메뉴 건너뛰기




Volumn 217, Issue , 2016, Pages 12-21

Whole-cell biocatalytic production of variously substituted β-aryl- and β-heteroaryl-β-amino acids

Author keywords

Aminomutase; Batch reaction sustainability; Chiral amine; Whole cell biocatalysis; Amino acids

Indexed keywords

BIOCATALYSTS; CELLS; CYTOLOGY; ESCHERICHIA COLI; REDOX REACTIONS;

EID: 84946945026     PISSN: 01681656     EISSN: 18734863     Source Type: Journal    
DOI: 10.1016/j.jbiotec.2015.10.012     Document Type: Article
Times cited : (18)

References (63)
  • 1
    • 84941072610 scopus 로고    scopus 로고
    • Chemoenzymatic synthesis of optically pure l- and d-biarylalanines through biocatalytic asymmetric amination and palladium-catalyzed arylation
    • Ahmed S.T., Parmeggiani F., Weise N.J., Flitsch S.L., Turner N.J. Chemoenzymatic synthesis of optically pure l- and d-biarylalanines through biocatalytic asymmetric amination and palladium-catalyzed arylation. ACS Catal. 2015, 5410-5413.
    • (2015) ACS Catal. , pp. 5410-5413
    • Ahmed, S.T.1    Parmeggiani, F.2    Weise, N.J.3    Flitsch, S.L.4    Turner, N.J.5
  • 2
    • 0014864612 scopus 로고
    • Formation of aromatic amino acid pools in Escherichia coli K-12
    • Brown K.D. Formation of aromatic amino acid pools in Escherichia coli K-12. J. Bacteriol. 1970, 104:177-188.
    • (1970) J. Bacteriol. , vol.104 , pp. 177-188
    • Brown, K.D.1
  • 3
    • 0015040644 scopus 로고
    • Maintenance and exchange of the aromatic amino acid pool in Escherichia coli
    • Brown K.D. Maintenance and exchange of the aromatic amino acid pool in Escherichia coli. J. Bacteriol. 1971, 106:70-81.
    • (1971) J. Bacteriol. , vol.106 , pp. 70-81
    • Brown, K.D.1
  • 4
    • 79952803469 scopus 로고    scopus 로고
    • Progress in the development of bestatin analogues as aminopeptidases inhibitors
    • Chen L., Teng Y., Xu W. Progress in the development of bestatin analogues as aminopeptidases inhibitors. Curr. Med. Chem. 2011, 18:964-976.
    • (2011) Curr. Med. Chem. , vol.18 , pp. 964-976
    • Chen, L.1    Teng, Y.2    Xu, W.3
  • 5
    • 33847273107 scopus 로고    scopus 로고
    • Permeability issues in whole-cell bioprocesses and cellular membrane engineering
    • Chen R.R.Z. Permeability issues in whole-cell bioprocesses and cellular membrane engineering. Appl. Microbiol. Biotechnol. 2007, 74:730-738.
    • (2007) Appl. Microbiol. Biotechnol. , vol.74 , pp. 730-738
    • Chen, R.R.Z.1
  • 6
    • 84860196682 scopus 로고    scopus 로고
    • Thermal bifunctionality of bacterial phenylalanine aminomutase and ammonia lyase enzymes
    • Chesters C., Wilding M., Goodall M., Micklefield J. Thermal bifunctionality of bacterial phenylalanine aminomutase and ammonia lyase enzymes. Angew. Chem. Int. Ed. Engl. 2012, 51:4344-4348.
