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Volumn 14, Issue 10, 2008, Pages 1148-1150

Convenient sytheses of homopropargylglycine

Author keywords

2 amino 5 hexynoic acid; Homopropargylglycine; Noncanonical amino acids; Strecker reaction

Indexed keywords

AMINOACYLASE; HOMOPROPARGYLGLYCINE; NITRILASE; PROPARGYLGLYCINE; TRIMETHYLSILYL DERIVATIVE; TRIMETHYLSILYLCYANIDE; UNCLASSIFIED DRUG; 2 AMINO 5 HEXENOIC ACID; 2-AMINO-5-HEXENOIC ACID; ALKYNE; BACTERIAL PROTEIN; BARSTAR PROTEIN, BACILLUS AMYLOLIQUEFACIENS; DRUG DERIVATIVE; GLYCINE; HEXANOIC ACID DERIVATIVE; RIBONUCLEASE;

EID: 57849149951     PISSN: 10752617     EISSN: 10991387     Source Type: Journal    
DOI: 10.1002/psc.1065     Document Type: Article
Times cited : (9)

References (30)
  • 1
    • 0035917812 scopus 로고    scopus 로고
    • Expanding the genetic code of Escherichia coli
    • Wang L, Brock A, Herberich B, Schultz PG. Expanding the genetic code of Escherichia coli. Science 2001; 292: 498-500.
    • (2001) Science , vol.292 , pp. 498-500
    • Wang, L.1    Brock, A.2    Herberich, B.3    Schultz, P.G.4
  • 3
    • 0001280314 scopus 로고
    • Biosynthesis by Escherichia coli of active altered proteins containing selenium instead of sulphur
    • Cohen GN, Cowie DB. Biosynthesis by Escherichia coli of active altered proteins containing selenium instead of sulphur. Biochim. Biophys. Acta 1957; 26: 252-261.
    • (1957) Biochim. Biophys. Acta , vol.26 , pp. 252-261
    • Cohen, G.N.1    Cowie, D.B.2
  • 4
    • 0029064088 scopus 로고
    • High-level biosynthetic substitution of methionine in proteins by its analogs 20 aminohexanoic acid, selenomethionine, telluromethionine and ethionine in Escherichia coli
    • Budisa N, Steipe B, Demange P, Eckerskorn C. Kellermanm J, Huber R. High-level biosynthetic substitution of methionine in proteins by its analogs 20 aminohexanoic acid, selenomethionine, telluromethionine and ethionine in Escherichia coli. Eur. J. Biochem. 1995; 230: 788-796.
    • (1995) Eur. J. Biochem , vol.230 , pp. 788-796
    • Budisa, N.1    Steipe, B.2    Demange, P.3    Eckerskorn, C.4    Kellermanm, J.5    Huber, R.6
  • 5
    • 0032928678 scopus 로고    scopus 로고
    • Toward the experimental codon reassignment in vivo: Protein building with an expanded amino acid repertoire
    • Budisa N, Minks C. Alefelder S, Wenger W, Dong FM, Moroder L, Huber R. Toward the experimental codon reassignment in vivo: protein building with an expanded amino acid repertoire. FASEB J. 1999: 13: 41-51.
    • (1999) FASEB J , vol.13 , pp. 41-51
    • Budisa, N.1    Minks, C.2    Alefelder, S.3    Wenger, W.4    Dong, F.M.5    Moroder, L.6    Huber, R.7
  • 6
    • 0034003659 scopus 로고    scopus 로고
    • Efficient incorporation of unsaturated methionine analogues into proteins in vivo
    • Van Hest JCM, Mick KL, Tirrell DA. Efficient incorporation of unsaturated methionine analogues into proteins in vivo. J. Am. Chem. Soc. 2000; 122: 1282-1288.
    • (2000) J. Am. Chem. Soc , vol.122 , pp. 1282-1288
    • Van Hest, J.C.M.1    Mick, K.L.2    Tirrell, D.A.3
  • 7
    • 0037039298 scopus 로고    scopus 로고
    • Incorporation of azides into recombinant proteins for chemoselective modification by the Staudinger ligation
