2    Amrhein, N.3    Schmid, J.4
  • 97
    • 3242892145 scopus 로고    scopus 로고
    • Fully integrated L-phenylalanine separation and concentration using reactive-extraction with liquid-liquid centrifuges in a fed-batch process with E. coli
    • Ruffer N., Heidersdorf U., Kretzers I., Sprenger G.A., Raeven L., Takors R. Fully integrated L-phenylalanine separation and concentration using reactive-extraction with liquid-liquid centrifuges in a fed-batch process with E. coli. Bioprocess Biosyst. Eng. 2004, 26:239-248.
    • (2004) Bioprocess Biosyst. Eng. , vol.26 , pp. 239-248
    • Ruffer, N.1    Heidersdorf, U.2    Kretzers, I.3    Sprenger, G.A.4    Raeven, L.5    Takors, R.6
  • 98
    • 70349964350 scopus 로고    scopus 로고
    • Automated design of synthetic ribosome binding sites to control protein expression
    • Salis H.M., Mirsky E.A., Voigt C.A. Automated design of synthetic ribosome binding sites to control protein expression. Nat. Biotechnol. 2009, 27:946-950.
    • (2009) Nat. Biotechnol. , vol.27 , pp. 946-950
    • Salis, H.M.1    Mirsky, E.A.2    Voigt, C.A.3
  • 99
    • 79958715193 scopus 로고    scopus 로고
    • Optimization of a heterologous pathway for the production of flavonoids from glucose
    • Santos C.N.S., Koffas M., Stephanopoulos G. Optimization of a heterologous pathway for the production of flavonoids from glucose. Metab. Eng. 2011, 13:392-400.
    • (2011) Metab. Eng. , vol.13 , pp. 392-400
    • Santos, C.N.S.1    Koffas, M.2    Stephanopoulos, G.3
  • 100
    • 35848961026 scopus 로고    scopus 로고
    • Development of a combined biological and chemical process for production of industrial aromatics from renewable resources
    • Sariaslani F.S. Development of a combined biological and chemical process for production of industrial aromatics from renewable resources. Annu. Rev. Microbiol. 2007, 61:51-69.
    • (2007) Annu. Rev. Microbiol. , vol.61 , pp. 51-69
    • Sariaslani, F.S.1
  • 101
    • 77749264485 scopus 로고    scopus 로고
    • Spatially ordered dynamics of the bacterial carbon fixation machinery
    • Savage D.F., Afonso B., Chen A.H., Silver P.A. Spatially ordered dynamics of the bacterial carbon fixation machinery. Science 2010, 327:1258-1261.
    • (2010) Science , vol.327 , pp. 1258-1261
    • Savage, D.F.1    Afonso, B.2    Chen, A.H.3    Silver, P.A.4
  • 104
    • 0033565448 scopus 로고    scopus 로고
    • Crystal structure of phenylalanine-regulated 3-deoxy-D-arabino-heptulosonate-7-phosphate synthase from Escherichia coli
    • Shumilin I.A., Kretsinger R.H., Bauerle R.H. Crystal structure of phenylalanine-regulated 3-deoxy-D-arabino-heptulosonate-7-phosphate synthase from Escherichia coli. Structure 1999, 7:865-875.
    • (1999) Structure , vol.7 , pp. 865-875
    • Shumilin, I.A.1    Kretsinger, R.H.2    Bauerle, R.H.3
  • 105
    • 0344631518 scopus 로고    scopus 로고
    • Substrate channeling
    • Spivey H.O., Ovádi J. Substrate channeling. Methods 1999, 19:306-321.
    • (1999) Methods , vol.19 , pp. 306-321
    • Spivey, H.O.1    Ovádi, J.2
  • 106
    • 34547435219 scopus 로고    scopus 로고
    • From scratch to value: engineering Escherichia coli wild type cells to the production of L-phenylalanine and other fine chemicals derived from chorismate
    • Sprenger G.A. From scratch to value: engineering Escherichia coli wild type cells to the production of L-phenylalanine and other fine chemicals derived from chorismate. Appl. Microbiol. Biotechnol. 2007, 75:739-749.