    • (2012) Angew. Chem. Int. Ed. Engl. , vol.51 , pp. 4344-4348
    • Chesters, C.1    Wilding, M.2    Goodall, M.3    Micklefield, J.4
  • 7
    • 0242349771 scopus 로고    scopus 로고
    • Kinetic analysis of the 4-methylideneimidazole-5-one-containing tyrosine aminomutase in enediyne antitumor antibiotic C-1027 biosynthesis
    • Christenson S.D., Wu W., Spies M.A., Shen B., Toney M.D. Kinetic analysis of the 4-methylideneimidazole-5-one-containing tyrosine aminomutase in enediyne antitumor antibiotic C-1027 biosynthesis. Biochemistry 2003, 42:12708-12718.
    • (2003) Biochemistry , vol.42 , pp. 12708-12718
    • Christenson, S.D.1    Wu, W.2    Spies, M.A.3    Shen, B.4    Toney, M.D.5
  • 8
    • 0022543506 scopus 로고
    • Cloning of the aroP gene and identification of its product in Escherichia coli K-12
    • Chye M.L., Guest J.R., Pittard J. Cloning of the aroP gene and identification of its product in Escherichia coli K-12. J. Bacteriol. 1986, 167:749-753.
    • (1986) J. Bacteriol. , vol.167 , pp. 749-753
    • Chye, M.L.1    Guest, J.R.2    Pittard, J.3
  • 9
    • 0030977049 scopus 로고    scopus 로고
    • A topological model for the general aromatic amino acid permease, AroP, of Escherichia coli
    • Cosgriff A.J., Pittard A.J. A topological model for the general aromatic amino acid permease, AroP, of Escherichia coli. J. Bacteriol. 1997, 179:3317-3323.
    • (1997) J. Bacteriol. , vol.179 , pp. 3317-3323
    • Cosgriff, A.J.1    Pittard, A.J.2
  • 10
    • 4243562790 scopus 로고
    • Jasplakinolide, a cyclodepsipeptide from the marine sponge, Jaspis sp
    • Crews P., Manes L.V., Boehler M. Jasplakinolide, a cyclodepsipeptide from the marine sponge, Jaspis sp. Tetrahedron Lett. 1986, 27:2797-2800.
    • (1986) Tetrahedron Lett. , vol.27 , pp. 2797-2800
    • Crews, P.1    Manes, L.V.2    Boehler, M.3
  • 12
    • 0025818883 scopus 로고
    • Asymmetric synthesis of R-β-amino butanoic acid and S-β-tyrosine-homochiral lithium amide equivalents for Michael additions to α,β-unsaturated esters
    • Davies S.G., Ichihara O. Asymmetric synthesis of R-β-amino butanoic acid and S-β-tyrosine-homochiral lithium amide equivalents for Michael additions to α,β-unsaturated esters. Tetrahedron: Asymmetry 1991, 2:183-186.
    • (1991) Tetrahedron: Asymmetry , vol.2 , pp. 183-186
    • Davies, S.G.1    Ichihara, O.2
  • 13
    • 33646689324 scopus 로고    scopus 로고
    • Asymmetric titanium-catalysed Michael addition of O-benzylhydroxylamine to α,β-unsaturated carbonyl compounds: synthesis of β-amino acid precursors
    • Falborg L., Jorgensen K.A. Asymmetric titanium-catalysed Michael addition of O-benzylhydroxylamine to α,β-unsaturated carbonyl compounds: synthesis of β-amino acid precursors. J. Chem. Soc. Perkin Trans. 1996, 1:2823-2826.
    • (1996) J. Chem. Soc. Perkin Trans. , vol.1 , pp. 2823-2826
    • Falborg, L.1    Jorgensen, K.A.2
  • 15
    • 34547949525 scopus 로고    scopus 로고
    • A transglutaminase homologue as a condensation catalyst in antibiotic assembly lines
    • Fortin P.D., Walsh C.T., Magarvey N.A. A transglutaminase homologue as a condensation catalyst in antibiotic assembly lines. Nature 2007, 448:824-827.