    • Kiick KL, Saxon E, Tirrell DA, Bertozzi CR. Incorporation of azides into recombinant proteins for chemoselective modification by the Staudinger ligation. Proc. Natl. Acad. Sci. U.S.A. 2002; 99: 19-24.
    • (2002) Proc. Natl. Acad. Sci. U.S.A , vol.99 , pp. 19-24
    • Kiick, K.L.1    Saxon, E.2    Tirrell, D.A.3    Bertozzi, C.R.4
  • 9
    • 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
  • 11
    • 0037099395 scopus 로고    scopus 로고
    • A stepwise Huisgen cycloaddition process: Copper(I)-catalyzed regioselective ligation of azides and terminal alkynes
    • Rostovtsev VV, Green LG, Fokin VV, Sharpless KB. 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
  • 12
    • 0037012920 scopus 로고    scopus 로고
    • Tornøe CW, 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.
    • Tornøe CW, 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.
  • 13
    • 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
  • 14
    • 0032575868 scopus 로고    scopus 로고
    • (2R)-2-Amino-6-hydroxy-4-hexynoic acid, and related amino acids in the fruiting bodies of amanita miculifera
    • Hatanaka SI, Niimura Y, Takishima K, Sugiyama J. (2R)-2-Amino-6-hydroxy-4-hexynoic acid, and related amino acids in the fruiting bodies of amanita miculifera. Phytochemistry 1998; 49: 573-578.
    • (1998) Phytochemistry , vol.49 , pp. 573-578
    • Hatanaka, S.I.1    Niimura, Y.2    Takishima, K.3    Sugiyama, J.4
  • 19
    • 0035888846 scopus 로고    scopus 로고
    • (E)-Selective hydrolysis of (E,Z)-α,β-unsaturated nitriles by the recombinant nitrilase AtNIT1 from Arabidopsis thaliana
    • Effenberger F, Oßwald S. (E)-Selective hydrolysis of (E,Z)-α,β-unsaturated nitriles by the recombinant nitrilase AtNIT1 from Arabidopsis thaliana. Tetrahedron: Asymmetry 2001; 12: 2581-2587.
    • (2001) Tetrahedron: Asymmetry , vol.12 , pp. 2581-2587
    • Effenberger, F.1    Oßwald, S.2
  • 20
    • 0035910856 scopus 로고    scopus 로고
    • Enantioselective hydrolysis of (RS)-2-fluoroarylacetonitriles using nitrilase from Arabidopsis thaliana
    • Effenberger F. Oßwald S. Enantioselective hydrolysis of (RS)-2-fluoroarylacetonitriles using nitrilase from Arabidopsis thaliana. Tetrahedron: Asymmetry 2001; 12: 279-285.
    • (2001) Tetrahedron: Asymmetry , vol.12 , pp. 279-285
    • Effenberger, F.1    Oßwald, S.2
  • 21
    • 33845183768 scopus 로고
    • Kinetic resolution of unnatural and rarely occurring amino acids: Enantioselective hydrolysis of N-acyl amino acids catalyzed by acylase I
    • Chenault HK, Dahmer J, Whitesides GM. Kinetic resolution of unnatural and rarely occurring amino acids: enantioselective hydrolysis of N-acyl amino acids catalyzed by acylase I. J. Am. Chem. Soc. 1989; 111: 6354-6364.
    • (1989) J. Am. Chem. Soc , vol.111 , pp. 6354-6364
    • Chenault, H.K.1    Dahmer, J.2    Whitesides, G.M.3
  • 22
    • 0026580837 scopus 로고
    • Use of Marfey's reagent to quantitate racemization upon anchoring of amino acids to solid supports for peptide synthesis
    • Adamson JG, Hoang T, Crivici A, Lajoie GA. Use of Marfey's reagent to quantitate racemization upon anchoring of amino acids to solid supports for peptide synthesis. Anal. Biochem. 1992: 202: 210-214.
    • (1992) Anal. Biochem , vol.202 , pp. 210-214
    • Adamson, J.G.1    Hoang, T.2    Crivici, A.3    Lajoie, G.A.4
