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Volumn 19, Issue 1, 2014, Pages 1004-1022

Coupling bioorthogonal chemistries with artificial metabolism: Intracellular biosynthesis of azidohomoalanine and its incorporation into recombinant proteins

Author keywords

Artificial metabolism metabolic engineering; Bioorthogonality; Click chemistry; Genetic code expansion; L Azidohomoalanine; L methionine; O Acetyl L homoserine sulfhydrylase; Posttranslational modifications

Indexed keywords

ALANINE; AZIDOHOMOALANINE; BACTERIAL PROTEIN; BARSTAR PROTEIN, BACILLUS AMYLOLIQUEFACIENS; DRUG DERIVATIVE; RECOMBINANT PROTEIN;

EID: 84893091826     PISSN: None     EISSN: 14203049     Source Type: Journal    
DOI: 10.3390/molecules19011004     Document Type: Article
Times cited : (46)

References (41)
  • 2
    • 84867623952 scopus 로고    scopus 로고
    • Post-translational modification: Nature's escape from genetic imprisonment and the basis for dynamic information encoding
    • Prabakaran, S.; Lippens, G.; Steen, H.; Gunawardena, J. Post-translational modification: Nature's escape from genetic imprisonment and the basis for dynamic information encoding. Wiley Interdiscip. Rev. Syst. Biol. Med. 2012, 4, 565-583.
    • (2012) Wiley Interdiscip. Rev. Syst. Biol. Med. , vol.4 , pp. 565-583
    • Prabakaran, S.1    Lippens, G.2    Steen, H.3    Gunawardena, J.4
  • 4
    • 84880964743 scopus 로고    scopus 로고
    • Expanded genetic code for the engineering of ribosomally synthetized and post-translationally modified peptide natural products (ripps)
    • Budisa, N. Expanded genetic code for the engineering of ribosomally synthetized and post-translationally modified peptide natural products (ripps). Curr. Opin. Biotechnol. 2013, 24, 591-598.
    • (2013) Curr. Opin. Biotechnol. , vol.24 , pp. 591-598
    • Budisa, N.1
  • 5
    • 8344222343 scopus 로고    scopus 로고
    • Prolegomena to future experimental efforts on genetic code engineering by expanding its amino acid repertoire
    • Budisa, N. Prolegomena to future experimental efforts on genetic code engineering by expanding its amino acid repertoire. Angew. Chem. Int. Ed. Engl. 2004, 43, 6426-6463.
    • (2004) Angew. Chem. Int. Ed. Engl. , vol.43 , pp. 6426-6463
    • Budisa, N.1
  • 6
    • 70349917806 scopus 로고    scopus 로고
    • Bioorthogonal chemistry: Fishing for selectivity in a sea of functionality
    • Sletten, E.M.; Bertozzi, C.R. Bioorthogonal chemistry: Fishing for selectivity in a sea of functionality. Angew. Chem. Int. Ed. Engl. 2009, 48, 6974-6998.
    • (2009) Angew. Chem. Int. Ed. Engl. , vol.48 , pp. 6974-6998
    • Sletten, E.M.1    Bertozzi, C.R.2
  • 7
    • 77951192829 scopus 로고    scopus 로고
    • Synthetic biology of protein folding
    • Moroder, L.; Budisa, N. Synthetic biology of protein folding. ChemPhysChem 2010, 11, 1181-1187.
    • (2010) ChemPhysChem , vol.11 , pp. 1181-1187
    • Moroder, L.1    Budisa, N.2
  • 8
    • 77955027713 scopus 로고    scopus 로고
    • In vivo double and triple labeling of proteins using synthetic amino acids
    • Lepthien, S.; Merkel, L.; Budisa, N. In vivo double and triple labeling of proteins using synthetic amino acids. Angew. Chem. Int. Ed. Engl. 2010, 49, 5446-5450.