    • (2007) Appl. Microbiol. Biotechnol. , vol.75 , pp. 739-749
    • Sprenger, G.A.1
  • 107
    • 66249101973 scopus 로고    scopus 로고
    • Structures of the G81A mutant form of the active chimera of (S)-mandelate dehydrogenase and its complex with two of its substrates
    • Sukumar N., Dewanti A., Merli A., Rossi G.L., Mitra B., Mathews F.S. Structures of the G81A mutant form of the active chimera of (S)-mandelate dehydrogenase and its complex with two of its substrates. Acta Crystallogr. D 2009, 65:543-552.
    • (2009) Acta Crystallogr. D , vol.65 , pp. 543-552
    • Sukumar, N.1    Dewanti, A.2    Merli, A.3    Rossi, G.L.4    Mitra, B.5    Mathews, F.S.6
  • 108
    • 80052688691 scopus 로고    scopus 로고
    • Metabolic engineering of the L-phenylalanine pathway in Escherichia coli for the production of S- or R-mandelic acid
    • Sun Z., Ning Y., Liu L., Liu Y., Sun B., Jiang W., Yang C., Yang S. Metabolic engineering of the L-phenylalanine pathway in Escherichia coli for the production of S- or R-mandelic acid. Microb. Cell Fact. 2011, 10:71.
    • (2011) Microb. Cell Fact. , vol.10 , pp. 71
    • Sun, Z.1    Ning, Y.2    Liu, L.3    Liu, Y.4    Sun, B.5    Jiang, W.6    Yang, C.7    Yang, S.8
  • 109
    • 79251580632 scopus 로고    scopus 로고
    • Design and application of a mevalonate-responsive regulatory protein
    • Tang S.Y., Cirino P.C. Design and application of a mevalonate-responsive regulatory protein. Angew. Chem. Int. Ed. 2011, 50:1084-1086.
    • (2011) Angew. Chem. Int. Ed. , vol.50 , pp. 1084-1086
    • Tang, S.Y.1    Cirino, P.C.2
  • 110
    • 0024586605 scopus 로고
    • Thermostable D-amino acid aminotransferase from a thermophilic Bacillus species. Purification, characterization, and active site sequence determination
    • Tanizawa K., Masu Y., Asano S., Tanaka H., Soda K. Thermostable D-amino acid aminotransferase from a thermophilic Bacillus species. Purification, characterization, and active site sequence determination. J. Biol. Chem. 1989, 264:2445-2449.
    • (1989) J. Biol. Chem. , vol.264 , pp. 2445-2449
    • Tanizawa, K.1    Masu, Y.2    Asano, S.3    Tanaka, H.4    Soda, K.5
  • 112
    • 0031030606 scopus 로고    scopus 로고
    • Nucleotide sequence of the Bacillus licheniformis ATCC 10716 dat gene and comparison of the predicted amino acid sequence with those of other bacterial species
    • Taylor P.P., Fotheringham I.G. Nucleotide sequence of the Bacillus licheniformis ATCC 10716 dat gene and comparison of the predicted amino acid sequence with those of other bacterial species. Biochim. Biophys. Acta (BBA)-Gene Struct. Expr. 1997, 1350:38-40.
    • (1997) Biochim. Biophys. Acta (BBA)-Gene Struct. Expr. , vol.1350 , pp. 38-40
    • Taylor, P.P.1    Fotheringham, I.G.2
  • 113
    • 0031731648 scopus 로고    scopus 로고
    • Novel biosynthetic approaches to the production of unnatural amino acids using transaminases
    • Taylor P.P., Pantaleone D.P., Senkpeil R.F., Fotheringham I.G. Novel biosynthetic approaches to the production of unnatural amino acids using transaminases. Trends Biotechnol. 1998, 16:412-418.
    • (1998) Trends Biotechnol. , vol.16 , pp. 412-418
    • Taylor, P.P.1    Pantaleone, D.P.2    Senkpeil, R.F.3    Fotheringham, I.G.4
  • 114
    • 42549102312 scopus 로고    scopus 로고
    • Phenolic acid-mediated regulation of the padC gene, encoding the phenolic acid decarboxylase of Bacillus subtilis
    • Tran N.P., Gury J., Dartois V., Nguyen T.K.C., Seraut H., Barthelmebs L., Gervais P., Cavin J.-F. Phenolic acid-mediated regulation of the padC gene, encoding the phenolic acid decarboxylase of Bacillus subtilis. J. Bacteriol. 2008, 190:3213-3224.
