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Volumn 4, Issue 6, 2012, Pages 478-484

Engineering methylaspartate ammonia lyase for the asymmetric synthesis of unnatural amino acids

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; AMMONIA LYASE; METHYLASPARTATE AMMONIA LYASE; METHYLASPARTATE AMMONIA-LYASE;

EID: 84862847925     PISSN: 17554330     EISSN: 17554349     Source Type: Journal    
DOI: 10.1038/nchem.1338     Document Type: Article
Times cited : (69)

References (33)
  • 2
    • 78449259734 scopus 로고    scopus 로고
    • Biocatalysis-key to sustainable industrial chemistry
    • Wohlgemuth, R. Biocatalysis-key to sustainable industrial chemistry. Curr. Opin. Biotechnol. 21, 713-724 (2010).
    • (2010) Curr. Opin. Biotechnol. , vol.21 , pp. 713-724
    • Wohlgemuth, R.1
  • 3
    • 16244402638 scopus 로고    scopus 로고
    • Advances in biocatalytic synthesis of pharmaceutical intermediates
    • Panke, S. & Wubbolts, M. Advances in biocatalytic synthesis of pharmaceutical intermediates. Curr. Opin. Chem. Biol. 9, 188-194 (2005).
    • (2005) Curr. Opin. Chem. Biol. , vol.9 , pp. 188-194
    • Panke, S.1    Wubbolts, M.2
  • 4
    • 3543087310 scopus 로고    scopus 로고
    • Trends and innovations in industrial biocatalysis for the production of fine chemicals
    • Panke, S., Held, M. & Wubbolts, M. Trends and innovations in industrial biocatalysis for the production of fine chemicals. Curr. Opin. Biotechnol. 15, 272-279 (2004).
    • (2004) Curr. Opin. Biotechnol. , vol.15 , pp. 272-279
    • Panke, S.1    Held, M.2    Wubbolts, M.3
  • 5
    • 79953308640 scopus 로고    scopus 로고
    • Ammonia lyases and aminomutases as biocatalysts for the synthesis of a-amino and β-amino acids
    • Turner, N. J. Ammonia lyases and aminomutases as biocatalysts for the synthesis of a-amino and β-amino acids. Curr. Opin. Chem. Biol. 15, 234-240 (2011).
    • (2011) Curr. Opin. Chem. Biol. , vol.15 , pp. 234-240
    • Turner, N.J.1
  • 7
    • 0026469359 scopus 로고
    • Sequencing, and expression in escherichia coli of the clostridium tetanomorphum gene encoding β-methylaspartase and characterization of the recombinant protein
    • Goda, S. K., Minton, N. P., Botting, N. P. & Gani, D. Cloning, sequencing, and expression in Escherichia coli of the Clostridium tetanomorphum gene encoding β-methylaspartase and characterization of the recombinant protein. Biochemistry 31, 10747-10756 (1992).
    • (1992) Biochemistry , vol.31 , pp. 10747-10756
    • Goda, S.K.1    Minton, N.P.2    Botting, N.P.3    Gani D. Cloning4
  • 8
    • 70349389004 scopus 로고    scopus 로고
    • Alteration of the diastereoselectivity of 3-methylaspartate ammonia lyase by using structure-based mutagenesis
    • Raj, H. et al. Alteration of the diastereoselectivity of 3-methylaspartate ammonia lyase by using structure-based mutagenesis. ChemBioChem 10, 2236-2245 (2009).
    • (2009) ChemBioChem , vol.10 , pp. 2236-2245
    • Raj, H.1
  • 9
    • 0014073069 scopus 로고
    • Divalent metal activation of β-methylaspartase. The importance of ionic radius
    • Bright, H. J. Divalent metal activation of β-methylaspartase. The importance of ionic radius. Biochemistry 6, 1191-1203 (1967).