    • (2007) Nature , vol.448 , pp. 824-827
    • Fortin, P.D.1    Walsh, C.T.2    Magarvey, N.A.3
  • 16
    • 0035382627 scopus 로고    scopus 로고
    • The outstanding biological stability of β- and γ-peptides toward proteolytic enzymes: an in vitro investigation with fifteen peptidases
    • Frackenpohl J., Arvidsson P.I., Schreiber J.V., Seebach D. The outstanding biological stability of β- and γ-peptides toward proteolytic enzymes: an in vitro investigation with fifteen peptidases. Chembiochem 2001, 2:445-455.
    • (2001) Chembiochem , vol.2 , pp. 445-455
    • Frackenpohl, J.1    Arvidsson, P.I.2    Schreiber, J.V.3    Seebach, D.4
  • 17
    • 0033519190 scopus 로고    scopus 로고
    • Synthesis and biological evaluation of a cyclo-β-tetrapeptide as a somatostatin analogue
    • Gademann K., Ernst M., Hoyer D., Seebach D. Synthesis and biological evaluation of a cyclo-β-tetrapeptide as a somatostatin analogue. Angew. Chem. Int. Ed. 1999, 38:1223-1226.
    • (1999) Angew. Chem. Int. Ed. , vol.38 , pp. 1223-1226
    • Gademann, K.1    Ernst, M.2    Hoyer, D.3    Seebach, D.4
  • 18
    • 20144381079 scopus 로고    scopus 로고
    • Transcriptional response of Escherichia coli to temperature shift
    • Gadgil M., Kapur V., Hu W.-S. Transcriptional response of Escherichia coli to temperature shift. Biotechnol. Progr. 2005, 21:689-699.
    • (2005) Biotechnol. Progr. , vol.21 , pp. 689-699
    • Gadgil, M.1    Kapur, V.2    Hu, W.-S.3
  • 19
    • 80053045956 scopus 로고    scopus 로고
    • Development of a commercial process for (S)-β-phenylalanine
    • Grayson J.I., Roos J., Osswald S. Development of a commercial process for (S)-β-phenylalanine. Org. Process Res. Dev. 2011, 15:1201-1206.
    • (2011) Org. Process Res. Dev. , vol.15 , pp. 1201-1206
    • Grayson, J.I.1    Roos, J.2    Osswald, S.3
  • 20
    • 0026469694 scopus 로고
    • Amino-acid-transport in bacteria
    • Haney S.A., Oxender D.L. Amino-acid-transport in bacteria. Int. Rev. Cytol. 1992, 137A:37-95.
    • (1992) Int. Rev. Cytol. , vol.137A , pp. 37-95
    • Haney, S.A.1    Oxender, D.L.2
  • 21
    • 58149109286 scopus 로고    scopus 로고
    • Development of a bulk enabling route to maraviroc (UK-427,857), a CCR-5 receptor antagonist
    • Haycock-Lewandowski S.J., Wilder A., Ahman J. Development of a bulk enabling route to maraviroc (UK-427,857), a CCR-5 receptor antagonist. Org. Process Res. Dev. 2008, 12:1094-1103.
    • (2008) Org. Process Res. Dev. , vol.12 , pp. 1094-1103
    • Haycock-Lewandowski, S.J.1    Wilder, A.2    Ahman, J.3
  • 23
    • 0345314096 scopus 로고    scopus 로고
    • Synthesis of a new chiral bisphospholane ligand for the Rh(I)-catalyzed enantioselective hydrogenation of isomeric β-acylamido acrylates
    • Holz J., Monsees A., Jiao H.J., You J.S., Komarov I.V., Fischer C., Drauz K., Borner A. Synthesis of a new chiral bisphospholane ligand for the Rh(I)-catalyzed enantioselective hydrogenation of isomeric β-acylamido acrylates. J. Org. Chem. 2003, 68:1701-1707.