    • (2008) J. Bacteriol. , vol.190 , pp. 3213-3224
    • Tran, N.P.1    Gury, J.2    Dartois, V.3    Nguyen, T.K.C.4    Seraut, H.5    Barthelmebs, L.6    Gervais, P.7    Cavin, J.-F.8
  • 115
    • 70449533072 scopus 로고    scopus 로고
    • Metabolic engineering of the complete pathway leading to heterologous biosynthesis of various flavonoids and stilbenoids in Saccharomyces cerevisiae
    • Trantas E., Panopoulos N., Ververidis F. Metabolic engineering of the complete pathway leading to heterologous biosynthesis of various flavonoids and stilbenoids in Saccharomyces cerevisiae. Metab. Eng. 2009, 11:355-366.
    • (2009) Metab. Eng. , vol.11 , pp. 355-366
    • Trantas, E.1    Panopoulos, N.2    Ververidis, F.3
  • 116
    • 67650261043 scopus 로고    scopus 로고
    • Gene yddG of Escherichia coli encoding the putative exporter of aromatic amino acids: constitutive transcription and dependence of the expression level on the cell growth rate
    • Tsyrenzhapova I.S., Doroshenko V.G., Airikh L.G., Mironov A.S., Mashko S.V. Gene yddG of Escherichia coli encoding the putative exporter of aromatic amino acids: constitutive transcription and dependence of the expression level on the cell growth rate. Russ. J. Genet. 2009, 45:601-609.
    • (2009) Russ. J. Genet. , vol.45 , pp. 601-609
    • Tsyrenzhapova, I.S.1    Doroshenko, V.G.2    Airikh, L.G.3    Mironov, A.S.4    Mashko, S.V.5
  • 117
    • 1842425628 scopus 로고    scopus 로고
    • Production of phenyllactic acid by lactic acid bacteria: an approach to the selection of strains contributing to food quality and preservation
    • Valerio F., Lavermicocca P., Pascale M., Visconti A. Production of phenyllactic acid by lactic acid bacteria: an approach to the selection of strains contributing to food quality and preservation. FEMS Microbiol. Lett. 2004, 233:289-295.
    • (2004) FEMS Microbiol. Lett. , vol.233 , pp. 289-295
    • Valerio, F.1    Lavermicocca, P.2    Pascale, M.3    Visconti, A.4
  • 118
    • 0023790061 scopus 로고
    • The involvement of an enantioselective transaminase in the metabolism of D-3-and D-4-hydroxyphenylglycine in Pseudomonas putida LW-4
    • Van den Tweel W., Smits J., Ogg R., De Bont J. The involvement of an enantioselective transaminase in the metabolism of D-3-and D-4-hydroxyphenylglycine in Pseudomonas putida LW-4. Appl. Microbiol. Biotechnol. 1988, 29:224-230.
    • (1988) Appl. Microbiol. Biotechnol. , vol.29 , pp. 224-230
    • Van den Tweel, W.1    Smits, J.2    Ogg, R.3    De Bont, J.4
  • 119
    • 33847252518 scopus 로고    scopus 로고
    • Production of p-hydroxycinnamic acid from glucose in Saccharomyces cerevisiae and Escherichia coli by expression of heterologous genes from plants and fungi
    • Vannelli T., Wei Qi W., Sweigard J., Gatenby A.A., Sariaslani F.S. Production of p-hydroxycinnamic acid from glucose in Saccharomyces cerevisiae and Escherichia coli by expression of heterologous genes from plants and fungi. Metab. Eng. 2007, 9:142-151.
    • (2007) Metab. Eng. , vol.9 , pp. 142-151
    • Vannelli, T.1    Wei Qi, W.2    Sweigard, J.3    Gatenby, A.A.4    Sariaslani, F.S.5
  • 122
    • 0042433548 scopus 로고    scopus 로고
    • Production of d-amino acids by N-acyl-d-amino acid amidohydrolase and its structure and function
    • Wakayama M., Yoshimune K., Hirose Y., Moriguchi M. Production of d-amino acids by N-acyl-d-amino acid amidohydrolase and its structure and function. J. Mol. Catal. B-Enzym. 2003, 23:71-85.