    • (1967) Biochemistry , vol.6 , pp. 1191-1203
    • Bright, H.J.1
  • 10
    • 0013492509 scopus 로고
    • On the mechanism of divalent metal activation of β-methylaspartase
    • Bright, H. J. On the mechanism of divalent metal activation of β-methylaspartase. J. Biol. Chem. 240, 1198-1210 (1965).
    • (1965) J. Biol. Chem. , vol.240 , pp. 1198-1210
    • Bright, H.J.1
  • 11
    • 0030729079 scopus 로고    scopus 로고
    • 3-Methylaspartate ammonia-lyase as a marker enzyme of the mesaconate pathway for (S)-glutamate fermentation in Enterobacteriaceae
    • Kato, Y. & Asano, Y. 3-Methylaspartate ammonia-lyase as a marker enzyme of the mesaconate pathway for (S)-glutamate fermentation in Enterobacteriaceae. Arch. Microbiol. 168, 457-463 (1997).
    • (1997) Arch. Microbiol. , vol.168 , pp. 457-463
    • Kato, Y.1    Asano, Y.2
  • 12
    • 0037040988 scopus 로고    scopus 로고
    • The structure of 3-methylaspartase from clostridium tetanomorphum functions via the common enolase chemical step
    • Asuncion, M., Blankenfeldt, W., Barlow, J. N., Gani, D. & Naismith, J. H. The structure of 3-methylaspartase from Clostridium tetanomorphum functions via the common enolase chemical step. J. Biol. Chem. 277, 8306-8311 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 8306-8311
    • Asuncion, M.1    Blankenfeldt, W.2    Barlow, J.N.3    Gani, D.4    Naismith, J.H.5
  • 13
    • 0036151237 scopus 로고    scopus 로고
    • Insights into enzyme evolution revealed by the structure of methylaspartate ammonia lyase
    • Levy, C. W. et al. Insights into enzyme evolution revealed by the structure of methylaspartate ammonia lyase. Structure 10, 105-113 (2002).
    • (2002) Structure , vol.10 , pp. 105-113
    • Levy, C.W.1
  • 14
    • 0013561354 scopus 로고
    • The mechanism of the methylaspartate ammonia-lyase reaction: Deuterium exchange
    • Bright, H. J., Ingraham, L. L. & Lundin, R. E. The mechanism of the methylaspartate ammonia-lyase reaction: deuterium exchange. Biochim. Biophys. Acta 81, 576-584 (1964).
    • (1964) Biochim. Biophys. Acta , vol.81 , pp. 576-584
    • Bright, H.J.1    Ingraham, L.L.2    Lundin, R.E.3
  • 15
    • 0001687226 scopus 로고
    • The mechanism of the β-methylaspartase reaction
    • Bright, H. The mechanism of the β-methylaspartase reaction. J. Biol. Chem. 239, 2307-2315 (1964).
    • (1964) J. Biol. Chem. , vol.239 , pp. 2307-2315
    • Bright, H.1
  • 16
    • 12644303230 scopus 로고    scopus 로고
    • The enolase superfamily: A general strategy for enzymecatalyzed abstraction of the a-protons of carboxylic acids
    • Babbitt, P. C. et al. The enolase superfamily: a general strategy for enzymecatalyzed abstraction of the a-protons of carboxylic acids. Biochemistry 35, 16489-16501 (1996).
    • (1996) Biochemistry , vol.35 , pp. 16489-16501
    • Babbitt, P.C.1
  • 17
    • 0023608355 scopus 로고
    • Enantiospecific synthesis of 3-substituted aspartic acids via enzymic amination of substituted fumaric acids
    • Akhtar, M., Botting, N. P., Cohen, M. A. & Gani, D. Enantiospecific synthesis of 3-substituted aspartic acids via enzymic amination of substituted fumaric acids. Tetrahedron 43, 5899-5908 (1987).