    • (2003) J. Org. Chem. , vol.68 , pp. 1701-1707
    • Holz, J.1    Monsees, A.2    Jiao, H.J.3    You, J.S.4    Komarov, I.V.5    Fischer, C.6    Drauz, K.7    Borner, A.8
  • 24
    • 33747799316 scopus 로고    scopus 로고
    • A biosynthetic gene cluster for the acetyl-CoA carboxylase inhibitor andrimid
    • Jin M., Fischbach M.A., Clardy J. A biosynthetic gene cluster for the acetyl-CoA carboxylase inhibitor andrimid. J. Am. Chem. Soc. 2006, 128:10660-10661.
    • (2006) J. Am. Chem. Soc. , vol.128 , pp. 10660-10661
    • Jin, M.1    Fischbach, M.A.2    Clardy, J.3
  • 25
    • 25444492596 scopus 로고    scopus 로고
    • Chiral diphosphine ligands based on camphor: synthesis and applications in asymmetric hydrogenations
    • Kadyrov R., Ilaldinov I.Z., Almena J., Monsees A., Riermeier T.H. Chiral diphosphine ligands based on camphor: synthesis and applications in asymmetric hydrogenations. Tetrahedron Lett. 2005, 46:7397-7400.
    • (2005) Tetrahedron Lett. , vol.46 , pp. 7397-7400
    • Kadyrov, R.1    Ilaldinov, I.Z.2    Almena, J.3    Monsees, A.4    Riermeier, T.H.5
  • 26
    • 68049090816 scopus 로고    scopus 로고
    • Oxidative stress-dependent toxicity of silver nanoparticles in human hepatoma cells
    • Kim S., Choi J.E., Choi J., Chung K.-H., Park K., Yi J., Ryu D.-Y. Oxidative stress-dependent toxicity of silver nanoparticles in human hepatoma cells. Toxicol. In Vitro 2009, 23:1076-1084.
    • (2009) Toxicol. In Vitro , vol.23 , pp. 1076-1084
    • Kim, S.1    Choi, J.E.2    Choi, J.3    Chung, K.-H.4    Park, K.5    Yi, J.6    Ryu, D.-Y.7
  • 27
    • 0027383520 scopus 로고
    • The stationary phase of the bacterial life cycle
    • Kolter R., Siegele D.A., Tormo A. The stationary phase of the bacterial life cycle. Annu. Rev. Microbiol. 1993, 47:855-874.
    • (1993) Annu. Rev. Microbiol. , vol.47 , pp. 855-874
    • Kolter, R.1    Siegele, D.A.2    Tormo, A.3
  • 28
    • 0347285394 scopus 로고    scopus 로고
    • Identification of the LIV-I/LS system as the third phenylalanine transporter in Escherichia coli K-12
    • Koyanagi T., Katayama T., Suzuki H., Kumagai H. Identification of the LIV-I/LS system as the third phenylalanine transporter in Escherichia coli K-12. J. Bacteriol. 2003, 186:343-350.
    • (2003) J. Bacteriol. , vol.186 , pp. 343-350
    • Koyanagi, T.1    Katayama, T.2    Suzuki, H.3    Kumagai, H.4
  • 29
    • 62149101848 scopus 로고    scopus 로고
    • Discovery of additional members of the tyrosine aminomutase enzyme family and the mutational analysis of CmdF
    • Krug D., Mueller R. Discovery of additional members of the tyrosine aminomutase enzyme family and the mutational analysis of CmdF. ChemBioChem 2009, 10:741-750.
    • (2009) ChemBioChem , vol.10 , pp. 741-750
    • Krug, D.1    Mueller, R.2
  • 30
    • 4043089374 scopus 로고    scopus 로고
    • 2-amino acids-syntheses, occurrence in natural products, and components of β-peptides
    • 2-amino acids-syntheses, occurrence in natural products, and components of β-peptides. Biopolymers 2004, 76:206-243.