    • (2003) J. Mol. Catal. B-Enzym. , vol.23 , pp. 71-85
    • Wakayama, M.1    Yoshimune, K.2    Hirose, Y.3    Moriguchi, M.4
  • 123
    • 0028058771 scopus 로고
    • Large-Scale and highly enantioselective synthesis of the taxol C-13 side chain through asymmetric dihydroxylation
    • Wang Z.M., Kolb H.C., Sharpless K.B. Large-Scale and highly enantioselective synthesis of the taxol C-13 side chain through asymmetric dihydroxylation. J. Org. Chem. 1994, 59:5104-5105.
    • (1994) J. Org. Chem. , vol.59 , pp. 5104-5105
    • Wang, Z.M.1    Kolb, H.C.2    Sharpless, K.B.3
  • 124
    • 33845496747 scopus 로고    scopus 로고
    • Discovery of a substrate selectivity switch in tyrosine ammonia-lyase, a member of the aromatic amino acid lyase family
    • Watts K.T., Mijts B.N., Lee P.C., Manning A.J., Schmidt-Dannert C. Discovery of a substrate selectivity switch in tyrosine ammonia-lyase, a member of the aromatic amino acid lyase family. Chem. Biol. 2006, 13:1317-1326.
    • (2006) Chem. Biol. , vol.13 , pp. 1317-1326
    • Watts, K.T.1    Mijts, B.N.2    Lee, P.C.3    Manning, A.J.4    Schmidt-Dannert, C.5
  • 125
    • 0025016270 scopus 로고
    • Cloning of an aroF allele encoding a tyrosine-insensitive 3-deoxy-D-arabino-heptulosonate 7-phosphate synthase
    • Weaver L.M., Herrmann K.M. Cloning of an aroF allele encoding a tyrosine-insensitive 3-deoxy-D-arabino-heptulosonate 7-phosphate synthase. J. Bacteriol. 1990, 172:6581-6584.
    • (1990) J. Bacteriol. , vol.172 , pp. 6581-6584
    • Weaver, L.M.1    Herrmann, K.M.2
  • 127
    • 0020407265 scopus 로고
    • Regulation of expression of the dadA gene encoding D-amino acid dehydrogenase in Escherichia coli: analysis of dadA-lac fusions and direction of dadA transcription
    • Wild J., Obrepalska B. Regulation of expression of the dadA gene encoding D-amino acid dehydrogenase in Escherichia coli: analysis of dadA-lac fusions and direction of dadA transcription. Mol. Gen. Genet. 1982, 186(3):405-410.
    • (1982) Mol. Gen. Genet. , vol.186 , Issue.3 , pp. 405-410
    • Wild, J.1    Obrepalska, B.2
  • 128
    • 0031552598 scopus 로고    scopus 로고
    • A stereo-inverting D-phenylglycine aminotransferase from Pseudomonas stutzeri ST-201: purification, characterization and application for D-phenylglycine synthesis
    • Wiyakrutta S., Meevootisom V. A stereo-inverting D-phenylglycine aminotransferase from Pseudomonas stutzeri ST-201: purification, characterization and application for D-phenylglycine synthesis. J. Biotechnol. 1997, 55:193-203.
    • (1997) J. Biotechnol. , vol.55 , pp. 193-203
    • Wiyakrutta, S.1    Meevootisom, V.2
  • 129
    • 84872221971 scopus 로고    scopus 로고
    • Metabolic engineering of Escherichia coli for (2S)-pinocembrin production from glucose by a modular metabolic strategy
    • Wu J., Du G., Zhou J., Chen J. Metabolic engineering of Escherichia coli for (2S)-pinocembrin production from glucose by a modular metabolic strategy. Metab. Eng. 2013, 16:48-55.
