메뉴 건너뛰기




Volumn 73, Issue 5, 2007, Pages 1525-1531

Recombinant polycistronic structure of hydantoinase process genes in Escherichia coli for the production of optically pure D-amino acids

Author keywords

[No Author keywords available]

Indexed keywords

D-AMINO ACIDS; HYDANTOINS; POLYCISTRONIC STRUCTURES;

EID: 33947270273     PISSN: 00992240     EISSN: None     Source Type: Journal    
DOI: 10.1128/AEM.02365-06     Document Type: Article
Times cited : (24)

References (25)
  • 1
    • 0035713489 scopus 로고    scopus 로고
    • Hydantoinases and related enzymes as biocatalysts for the synthesis of unnatural chiral amino acids
    • Altenbuchner, J., M. Siemann-Herzberg, and C. Syldatk. 2001. Hydantoinases and related enzymes as biocatalysts for the synthesis of unnatural chiral amino acids. Curr. Opin. Biotechnol. 12:559-563.
    • (2001) Curr. Opin. Biotechnol , vol.12 , pp. 559-563
    • Altenbuchner, J.1    Siemann-Herzberg, M.2    Syldatk, C.3
  • 3
    • 0008899495 scopus 로고
    • The isolation of amino-acids in the form of the corresponding carbamido-acids and hydantoins
    • Boyd, W. J. 1933. The isolation of amino-acids in the form of the corresponding carbamido-acids and hydantoins. Biochem. J. 27:1838-1848.
    • (1933) Biochem. J , vol.27 , pp. 1838-1848
    • Boyd, W.J.1
  • 4
    • 0033230902 scopus 로고    scopus 로고
    • One step production of D-p-hydroxyphenylglycine by recombinant Escherichia coli strains
    • Chao, Y. P., H. Fu, T. E. Lo, P. T. Cheng, and J. J. Wang. 1999. One step production of D-p-hydroxyphenylglycine by recombinant Escherichia coli strains. Biotechnol. Prog. 15:1039-1045.
    • (1999) Biotechnol. Prog , vol.15 , pp. 1039-1045
    • Chao, Y.P.1    Fu, H.2    Lo, T.E.3    Cheng, P.T.4    Wang, J.J.5
  • 6
    • 0018583412 scopus 로고
    • Rapid mapping of transposon insertion and deletion mutations in the large Ti-plasmids of Agrobacterium tumefaciens
    • Dhaese, P., H. De Greve, H. Decraemer, J. Schell, and M. Van Montagu. 1979. Rapid mapping of transposon insertion and deletion mutations in the large Ti-plasmids of Agrobacterium tumefaciens. Nucleic Acids Res. 7:1837-1849.
    • (1979) Nucleic Acids Res , vol.7 , pp. 1837-1849
    • Dhaese, P.1    De Greve, H.2    Decraemer, H.3    Schell, J.4    Van Montagu, M.5
  • 7
    • 0001674145 scopus 로고
    • The carboxylation of hydantoins
    • Finkbeiner, H. 1965. The carboxylation of hydantoins. J. Org. Chem. 30:3414-3419.
    • (1965) J. Org. Chem , vol.30 , pp. 3414-3419
    • Finkbeiner, H.1
  • 8
    • 0031977176 scopus 로고    scopus 로고
    • Efficient conversion of 5-substituted hydantoins to D-α-amino acids using recombinant Escherichia coli strains
    • Grifantini, R., G. Galli, G. Carpani, C. Praseti, G. Frascotti, and G. Grandi. 1998. Efficient conversion of 5-substituted hydantoins to D-α-amino acids using recombinant Escherichia coli strains. Microbiology 144:947-954.
    • (1998) Microbiology , vol.144 , pp. 947-954
    • Grifantini, R.1    Galli, G.2    Carpani, G.3    Praseti, C.4    Frascotti, G.5    Grandi, G.6
  • 9
    • 0019393944 scopus 로고
    • A perspective on the application of genetic engineering: Stability of recombinant plasmid
    • Imanaka, T., and S. Aiba. 1981. A perspective on the application of genetic engineering: stability of recombinant plasmid. Ann. N. Y. Acad. Sci. 369:1-14.
    • (1981) Ann. N. Y. Acad. Sci , vol.369 , pp. 1-14
    • Imanaka, T.1    Aiba, S.2
  • 10
    • 0028893981 scopus 로고
    • Optimization of the enzymatic synthesis of D-p-hydroxyphenylglycine from DL-5-substituted hydantoin using D-hydantoinase and D-carbamoylase
    • Kim, G. J., and H. S. Kim. 1995. Optimization of the enzymatic synthesis of D-p-hydroxyphenylglycine from DL-5-substituted hydantoin using D-hydantoinase and D-carbamoylase. Enzyme Microb. Technol. 17:63-67.
    • (1995) Enzyme Microb. Technol , vol.17 , pp. 63-67
    • Kim, G.J.1    Kim, H.S.2
  • 11
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T
    • Laemmli, U. K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T. Nature 227:680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 13
    • 0141482492 scopus 로고
    • Chemical racemization of 5-benzylhydantoin
    • Lazarus, R. A. 1990. Chemical racemization of 5-benzylhydantoin. J. Org. Chem. 55:4755-4757.
    • (1990) J. Org. Chem , vol.55 , pp. 4755-4757
    • Lazarus, R.A.1
  • 14
    • 0033527087 scopus 로고    scopus 로고