  • 23
    • 0028147247 scopus 로고
    • Asymmetric Strecker synthesis using enantiopure sulfinimines: A convenient synthesis of α-amino acids
    • Davis FA, Reddy RE, Portonovo PS. Asymmetric Strecker synthesis using enantiopure sulfinimines: A convenient synthesis of α-amino acids. Tetrahedron Lett. 1994; 35: 9351-9354.
    • (1994) Tetrahedron Lett , vol.35 , pp. 9351-9354
    • Davis, F.A.1    Reddy, R.E.2    Portonovo, P.S.3
  • 24
    • 0043032834 scopus 로고    scopus 로고
    • Highly diastereoselective Strecker reaction of enolizable aliphatic sulfinimines
    • Li BF, Yuan K, Zhang MJ, Wu H, Dai LX, Wang QR, Hou XL. Highly diastereoselective Strecker reaction of enolizable aliphatic sulfinimines. J. Org. Chem. 2003; 68: 6264-6267.
    • (2003) J. Org. Chem , vol.68 , pp. 6264-6267
    • Li, B.F.1    Yuan, K.2    Zhang, M.J.3    Wu, H.4    Dai, L.X.5    Wang, Q.R.6    Hou, X.L.7
  • 25
    • 0001475118 scopus 로고    scopus 로고
    • Studies toward the asymmetric synthesis of -amino phosphonic acids via the addition of phosphites to enantiopure sulfinimines
    • Lefebvre MI. Evans SA Jr. Studies toward the asymmetric synthesis of -amino phosphonic acids via the addition of phosphites to enantiopure sulfinimines. J. Org. Chem. 1997: 62: 7532-7533.
    • (1997) J. Org. Chem , vol.62 , pp. 7532-7533
    • Lefebvre, M.I.1    Evans Jr., S.A.2
  • 26
    • 0030020116 scopus 로고    scopus 로고
    • A new efficient synthesis of acetyltelluro- and acetylselenomethionine and their use in the biosynthesis of heavy-atom protein analogs
    • Karnbrock W, Weyher E. Budisa N, Huber R, Moroder L. A new efficient synthesis of acetyltelluro- and acetylselenomethionine and their use in the biosynthesis of heavy-atom protein analogs. J. Am. Chem. Soc. 1996: 118: 913-914.
    • (1996) J. Am. Chem. Soc , vol.118 , pp. 913-914
    • Karnbrock, W.1    Weyher, E.2    Budisa, N.3    Huber, R.4    Moroder, L.5
  • 27
    • 0032776419 scopus 로고    scopus 로고
    • Folding of barstar C40A/C82A/P27A and catalysis of the peptidyl-prolyl cis/trans isomerization by human cytosolic cyclophilin (Cyp18)
    • Golbik R, Fischer G, Fersht AR. Folding of barstar C40A/C82A/P27A and catalysis of the peptidyl-prolyl cis/trans isomerization by human cytosolic cyclophilin (Cyp18). Protein Sci. 1999; 8: 1505-1514.
    • (1999) Protein Sci , vol.8 , pp. 1505-1514
    • Golbik, R.1    Fischer, G.2    Fersht, A.R.3
  • 28
    • 0022508657 scopus 로고
    • Sequence determinants of cytosolic N-terminal protein processing
    • Flinta C, Persson B, Jornvall H, Vonheijne G. Sequence determinants of cytosolic N-terminal protein processing. Eur. J. Biochem. 1986; 154: 193-196.
    • (1986) Eur. J. Biochem , vol.154 , pp. 193-196
    • Flinta, C.1    Persson, B.2    Jornvall, H.3    Vonheijne, G.4
  • 30
    • 26844472243 scopus 로고    scopus 로고
    • Selective dye-labeling of newly synthesized proteins in bacterial cells
    • Beatty KE, Xie F, Wang Q, Tirrell DA. Selective dye-labeling of newly synthesized proteins in bacterial cells. J. Am. Chem. Soc. 2005; 127: 14150-14151.
    • (2005) J. Am. Chem. Soc , vol.127 , pp. 14150-14151
    • Beatty, K.E.1    Xie, F.2    Wang, Q.3    Tirrell, D.A.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.