    • (2013) Metab. Eng. , vol.16 , pp. 48-55
    • Wu, J.1    Du, G.2    Zhou, J.3    Chen, J.4
  • 130
    • 35148882050 scopus 로고    scopus 로고
    • Improved production of p-hydroxycinnamic acid from tyrosine using a novel thermostable phenylalanine/tyrosine ammonia lyase enzyme
    • Xue Z., McCluskey M., Cantera K., Ben-Bassat A., Sariaslani F.S., Huang L. Improved production of p-hydroxycinnamic acid from tyrosine using a novel thermostable phenylalanine/tyrosine ammonia lyase enzyme. Enzyme Microb. Technol. 2007, 42:58-64.
    • (2007) Enzyme Microb. Technol. , vol.42 , pp. 58-64
    • Xue, Z.1    McCluskey, M.2    Cantera, K.3    Ben-Bassat, A.4    Sariaslani, F.S.5    Huang, L.6
  • 131
    • 84859776222 scopus 로고    scopus 로고
    • The future of metabolic engineering and synthetic biology: towards a systematic practice
    • Yadav V.G., De Mey M., Lim C.G., Ajikumar P.K., Stephanopoulos G. The future of metabolic engineering and synthetic biology: towards a systematic practice. Metab. Eng. 2012, 14:233-241.
    • (2012) Metab. Eng. , vol.14 , pp. 233-241
    • Yadav, V.G.1    De Mey, M.2    Lim, C.G.3    Ajikumar, P.K.4    Stephanopoulos, G.5
  • 132
    • 84878218240 scopus 로고    scopus 로고
    • Enhanced production of L-phenylalanine in Corynebacterium glutamicum due to the introduction of Escherichia coli wild-type gene aroH
    • Zhang C., Zhang J., Kang Z., Du G., Yu X., Wang T., Chen J. Enhanced production of L-phenylalanine in Corynebacterium glutamicum due to the introduction of Escherichia coli wild-type gene aroH. J. Ind. Microbiol. Biotechnol. 2013, 40:643-651.
    • (2013) J. Ind. Microbiol. Biotechnol. , vol.40 , pp. 643-651
    • Zhang, C.1    Zhang, J.2    Kang, Z.3    Du, G.4    Yu, X.5    Wang, T.6    Chen, J.7
  • 133
    • 0032513052 scopus 로고    scopus 로고
    • Chorismate mutase-prephenate dehydratase from Escherichia coli: study of catalytic and regulatory domains using genetically engineered proteins
    • Zhang S., Pohnert G., Kongsaeree P., Wilson D.B., Clardy J., Ganem B. Chorismate mutase-prephenate dehydratase from Escherichia coli: study of catalytic and regulatory domains using genetically engineered proteins. J. Biol. Chem. 1998, 273:6248-6253.
    • (1998) J. Biol. Chem. , vol.273 , pp. 6248-6253
    • Zhang, S.1    Pohnert, G.2    Kongsaeree, P.3    Wilson, D.B.4    Clardy, J.5    Ganem, B.6
  • 134
    • 84855188845 scopus 로고    scopus 로고
    • Development of L-tryptophan production strains by defined genetic modification in Escherichia coli
    • Zhao Z.J., Zou C., Zhu Y.X., Dai J., Chen S., Wu D., Wu J., Chen J. Development of L-tryptophan production strains by defined genetic modification in Escherichia coli. J. Ind. Microbiol. Biotechnol. 2011, 38:1921-1929.
    • (2011) J. Ind. Microbiol. Biotechnol. , vol.38 , pp. 1921-1929
    • Zhao, Z.J.1    Zou, C.2    Zhu, Y.X.3    Dai, J.4    Chen, S.5    Wu, D.6    Wu, J.7    Chen, J.8
  • 135
    • 80052495837 scopus 로고    scopus 로고
    • Enhanced L-phenylalanine production by recombinant Escherichia coli BR-42 (pAP-B03) resistant to bacteriophage BP-1 via a two-stage feeding approach
    • Zhou H., Liao X., Liu L., Wang T., Du G., Chen J. Enhanced L-phenylalanine production by recombinant Escherichia coli BR-42 (pAP-B03) resistant to bacteriophage BP-1 via a two-stage feeding approach. J. Ind. Microbiol. Biotechnol. 2011, 38:1219-1227.
    • (2011) J. Ind. Microbiol. Biotechnol. , vol.38 , pp. 1219-1227
    • Zhou, H.1    Liao, X.2    Liu, L.3    Wang, T.4    Du, G.5    Chen, J.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.