    • Modeling, simulation, and kinetic analysis of a heterogeneous reaction system for the enzymatic conversion of poorly soluble substrate
    • Lee, D. C., J. H. Park, G. J. Kim, and H. S. Kim. 1999. Modeling, simulation, and kinetic analysis of a heterogeneous reaction system for the enzymatic conversion of poorly soluble substrate. Biotechnol. Bioeng. 64:272-283.
    • (1999) Biotechnol. Bioeng , vol.64 , pp. 272-283
    • Lee, D.C.1    Park, J.H.2    Kim, G.J.3    Kim, H.S.4
  • 16
    • 0036862421 scopus 로고    scopus 로고
    • Complete conversion of D,L-5-monosubstituted hydantoins with a low velocity of chemical racemization into D-amino acids using whole cells of recombinant Escherichia coli
    • Martinez-Rodriguez, S., F. J. Las Heras-Vazquez, J. M. Clemente-Jimenez, L. Mingorance-Cazorla, and F. Rodriguez-Vico. 2002. Complete conversion of D,L-5-monosubstituted hydantoins with a low velocity of chemical racemization into D-amino acids using whole cells of recombinant Escherichia coli. Biotechnol. Prog. 18:1201-1206.
    • (2002) Biotechnol. Prog , vol.18 , pp. 1201-1206
    • Martinez-Rodriguez, S.1    Las Heras-Vazquez, F.J.2    Clemente-Jimenez, J.M.3    Mingorance-Cazorla, L.4    Rodriguez-Vico, F.5
  • 18
    • 13844299133 scopus 로고    scopus 로고
    • D-Amino acid production by E. coli co-expressed three genes encoding hydantoin racemase, D-hydantoinase and N-carbamoyl-D-amino acid amidohydolase
    • Nozaki, H., Y. Takenaka, I. Kira, K. Watanabe, and K. Yokozeki. 2005. D-Amino acid production by E. coli co-expressed three genes encoding hydantoin racemase, D-hydantoinase and N-carbamoyl-D-amino acid amidohydolase. J. Mol. Catal. B 32:213-218.
    • (2005) J. Mol. Catal. B , vol.32 , pp. 213-218
    • Nozaki, H.1    Takenaka, Y.2    Kira, I.3    Watanabe, K.4    Yokozeki, K.5
  • 19
    • 0034233319 scopus 로고    scopus 로고
    • Production of D-amino acids using whole cells of recombinant Escherichia coli with separately and coexpressed D-hydantoinase and N-carbamoylase
    • Park, J. H., G. J. Kim, and H. S. Kim. 2000. Production of D-amino acids using whole cells of recombinant Escherichia coli with separately and coexpressed D-hydantoinase and N-carbamoylase. Biotechnol. Prog. 16:564-570.
    • (2000) Biotechnol. Prog , vol.16 , pp. 564-570
    • Park, J.H.1    Kim, G.J.2    Kim, H.S.3
  • 20
    • 84955335567 scopus 로고    scopus 로고
    • Hydrolysis and formation of hydantoins
    • K. Drauz and H. Waldmann ed, Wiley-VCH, Weinheim, Germany
    • Pietzsch, M., and C. Syldatk. 2002. Hydrolysis and formation of hydantoins, p. 761-799. In K. Drauz and H. Waldmann (ed.), Enzyme catalysis in organic synthesis. Wiley-VCH, Weinheim, Germany.
    • (2002) Enzyme catalysis in organic synthesis , pp. 761-799
    • Pietzsch, M.1    Syldatk, C.2
  • 22
    • 0002426626 scopus 로고
    • Production of optically pure D- and L-α-amino acids by bioconversion of D,L-5-monosubstituted hydantoin derivatives
    • Syldatk, C., A. Läufer, R. Müller, and H. Höke. 1990. Production of optically pure D- and L-α-amino acids by bioconversion of D,L-5-monosubstituted hydantoin derivatives. Adv. Biochem. Eng. Biotechnol. 41:29-75.
    • (1990) Adv. Biochem. Eng. Biotechnol , vol.41 , pp. 29-75
    • Syldatk, C.1    Läufer, A.2    Müller, R.3    Höke, H.4
  • 23
    • 0001141297 scopus 로고
    • The chemistry of hydantoins
    • Ware, E. 1950. The chemistry of hydantoins. Chem. Rev. 46:403-470.
    • (1950) Chem. Rev , vol.46 , pp. 403-470
    • Ware, E.1
  • 24
    • 0035831306 scopus 로고    scopus 로고
    • Development of an Escherichia coli whole cell biocatalyst for the production of L-amino acids
    • Wilms, B., A. Wiese, C. Syldatk, R. Mattes, and J. Altenbuchner. 2001. Development of an Escherichia coli whole cell biocatalyst for the production of L-amino acids. J. Biotechnol. 86:19-30.
    • (2001) J. Biotechnol , vol.86 , pp. 19-30
    • Wilms, B.1    Wiese, A.2    Syldatk, C.3    Mattes, R.4    Altenbuchner, J.5
  • 25
    • 0004098009 scopus 로고
    • Microbial enzymes as catalysts for synthesis of biologically useful compounds
    • J. Tramper and H. C. van der Plas ed, Elsevier, Amsterdam, The Netherlands
    • Yamada, H., and H. Shimizu. 1985. Microbial enzymes as catalysts for synthesis of biologically useful compounds, p. 19-37. In J. Tramper and H. C. van der Plas (ed.), Biocatalysts in organic synthesis. Elsevier, Amsterdam, The Netherlands.
    • (1985) Biocatalysts in organic synthesis , pp. 19-37
    • Yamada, H.1    Shimizu, H.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.