메뉴 건너뛰기




Volumn 404, Issue 1, 2010, Pages 56-69

Structural insights into substrate specificity in variants of N-acetylneuraminic acid lyase produced by directed evolution

Author keywords

Directed evolution; N acetylneuraminic acid lyase; Protein engineering; Substrate specificity; X ray crystallography

Indexed keywords

2,3,4 TRIHYDROXY N,N DIPROPYLBUTANAMIDE; BACTERIAL ENZYME; LYASE; LYASE INHIBITOR; N ACETYLNEURAMINATE LYASE; PYRUVIC ACID; UNCLASSIFIED DRUG;

EID: 78049434868     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2010.08.008     Document Type: Article
Times cited : (28)

References (34)
  • 1
    • 20844460916 scopus 로고    scopus 로고
    • Structure-guided saturation mutagenesis of N-acetylneuraminic acid lyase for the synthesis of sialic acid mimetics
    • Williams G.J., Woodhall T., Nelson A., Berry A. Structure-guided saturation mutagenesis of N-acetylneuraminic acid lyase for the synthesis of sialic acid mimetics. Protein Eng. Des. Sel. 2005, 18:239-246.
    • (2005) Protein Eng. Des. Sel. , vol.18 , pp. 239-246
    • Williams, G.J.1    Woodhall, T.2    Nelson, A.3    Berry, A.4
  • 2
    • 33845586873 scopus 로고
    • Plenum Publishing Corp., New York, NY, A. Rosenberg, C.L. Schengrund (Eds.)
    • McGuire E.J. The Biology of Sialic Acids 1976, Plenum Publishing Corp., New York, NY. A. Rosenberg, C.L. Schengrund (Eds.).
    • (1976) The Biology of Sialic Acids
    • McGuire, E.J.1
  • 3
    • 0003631621 scopus 로고
    • Plenum Press, New York, NY, A. Rosenberg (Ed.)
    • Biology of the Sialic Acids 1995, Plenum Press, New York, NY. A. Rosenberg (Ed.).
    • (1995) Biology of the Sialic Acids
  • 4
    • 0030774869 scopus 로고    scopus 로고
    • Synthesis of a novel sialic acid derivative (sialylphospholipid) as an antirotaviral agent
    • Koketsu M., Nitoda T., Sugino H., Juneja L.R., Kim M., Yamamoto T., et al. Synthesis of a novel sialic acid derivative (sialylphospholipid) as an antirotaviral agent. J. Med. Chem. 1997, 40:3332-3335.
    • (1997) J. Med. Chem. , vol.40 , pp. 3332-3335
    • Koketsu, M.1    Nitoda, T.2    Sugino, H.3    Juneja, L.R.4    Kim, M.5    Yamamoto, T.6
  • 5
    • 67650766460 scopus 로고    scopus 로고
    • Synthetic sialic-acid-containing polyvalent antiviral inhibitors
    • Carlescu I., Scutaru D., Popa M., Uglea C.V. Synthetic sialic-acid-containing polyvalent antiviral inhibitors. Med. Chem. Res. 2009, 18:477-494.
    • (2009) Med. Chem. Res. , vol.18 , pp. 477-494
    • Carlescu, I.1    Scutaru, D.2    Popa, M.3    Uglea, C.V.4
  • 6
    • 0034699492 scopus 로고    scopus 로고
    • BCX-1812 (RWJ-270201): discovery of a novel, highly potent, orally active, and selective influenza neuraminidase inhibitor through structure-based drug design
    • Babu Y.S., Chand P., Bantia S., Kotian P., Dehghani A., El-Kattan Y., et al. BCX-1812 (RWJ-270201): discovery of a novel, highly potent, orally active, and selective influenza neuraminidase inhibitor through structure-based drug design. J. Med. Chem. 2000, 43:3482-3486.
    • (2000) J. Med. Chem. , vol.43 , pp. 3482-3486
    • Babu, Y.S.1    Chand, P.2    Bantia, S.3    Kotian, P.4    Dehghani, A.5    El-Kattan, Y.6
  • 7
  • 8
    • 0029109703 scopus 로고
    • Enzymes in organic synthesis: application to the problems of carbohydrate recognition (Part 1)
    • Wong C.H., Halcomb R.L., Ichikawa Y., Kajimoto T. Enzymes in organic synthesis: application to the problems of carbohydrate recognition (Part 1). Angew. Chem. Int. Ed. 1995, 34:412-432.
    • (1995) Angew. Chem. Int. Ed. , vol.34 , pp. 412-432
    • Wong, C.H.1    Halcomb, R.L.2    Ichikawa, Y.3    Kajimoto, T.4
  • 9
    • 0033524883 scopus 로고    scopus 로고
    • Substrate-assisted catalysis in sialic acid aldolase
    • Smith B.J., Lawrence M.C., Barbosa J.A.R.G. Substrate-assisted catalysis in sialic acid aldolase. J. Org. Chem. 1999, 64:945-949.
    • (1999) J. Org. Chem. , vol.64 , pp. 945-949
    • Smith, B.J.1    Lawrence, M.C.2    Barbosa, J.A.R.G.3
  • 10
    • 6344289413 scopus 로고    scopus 로고
    • The structural basis for substrate promiscuity in 2-keto-3-deoxygluconate aldolase from the Entner-Doudoroff pathway in Sulfolobus solfataricus