    • (2010) Angew. Chem. Int. Ed. Engl. , vol.49 , pp. 5446-5450
    • Lepthien, S.1    Merkel, L.2    Budisa, N.3
  • 9
    • 78650155287 scopus 로고    scopus 로고
    • Synthesis of proteins with defined posttranslational modifications using the genetic noncanonical amino acid incorporation approach
    • Liu, W.R.; Wang, Y.S.; Wan, W. Synthesis of proteins with defined posttranslational modifications using the genetic noncanonical amino acid incorporation approach. Mol. Biosyst. 2011, 7, 38-47.
    • (2011) Mol. Biosyst. , vol.7 , pp. 38-47
    • Liu, W.R.1    Wang, Y.S.2    Wan, W.3
  • 10
    • 36749014055 scopus 로고
    • 1,3-Dipolar cycloadditions. Past and future
    • Huisgen, R. 1,3-Dipolar cycloadditions. Past and future. Angew. Chem. Int. Ed. Engl. 1963, 2, 565-598.
    • (1963) Angew. Chem. Int. Ed. Engl. , vol.2 , pp. 565-598
    • Huisgen, R.1
  • 11
    • 0037012920 scopus 로고    scopus 로고
    • Peptidotriazoles on solid phase: [1,23]-Triazoles by regiospecific copper(I)-catalyzed 13-dipolar cycloadditions of terminal alkynes to azides
    • Tornoe, C.W.; Christensen, C.; Meldal, M. Peptidotriazoles on solid phase: [1,2,3]-Triazoles by regiospecific copper(I)-catalyzed 1,3-dipolar cycloadditions of terminal alkynes to azides. J. Org. Chem. 2002, 67, 3057-3064.
    • (2002) J Org Chem , vol.67 , pp. 3057-3064
    • Tornoe, C.W.1    Christensen, C.2    Meldal, M.3
  • 12
    • 0037099395 scopus 로고    scopus 로고
    • A stepwise huisgen cycloaddition process: Copper(I)-catalyzed regioselective "ligation" of azides and terminal alkynes
    • Rostovtsev, V.V.; Green, L.G.; Fokin, V.V.; Sharpless, K.B. A stepwise huisgen cycloaddition process: Copper(I)-catalyzed regioselective "ligation" of azides and terminal alkynes. Angew. Chem. Int. Ed. Engl. 2002, 41, 2596-2599.
    • (2002) Angew. Chem. Int. Ed. Engl. , vol.41 , pp. 2596-2599
    • Rostovtsev, V.V.1    Green, L.G.2    Fokin, V.V.3    Sharpless, K.B.4
  • 13
    • 67650469993 scopus 로고    scopus 로고
    • Protein iodination by click chemistry
    • Dong, S.; Moroder, L.; Budisa, N. Protein iodination by click chemistry. ChemBioChem 2009, 10, 1149-1151.
    • (2009) ChemBioChem , vol.10 , pp. 1149-1151
    • Dong, S.1    Moroder, L.2    Budisa, N.3
  • 14
    • 34547397482 scopus 로고    scopus 로고
    • Biochemical analysis on the parallel pathways of methionine biosynthesis in corynebacterium glutamicum
    • Hwang, B.J.; Park, S.D.; Kim, Y.; Kim, P.; Lee, H.S. Biochemical analysis on the parallel pathways of methionine biosynthesis in corynebacterium glutamicum. J. Microbiol. Biotechnol. 2007, 17, 1010-1017.
    • (2007) J. Microbiol. Biotechnol. , vol.17 , pp. 1010-1017
    • Hwang, B.J.1    Park, S.D.2    Kim, Y.3    Kim, P.4    Lee, H.S.5
  • 15
    • 77957051315 scopus 로고    scopus 로고
    • Towards methionine overproduction in corynebacterium glutamicum- methanethiol and dimethyldisulfide as reduced sulfur sources
    • Bolten, C.J.; Schroder, H.; Dickschat, J.; Wittmann, C. Towards methionine overproduction in corynebacterium glutamicum-methanethiol and dimethyldisulfide as reduced sulfur sources. J. Microbiol. Biotechnol. 2010, 20, 1196-1203.