    • (2004) Biopolymers , vol.76 , pp. 206-243
    • Lelais, G.1    Seebach, D.2
  • 31
    • 0037201534 scopus 로고    scopus 로고
    • Recent advances in the stereoselective synthesis of β-amino acids
    • Liu M., Sibi M.P. Recent advances in the stereoselective synthesis of β-amino acids. Tetrahedron 2002, 58:7991-8035.
    • (2002) Tetrahedron , vol.58 , pp. 7991-8035
    • Liu, M.1    Sibi, M.P.2
  • 33
    • 0025895518 scopus 로고
    • Enantioselective synthesis of β-amino acids based on Binap-Ruthenium(II) catalyzed hydrogenation
    • Lubell W.D., Kitamura M., Noyori R. Enantioselective synthesis of β-amino acids based on Binap-Ruthenium(II) catalyzed hydrogenation. Tetrahedron-Asymmetry 1991, 2:543-554.
    • (1991) Tetrahedron-Asymmetry , vol.2 , pp. 543-554
    • Lubell, W.D.1    Kitamura, M.2    Noyori, R.3
  • 34
    • 53449094346 scopus 로고    scopus 로고
    • Gatekeeping versus promiscuity in the early stages of the andrimid biosynthetic assembly line
    • Magarvey N.A., Fortin P.D., Thomas P.M., Kelleher N.L., Walsh C.T. Gatekeeping versus promiscuity in the early stages of the andrimid biosynthetic assembly line. ACS Chem. Biol. 2008, 3:542-554.
    • (2008) ACS Chem. Biol. , vol.3 , pp. 542-554
    • Magarvey, N.A.1    Fortin, P.D.2    Thomas, P.M.3    Kelleher, N.L.4    Walsh, C.T.5
  • 35
    • 34548259160 scopus 로고    scopus 로고
    • Unusual mechanism for an aminomutase rearrangement: retention of configuration at the migration termini
    • Mutatu W., Klettke K.L., Foster C., Walker K.D. Unusual mechanism for an aminomutase rearrangement: retention of configuration at the migration termini. Biochemistry 2007, 46:9785-9794.
    • (2007) Biochemistry , vol.46 , pp. 9785-9794
    • Mutatu, W.1    Klettke, K.L.2    Foster, C.3    Walker, K.D.4
  • 36
    • 4644315650 scopus 로고    scopus 로고
    • Accelerating whole-cell biocatalysis by reducing outer membrane permeability barrier
    • Ni Y., Chen R.R. Accelerating whole-cell biocatalysis by reducing outer membrane permeability barrier. Biotechnol. Bioeng. 2004, 87:804-811.
    • (2004) Biotechnol. Bioeng. , vol.87 , pp. 804-811
    • Ni, Y.1    Chen, R.R.2
  • 37
    • 0017596420 scopus 로고
    • Synthesis and structure-activity-relationships of bestatin analogs, inhibitors of aminopeptidase-B
    • Nishizawa R., Saino T., Takita T., Suda H., Aoyagi T., Umezawa H. Synthesis and structure-activity-relationships of bestatin analogs, inhibitors of aminopeptidase-B. J. Med. Chem. 1977, 20:510-515.
    • (1977) J. Med. Chem. , vol.20 , pp. 510-515
    • Nishizawa, R.1    Saino, T.2    Takita, T.3    Suda, H.4    Aoyagi, T.5    Umezawa, H.6
  • 38
    • 85019292341 scopus 로고    scopus 로고
    • Catalysis of organic reactions-modern catalysis in the synthesis of some pharmaceuticals and fine chemicals
    • Petrovic S.D., Misic-Vukovic M.M., Mijin D.Z. Catalysis of organic reactions-modern catalysis in the synthesis of some pharmaceuticals and fine chemicals. Chem. Indus. 2002, 1:10-16.
    • (2002) Chem. Indus. , vol.1 , pp. 10-16
    • Petrovic, S.D.1    Misic-Vukovic, M.M.2    Mijin, D.Z.3
  • 39
    • 0029966330 scopus 로고    scopus 로고
    • Topology of the phenylalanine-specific permease of Escherichia coli
    • Pi J., Pittard A.J. Topology of the phenylalanine-specific permease of Escherichia coli. J. Bacteriol. 1996, 178:2650-2655.