    • (1987) Tetrahedron , vol.43 , pp. 5899-5908
    • Akhtar, M.1    Botting, N.P.2    Cohen, M.A.3    Gani, D.4
  • 18
    • 0024291672 scopus 로고
    • Substrate specificity of the 3-methylaspartate ammonia-lyase reaction: Observation of differential relative reaction rates for substrate-product pairs
    • Botting, N. P., Akhtar, M., Cohen, M. A. & Gani, D. Substrate specificity of the 3-methylaspartate ammonia-lyase reaction: observation of differential relative reaction rates for substrate-product pairs. Biochemistry 27, 2953-2955 (1988).
    • (1988) Biochemistry , vol.27 , pp. 2953-2955
    • Botting, N.P.1    Akhtar, M.2    Cohen, M.A.3    Gani, D.4
  • 19
    • 0345084878 scopus 로고    scopus 로고
    • Preparation of n-substituted aspartic acids via enantiospecific conjugate addition of n-nucleophiles to fumaric acids using methylaspartase: Synthetic utility and mechanistic implications
    • Gulzar, M. S., Akhtar, M. & Gani, D. Preparation of N-substituted aspartic acids via enantiospecific conjugate addition of N-nucleophiles to fumaric acids using methylaspartase: synthetic utility and mechanistic implications. J. Chem. Soc. Perkin Trans. 1, 649-656 (1997).
    • (1997) J. Chem. Soc. Perkin Trans. , vol.1 , pp. 649-656
    • Gulzar, M.S.1    Akhtar, M.2    Gani, D.3
  • 21
    • 22144485602 scopus 로고    scopus 로고
    • Expanding the range of substrate acceptance of enzymes: Combinatorial active-site saturation test
    • Reetz, M. T., Bocola, M., Carballeira, J. D., Zha, D. & Vogel, A. Expanding the range of substrate acceptance of enzymes: combinatorial active-site saturation test. Angew. Chem. Int. Ed. 44, 4192-4196 (2005).
    • (2005) Angew. Chem. Int. Ed. , vol.44 , pp. 4192-4196
    • Reetz, M.T.1    Bocola, M.2    Carballeira, J.D.3    Zha, D.4    Vogel, A.5
  • 22
    • 18144403554 scopus 로고    scopus 로고
    • Improving enzyme properties: When are closer mutations better?
    • Morley, K. L. & Kazlauskas, R. J. Improving enzyme properties: when are closer mutations better? Trends Biotechnol. 23, 231-237 (2005).
    • (2005) Trends Biotechnol. , vol.23 , pp. 231-237
    • Morley, K.L.1    Kazlauskas, R.J.2
  • 24
    • 68049106179 scopus 로고    scopus 로고
    • Directed evolution drives the next generation of biocatalysts
    • Turner, N. J. Directed evolution drives the next generation of biocatalysts. Nature Chem. Biol. 5, 567-573 (2009).
    • (2009) Nature Chem. Biol. , vol.5 , pp. 567-573
    • Turner, N.J.1
  • 25
    • 1842585550 scopus 로고    scopus 로고
    • Characterization of novel l-threo-b-benzyloxyaspartate derivatives, potent blockers of the glutamate transporters
    • Shimamoto, K. et al. Characterization of novel L-threo-b- benzyloxyaspartate derivatives, potent blockers of the glutamate transporters. Mol. Pharmacol. 65, 1008-1015 (2004).
    • (2004) Mol. Pharmacol. , vol.65 , pp. 1008-1015
    • Shimamoto, K.1
  • 26
    • 48249112610 scopus 로고    scopus 로고
    • Glutamate transporter blockers for elucidation of the function of excitatory neurotransmission systems
    • Shimamoto, K. Glutamate transporter blockers for elucidation of the function of excitatory neurotransmission systems. Chem. Rec. 8, 182-199 (2008).