    • (2010) J. Microbiol. Biotechnol. , vol.20 , pp. 1196-1203
    • Bolten, C.J.1    Schroder, H.2    Dickschat, J.3    Wittmann, C.4
  • 16
    • 0033619186 scopus 로고    scopus 로고
    • Cloning and characterization of the kluyveromyces lactis homocysteine synthase gene
    • Brzywczy, J.; Paszewski, A. Cloning and characterization of the kluyveromyces lactis homocysteine synthase gene. Yeast 1999, 15, 1403-1409.
    • (1999) Yeast , vol.15 , pp. 1403-1409
    • Brzywczy, J.1    Paszewski, A.2
  • 17
    • 0024847671 scopus 로고
    • Roles of O-Acetyl-L-homoserine sulfhydrylases in micro-organisms
    • Yamagata, S. Roles of O-Acetyl-L-homoserine sulfhydrylases in micro-organisms. Biochimie 1989, 71, 1125-1143.
    • (1989) Biochimie , vol.71 , pp. 1125-1143
    • Yamagata, S.1
  • 18
    • 0007323546 scopus 로고
    • Synthesis of selenocystine and selenohomocystine with O-Acetylhomoserine sulfhydrylase
    • Chocat, P.; Esaki, N.; Tanaka, H.; Kenji Soda, K. Synthesis of selenocystine and selenohomocystine with O-Acetylhomoserine sulfhydrylase. Agric. Biol. Chem. 1985, 49, 1143-1150.
    • (1985) Agric. Biol. Chem. , vol.49 , pp. 1143-1150
    • Chocat, P.1    Esaki, N.2    Tanaka, H.3    Kenji Soda, K.4
  • 19
    • 0037385630 scopus 로고    scopus 로고
    • Semisynthetic production of unnatural L-Alpha-Amino acids by metabolic engineering of the cysteine-biosynthetic Pathway
    • Maier, T.H. Semisynthetic production of unnatural L-Alpha-Amino acids by metabolic engineering of the cysteine-biosynthetic Pathway. Nat. Biotechnol. 2003, 21, 422-427.
    • (2003) Nat. Biotechnol. , vol.21 , pp. 422-427
    • Maier, T.H.1
  • 20
    • 78651391299 scopus 로고    scopus 로고
    • Protein thiocarboxylate-dependent methionine biosynthesis in wolinella succinogenes
    • Krishnamoorthy, K.; Begley, T.P. Protein thiocarboxylate-dependent methionine biosynthesis in wolinella succinogenes. J. Am. Chem. Soc. 2011, 133, 379-386.
    • (2011) J. Am. Chem. Soc. , vol.133 , pp. 379-386
    • Krishnamoorthy, K.1    Begley, T.P.2
  • 21
    • 84860405443 scopus 로고    scopus 로고
    • Sulfur amino acid metabolism limits the growth of children living in environments of poor sanitation
    • Bickler, S.W.; Ring, J.; de Maio, A. Sulfur amino acid metabolism limits the growth of children living in environments of poor sanitation. Med. Hypotheses 2011, 77, 380-382.
    • (2011) Med. Hypotheses , vol.77 , pp. 380-382
    • Bickler, S.W.1    Ring, J.2    De Maio, A.3
  • 23
    • 55849112685 scopus 로고    scopus 로고
    • Azatryptophans endow proteins with intrinsic blue fluorescence
    • Lepthien, S.; Hoesl, M.G.; Merkel, L.; Budisa, N. Azatryptophans endow proteins with intrinsic blue fluorescence. Proc. Natl. Acad. Sci. USA 2008, 105, 16095-16100.