    • (1996) J. Bacteriol. , vol.178 , pp. 2650-2655
    • Pi, J.1    Pittard, A.J.2
  • 40
    • 0025766783 scopus 로고
    • Cloning and sequencing of the pheP gene, which encodes the phenylalanine-specific transport system of Escherichia coli
    • Pi J., Wookey P.J., Pittard A.J. Cloning and sequencing of the pheP gene, which encodes the phenylalanine-specific transport system of Escherichia coli. J. Bacteriol. 1991, 173:3622-3629.
    • (1991) J. Bacteriol. , vol.173 , pp. 3622-3629
    • Pi, J.1    Wookey, P.J.2    Pittard, A.J.3
  • 41
    • 84907053915 scopus 로고    scopus 로고
    • Continuous flow synthesis of β-amino acids from α-amino acids via Arndt-Eistert homologation
    • Pinho V.D., Gutmann B., Kappe C.O. Continuous flow synthesis of β-amino acids from α-amino acids via Arndt-Eistert homologation. RSC Adv. 2014, 4:37419-37422.
    • (2014) RSC Adv. , vol.4 , pp. 37419-37422
    • Pinho, V.D.1    Gutmann, B.2    Kappe, C.O.3
  • 42
    • 0014430315 scopus 로고
    • Amino acid transport systems in E. coli K-12
    • Piperno J.R., Oxender D.L. Amino acid transport systems in E. coli K-12. J. Biol. Chem. 1968, 243:5914-5920.
    • (1968) J. Biol. Chem. , vol.243 , pp. 5914-5920
    • Piperno, J.R.1    Oxender, D.L.2
  • 43
    • 84907741516 scopus 로고    scopus 로고
    • Ring-substituted α-arylalanines for probing substituent effects on the isomerization reaction catalyzed by an aminomutase
    • Ratnayake N.D., Liu N., Kuhn L.A., Walker K.D. Ring-substituted α-arylalanines for probing substituent effects on the isomerization reaction catalyzed by an aminomutase. ACS Catal. 2014, 4:3077-3090.
    • (2014) ACS Catal. , vol.4 , pp. 3077-3090
    • Ratnayake, N.D.1    Liu, N.2    Kuhn, L.A.3    Walker, K.D.4
  • 44
    • 79957978699 scopus 로고    scopus 로고
    • Stereochemistry and mechanism of a microbial phenylalanine aminomutase
    • Ratnayake N.D., Wanninayake U., Geiger J.H., Walker K.D. Stereochemistry and mechanism of a microbial phenylalanine aminomutase. J. Am. Chem. Soc. 2011, 133:8531-8533.
    • (2011) J. Am. Chem. Soc. , vol.133 , pp. 8531-8533
    • Ratnayake, N.D.1    Wanninayake, U.2    Geiger, J.H.3    Walker, K.D.4
  • 45
    • 84883272014 scopus 로고    scopus 로고
    • Biocatalysis in organic chemistry and biotechnology: past, present, and future
    • Reetz M.T. Biocatalysis in organic chemistry and biotechnology: past, present, and future. J. Am. Chem. Soc. 2013, 135:12480-12496.
    • (2013) J. Am. Chem. Soc. , vol.135 , pp. 12480-12496
    • Reetz, M.T.1
  • 46
    • 84857581433 scopus 로고    scopus 로고
    • Transaminases for the synthesis of enantiopure β-amino acids
    • Rudat J., Brucher B.R., Syldatk C. Transaminases for the synthesis of enantiopure β-amino acids. AMB Express 2012, 2:11.