    • (2008) Chem. Rec. , vol.8 , pp. 182-199
    • Shimamoto, K.1
  • 27
    • 26944498280 scopus 로고    scopus 로고
    • The substituted aspartate analogue l-b-threo-benzylaspartate preferentially inhibits the neuronal excitatory amino acid transporter eaat3
    • Esslinger, C. S. et al. The substituted aspartate analogue L-b-threo-benzylaspartate preferentially inhibits the neuronal excitatory amino acid transporter EAAT3. Neuropharmacology 49, 850-861 (2005).
    • (2005) Neuropharmacology , vol.49 , pp. 850-861
    • Esslinger, C.S.1
  • 28
    • 23844450692 scopus 로고    scopus 로고
    • The excitatory amino acid transporters: Pharmacological insights on substrate and inhibitor specificity of the eaat subtypes
    • Bridges, R. J. & Esslinger, C. S. The excitatory amino acid transporters: pharmacological insights on substrate and inhibitor specificity of the EAAT subtypes. Pharmacol. Ther. 107, 271-285 (2005).
    • (2005) Pharmacol. Ther. , vol.107 , pp. 271-285
    • Bridges, R.J.1    Esslinger, C.S.2
  • 29
    • 49149120836 scopus 로고    scopus 로고
    • Synthesis and preliminary pharmacological evaluation of novel derivatives of l-b-threobenzylaspartate as inhibitors of the neuronal glutamate transporter eaat3
    • Mavencamp, T. L., Rhoderick, J. F., Bridges, R. J. & Esslinger, C. S. Synthesis and preliminary pharmacological evaluation of novel derivatives of L-b-threobenzylaspartate as inhibitors of the neuronal glutamate transporter EAAT3. Bioorg. Med. Chem. 16, 7740-7748 (2008).
    • (2008) Bioorg. Med. Chem. , vol.16 , pp. 7740-7748
    • Mavencamp, T.L.1    Rhoderick, J.F.2    Bridges, R.J.3    Esslinger, C.S.4
  • 30
    • 0034613643 scopus 로고    scopus 로고
    • Syntheses of optically pure β-hydroxyaspartate derivatives as glutamate transporter blockers
    • Shimamoto, K. et al. Syntheses of optically pure β-hydroxyaspartate derivatives as glutamate transporter blockers. Bioorg. Med. Chem. Lett. 10, 2407-2410 (2000).
    • (2000) Bioorg. Med. Chem. Lett. , vol.10 , pp. 2407-2410
    • Shimamoto, K.1
  • 31
    • 77953617184 scopus 로고    scopus 로고
    • Synthesis of orthogonally protected l-threo-b-ethoxyasparagine
    • Spengler, J., Pelay, M., Tulla-Puche, J. & Albericio, F. Synthesis of orthogonally protected L-threo-b-ethoxyasparagine. Amino Acids 39, 161-165 (2010).
    • (2010) Amino Acids , vol.39 , pp. 161-165
    • Spengler, J.1    Pelay, M.2    Tulla-Puche, J.3    Albericio, F.4
  • 32
    • 0027291987 scopus 로고
    • Design of synthetic gene libraries encoding random sequence proteins with desired ensemble characteristics
    • LaBean, T. H. & Kauffman, S. A. Design of synthetic gene libraries encoding random sequence proteins with desired ensemble characteristics. Protein Sci. 2, 1249-1254 (1993).
    • (1993) Protein Sci. , vol.2 , pp. 1249-1254
    • LaBean, T.H.1    Kauffman, S.A.2
  • 33
    • 0024520745 scopus 로고
    • Site-directed mutagenesis by overlap extension using the polymerase chain reaction
    • Ho, S. N., Hunt, H. D., Horton, R. M., Pullen, J. K. & Pease, L. R. Site-directed mutagenesis by overlap extension using the polymerase chain reaction. Gene 77, 51-59 (1989).
    • (1989) Gene , vol.77 , pp. 51-59
    • Ho, S.N.1    Hunt, H.D.2    Horton, R.M.3    Pullen, J.K.4    Pease, L.R.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.