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 16095-16100
    • Lepthien, S.1    Hoesl, M.G.2    Merkel, L.3    Budisa, N.4
  • 24
    • 80053079698 scopus 로고    scopus 로고
    • A novel mechanism of sulfur transfer catalyzed by O-Acetylhomoserine sulfhydrylase in the methionine-biosynthetic pathway of wolinella succinogenes
    • Tran, T.H.; Krishnamoorthy, K.; Begley, T.P.; Ealick, S.E. A novel mechanism of sulfur transfer catalyzed by O-Acetylhomoserine sulfhydrylase in the methionine-biosynthetic pathway of wolinella succinogenes. Acta Crystallogr. D Biol. Crystallogr. 2011, 67, 831-838.
    • (2011) Acta Crystallogr. D Biol. Crystallogr. , vol.67 , pp. 831-838
    • Tran, T.H.1    Krishnamoorthy, K.2    Begley, T.P.3    Ealick, S.E.4
  • 25
    • 84881525954 scopus 로고    scopus 로고
    • Structure-based mechanism for early PLP-mediated steps of rabbit cytosolic serine hydroxymethyltransferase reaction
    • Di Salvo, M.L.; Scarsdale, J.N.; Kazanina, G.; Contestabile, R.; Schirch, V.; Wright, H.T. Structure-based mechanism for early PLP-mediated steps of rabbit cytosolic serine hydroxymethyltransferase reaction. Biomed. Res. Int. 2013, 2013, 458571.
    • (2013) Biomed. Res. Int. , vol.2013 , pp. 458571
    • Di Salvo, M.L.1    Scarsdale, J.N.2    Kazanina, G.3    Contestabile, R.4    Schirch, V.5    Wright, H.T.6
  • 26
    • 84871911425 scopus 로고    scopus 로고
    • Alanine racemase from Tolypocladium inflatum: A key PLP-dependent enzyme in cyclosporin biosynthesis and a model of catalytic promiscuity
    • Di Salvo, M.L.; Florio, R.; Paiardini, A.; Vivoli, M.; D'Aguanno, S.; Contestabile, R. Alanine racemase from Tolypocladium inflatum: A key PLP-dependent enzyme in cyclosporin biosynthesis and a model of catalytic promiscuity. Arch. Biochem. Biophys. 2013, 529, 55-65.
    • (2013) Arch. Biochem. Biophys. , vol.529 , pp. 55-65
    • Di Salvo, M.L.1    Florio, R.2    Paiardini, A.3    Vivoli, M.4    D'Aguanno, S.5    Contestabile, R.6
  • 27
    • 80054683060 scopus 로고    scopus 로고
    • Serine hydroxymethyltransferase: A model enzyme for mechanistic, structural, and evolutionary studies
    • Florio, R.; di Salvo, M.L.; Vivoli, M.; Contestabile, R. Serine hydroxymethyltransferase: A model enzyme for mechanistic, structural, and evolutionary studies. Biochim. Biophys. Acta 2011, 1814, 1489-1496.
    • (2011) Biochim. Biophys. Acta , vol.1814 , pp. 1489-1496
    • Florio, R.1    Di Salvo, M.L.2    Vivoli, M.3    Contestabile, R.4
  • 28
    • 33645325418 scopus 로고    scopus 로고
    • Efficient Incorporation of unnatural amino acids into proteins in Escherichia coli
    • Ryu, Y.; Schultz, P.G. Efficient Incorporation of unnatural amino acids into proteins in Escherichia coli. Nat. Methods 2006, 3, 263-265.
    • (2006) Nat. Methods , vol.3 , pp. 263-265
    • Ryu, Y.1    Schultz, P.G.2
  • 29
    • 34548170626 scopus 로고    scopus 로고
    • Preparation of the functionalizable methionine surrogate azidohomoalanine via copper-catalyzed diazo transfer
    • Link, A.J.; Vink, M.K.; Tirrell, D.A. Preparation of the functionalizable methionine surrogate azidohomoalanine via copper-catalyzed diazo transfer. Nat. Protoc. 2007, 2, 1879-1883.