    • (2012) AMB Express , vol.2 , pp. 11
    • Rudat, J.1    Brucher, B.R.2    Syldatk, C.3
  • 48
    • 84880115442 scopus 로고    scopus 로고
    • Whole-cell biocatalysis for selective and productive CO functional group introduction and modification
    • Schrewe M., Julsing M.K., Buhler B., Schmid A. Whole-cell biocatalysis for selective and productive CO functional group introduction and modification. Chem. Soc. Rev. 2013, 42:6346-6377.
    • (2013) Chem. Soc. Rev. , vol.42 , pp. 6346-6377
    • Schrewe, M.1    Julsing, M.K.2    Buhler, B.3    Schmid, A.4
  • 49
    • 0033153367 scopus 로고    scopus 로고
    • Pleated sheets and turns of β-peptides with proteinogenic side chains
    • Seebach D., Abele S., Gademann K., Bernhard J. Pleated sheets and turns of β-peptides with proteinogenic side chains. Angew. Chem. Int. Ed. 1999, 38:1595-1597.
    • (1999) Angew. Chem. Int. Ed. , vol.38 , pp. 1595-1597
    • Seebach, D.1    Abele, S.2    Gademann, K.3    Bernhard, J.4
  • 50
    • 0001452530 scopus 로고    scopus 로고
    • 3-peptides with proteinaceous side chains: synthesis and solution structures of constitutional isomers, a novel helical secondary structure and the influence of solvation and hydrophobic interactions on folding
    • 3-peptides with proteinaceous side chains: synthesis and solution structures of constitutional isomers, a novel helical secondary structure and the influence of solvation and hydrophobic interactions on folding. Helv. Chim. Acta 1998, 81:932-982.
    • (1998) Helv. Chim. Acta , vol.81 , pp. 932-982
    • Seebach, D.1    Abele, S.2    Gademann, K.3    Guichard, G.4    Hintermann, T.5    Jaun, B.6    Matthews, J.L.7    Schreiber, J.V.8
  • 51
    • 0029953285 scopus 로고    scopus 로고
    • β-Peptides: synthesis by Arndt-Eistert homologation with concomitant peptide coupling. Structure determination by NMR and CD spectroscopy and by X-ray crystallography. Helical secondary structure of a β-hexapeptide in solution and its stability towards pepsin
    • Seebach D., Overhand M., Kiihnle F.N.M., Martinoni B. β-Peptides: synthesis by Arndt-Eistert homologation with concomitant peptide coupling. Structure determination by NMR and CD spectroscopy and by X-ray crystallography. Helical secondary structure of a β-hexapeptide in solution and its stability towards pepsin. Helv. Chim. Acta 1996, 79:913-941.
    • (1996) Helv. Chim. Acta , vol.79 , pp. 913-941
    • Seebach, D.1    Overhand, M.2    Kiihnle, F.N.M.3    Martinoni, B.4
  • 52
    • 0029906929 scopus 로고    scopus 로고
    • Stereoselective synthesis of β-amino acids via conjugate addition of nitrogen nucleophiles to α,β-unsaturated esters-recent advances
    • Sewald N. Stereoselective synthesis of β-amino acids via conjugate addition of nitrogen nucleophiles to α,β-unsaturated esters-recent advances. Amino Acids 1996, 11:397-408.
    • (1996) Amino Acids , vol.11 , pp. 397-408
    • Sewald, N.1
  • 53
    • 0001052215 scopus 로고    scopus 로고
    • N-Benzylhydroxylamine addition to β-aryl enoates. Enantioselective synthesis of β-aryl-β-amino acid precursors
    • Sibi M.P., Liu M. N-Benzylhydroxylamine addition to β-aryl enoates. Enantioselective synthesis of β-aryl-β-amino acid precursors. Org. Lett. 2000, 2:3393-3396.