    • (2007) Nat. Protoc. , vol.2 , pp. 1879-1883
    • Link, A.J.1    Vink, M.K.2    Tirrell, D.A.3
  • 31
    • 38849157944 scopus 로고    scopus 로고
    • In vivo chemoenzymatic control of n-terminal processing in recombinant human epidermal growth factor
    • Merkel, L.; Cheburkin, Y.; Wiltschi, B.; Budisa, N. In vivo chemoenzymatic control of n-terminal processing in recombinant human epidermal growth factor. ChemBioChem 2007, 8, 2227-2232.
    • (2007) ChemBioChem , vol.8 , pp. 2227-2232
    • Merkel, L.1    Cheburkin, Y.2    Wiltschi, B.3    Budisa, N.4
  • 33
    • 48649092556 scopus 로고    scopus 로고
    • Efficient N-terminal glycoconjugation of proteins by the N-end rule
    • Merkel, L.; Beckmann, H.S.; Wittmann, V.; Budisa, N. Efficient N-terminal glycoconjugation of proteins by the N-end rule. ChemBioChem 2008, 9, 1220-1224.
    • (2008) ChemBioChem , vol.9 , pp. 1220-1224
    • Merkel, L.1    Beckmann, H.S.2    Wittmann, V.3    Budisa, N.4
  • 35
    • 0014198939 scopus 로고
    • Acetylhomoserine. An intermediate in the fungal biosynthesis of methionine
    • Nagai, S.; Flavin, M. Acetylhomoserine. An intermediate in the fungal biosynthesis of methionine. J. Biol. Chem. 1967, 242, 3884-3895.
    • (1967) J. Biol. Chem. , vol.242 , pp. 3884-3895
    • Nagai, S.1    Flavin, M.2
  • 37
    • 72449130848 scopus 로고    scopus 로고
    • Role of a conserved active site cation-pi interaction in Escherichia coli serine hydroxymethyltransferase
    • Vivoli, M.; Angelucci, F.; Ilari, A.; Morea, V.; Angelaccio, S.; di Salvo, M.L.; Contestabile, R. Role of a conserved active site cation-pi interaction in Escherichia coli serine hydroxymethyltransferase. Biochemistry 2009, 48, 12034-12046.
    • (2009) Biochemistry , vol.48 , pp. 12034-12046
    • Vivoli, M.1    Angelucci, F.2    Ilari, A.3    Morea, V.4    Angelaccio, S.5    Di Salvo, M.L.6    Contestabile, R.7
  • 38
    • 0035876180 scopus 로고    scopus 로고
    • Incorporation of beta-selenolo [3,2-b]Pyrrolyl-Alanine into proteins for phase determination in protein X-Ray crystallography
    • Bae, J.H.; Alefelder, S.; Kaiser, J.T.; Friedrich, R.; Moroder, L.; Huber, R.; Budisa, N. Incorporation of beta-selenolo[3,2-b]Pyrrolyl-Alanine into proteins for phase determination in protein X-Ray crystallography. J. Mol. Biol. 2001, 309, 925-936.
    • (2001) J. Mol. Biol. , vol.309 , pp. 925-936
    • Bae, J.H.1    Alefelder, S.2    Kaiser, J.T.3    Friedrich, R.4    Moroder, L.5    Huber, R.6    Budisa, N.7
  • 41
    • 54849405131 scopus 로고    scopus 로고
    • Intracellular uptake and inhibitory activity of aromatic fluorinated amino acids in human breast cancer cells
    • Giese, C.; Lepthien, S.; Metzner, L.; Brandsch, M.; Budisa, N.; Lilie, H. Intracellular uptake and inhibitory activity of aromatic fluorinated amino acids in human breast cancer cells. ChemMedChem 2008, 3, 1449-1456.
    • (2008) ChemMedChem , vol.3 , pp. 1449-1456
    • Giese, C.1    Lepthien, S.2    Metzner, L.3    Brandsch, M.4    Budisa, N.5    Lilie, H.6


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