    • (2000) Org. Lett. , vol.2 , pp. 3393-3396
    • Sibi, M.P.1    Liu, M.2
  • 55
    • 84858177898 scopus 로고    scopus 로고
    • Insights into the mechanistic pathway of the Pantoea agglomerans phenylalanine aminomutase
    • Strom S., Wanninayake U., Ratnayake N.D., Walker K.D., Geiger J.H. Insights into the mechanistic pathway of the Pantoea agglomerans phenylalanine aminomutase. Angew. Chem. Int. Ed. 2012, 51:2898-2902.
    • (2012) Angew. Chem. Int. Ed. , vol.51 , pp. 2898-2902
    • Strom, S.1    Wanninayake, U.2    Ratnayake, N.D.3    Walker, K.D.4    Geiger, J.H.5
  • 57
    • 11144225850 scopus 로고    scopus 로고
    • Cloning, heterologous expression, and characterization of a phenylalanine aminomutase involved in Taxol biosynthesis
    • Walker K.D., Klettke K., Akiyama T., Croteau R. Cloning, heterologous expression, and characterization of a phenylalanine aminomutase involved in Taxol biosynthesis. J. Biol. Chem. 2004, 279:53947-53954.
    • (2004) J. Biol. Chem. , vol.279 , pp. 53947-53954
    • Walker, K.D.1    Klettke, K.2    Akiyama, T.3    Croteau, R.4
  • 58
    • 84881052336 scopus 로고    scopus 로고
    • A bacterial tyrosine aminomutase proceeds through retention or inversion of stereochemistry to catalyze its isomerization reaction
    • Wanninayake U., Walker K.D. A bacterial tyrosine aminomutase proceeds through retention or inversion of stereochemistry to catalyze its isomerization reaction. J. Am. Chem. Soc. 2013, 135:11193-11204.
    • (2013) J. Am. Chem. Soc. , vol.135 , pp. 11193-11204
    • Wanninayake, U.1    Walker, K.D.2
  • 60
    • 0017726516 scopus 로고
    • Regulation of aromatic amino acid transport systems in Escherichia coli K-12
    • Whipp M.J., Pittard A.J. Regulation of aromatic amino acid transport systems in Escherichia coli K-12. J. Bacteriol. 1977, 132:453-461.
    • (1977) J. Bacteriol. , vol.132 , pp. 453-461
    • Whipp, M.J.1    Pittard, A.J.2
  • 61
    • 0015329291 scopus 로고
    • Specificity of the aromatic amino acid permeases of Escherichia coli
    • 71
    • Willshaw G., Tristram H. Specificity of the aromatic amino acid permeases of Escherichia coli. Biochem. J. 1972, 127. 71.
    • (1972) Biochem. J. , vol.127
    • Willshaw, G.1    Tristram, H.2
  • 62
    • 0031464787 scopus 로고    scopus 로고
    • Total synthesis of the anti methicillin-resistant Staphylococcus aureus peptide antibiotics TAN-1057A-D
    • Yuan C.G., Williams R.M. Total synthesis of the anti methicillin-resistant Staphylococcus aureus peptide antibiotics TAN-1057A-D. J. Am. Chem. Soc. 1997, 119:11777-11784.
    • (1997) J. Am. Chem. Soc. , vol.119 , pp. 11777-11784
    • Yuan, C.G.1    Williams, R.M.2
  • 63
    • 79955009094 scopus 로고    scopus 로고
    • Novel reference genes for quantifying transcriptional responses of Escherichia coli to protein overexpression by quantitative PCR
    • Zhou K., Zhou L.H., Lim Q.E., Zou R.Y., Stephanopoulos G., Too H.P. Novel reference genes for quantifying transcriptional responses of Escherichia coli to protein overexpression by quantitative PCR. BMC Mol. Biol. 2011, 12:18.
    • (2011) BMC Mol. Biol. , vol.12 , pp. 18
    • Zhou, K.1    Zhou, L.H.2    Lim, Q.E.3    Zou, R.Y.4    Stephanopoulos, G.5    Too, H.P.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.