    • Theodossis A., Walden H., Westwick E.J., Connaris H., Lamble H.J., Hough D.W., et al. The structural basis for substrate promiscuity in 2-keto-3-deoxygluconate aldolase from the Entner-Doudoroff pathway in Sulfolobus solfataricus. J. Biol. Chem. 2004, 279:43886-43892.
    • (2004) J. Biol. Chem. , vol.279 , pp. 43886-43892
    • Theodossis, A.1    Walden, H.2    Westwick, E.J.3    Connaris, H.4    Lamble, H.J.5    Hough, D.W.6
  • 12
    • 17044367480 scopus 로고    scopus 로고
    • Creation of a tailored aldolase for the parallel synthesis of sialic acid mimetics
    • Woodhall T., Williams G.J., Berry A., Nelson A. Creation of a tailored aldolase for the parallel synthesis of sialic acid mimetics. Angew. Chem. Int. Ed. 2005, 44:2109-2112.
    • (2005) Angew. Chem. Int. Ed. , vol.44 , pp. 2109-2112
    • Woodhall, T.1    Williams, G.J.2    Berry, A.3    Nelson, A.4
  • 13
    • 0026530319 scopus 로고
    • Elucidation of the topological parameters of N-acetylneuraminic acid and some analogues involved in their interaction with the N-acetylneuraminate lyase from Clostridium perfringens
    • Zbiral E., Kleineidam R.G., Schreiner E., Hartmann M., Christian R., Schauer R. Elucidation of the topological parameters of N-acetylneuraminic acid and some analogues involved in their interaction with the N-acetylneuraminate lyase from Clostridium perfringens. Biochem. J. 1992, 282:511-516.
    • (1992) Biochem. J. , vol.282 , pp. 511-516
    • Zbiral, E.1    Kleineidam, R.G.2    Schreiner, E.3    Hartmann, M.4    Christian, R.5    Schauer, R.6
  • 14
    • 0028773463 scopus 로고
    • The three-dimensional structure of N-acetylneuraminate lyase from Escherichia coli
    • Izard T., Lawrence M.C., Malby R.L., Lilley G.G., Colman P.M. The three-dimensional structure of N-acetylneuraminate lyase from Escherichia coli. Structure 1994, 2:361-369.
    • (1994) Structure , vol.2 , pp. 361-369
    • Izard, T.1    Lawrence, M.C.2    Malby, R.L.3    Lilley, G.G.4    Colman, P.M.5
  • 16
    • 0034721945 scopus 로고    scopus 로고
    • Active site modulation in the N-acetylneuraminate lyase subfamily as revealed by the structure of the inhibitor-complexed Haemophilus influenzae enzyme
    • Barbosa J.A.R.G., Smith B.J., DeGori R., Ooi H.C., Marcuccio S.M., Campi E.M., et al. Active site modulation in the N-acetylneuraminate lyase subfamily as revealed by the structure of the inhibitor-complexed Haemophilus influenzae enzyme. J. Mol. Biol. 2000, 303:405-421.
    • (2000) J. Mol. Biol. , vol.303 , pp. 405-421
    • Barbosa, J.A.R.G.1    Smith, B.J.2    DeGori, R.3    Ooi, H.C.4    Marcuccio, S.M.5    Campi, E.M.6
  • 17
    • 0016810498 scopus 로고
    • Structure of chicken muscle triose-phosphate isomerase determined crystallographically at 2.5 Å resolution using amino acid sequence data
    • Banner D.W., Bloomer A.C., Petsko G.A., Phillips D.C., Pogson C.I., Wilson I.A., et al. Structure of chicken muscle triose-phosphate isomerase determined crystallographically at 2.5 Å resolution using amino acid sequence data. Nature 1975, 255:609-614.
    • (1975) Nature , vol.255 , pp. 609-614
    • Banner, D.W.1    Bloomer, A.C.2    Petsko, G.A.3    Phillips, D.C.4    Pogson, C.I.5    Wilson, I.A.6
  • 18
    • 0038625074 scopus 로고    scopus 로고
    • Mimicking natural evolution in vitro: an N-acetylneuraminic acid lyase mutant with an increased dihydrodipicolinate synthase activity
    • Joerger A.C., Mayer S., Fersht A.R. Mimicking natural evolution in vitro: an N-acetylneuraminic acid lyase mutant with an increased dihydrodipicolinate synthase activity. Proc. Natl Acad. Sci. USA 2003, 100:5694-5699.
    • (2003) Proc. Natl Acad. Sci. USA , vol.100 , pp. 5694-5699
    • Joerger, A.C.1    Mayer, S.2    Fersht, A.R.3
  • 20
    • 18844391810 scopus 로고    scopus 로고
    • Synthesis of screening substrates for the directed evolution of sialic acid aldolase: towards tailored enzymes for the preparation of influenza A inhibitor analogues
    • Woodhall T., Williams G.J., Berry A., Nelson A. Synthesis of screening substrates for the directed evolution of sialic acid aldolase: towards tailored enzymes for the preparation of influenza A inhibitor analogues. Org. Biomol. Chem. 2005, 3:1795-1800.
    • (2005) Org. Biomol. Chem. , vol.3 , pp. 1795-1800
    • Woodhall, T.1    Williams, G.J.2    Berry, A.3    Nelson, A.4
  • 21
    • 60149098165 scopus 로고    scopus 로고
    • Structural basis for catalysis of a tetrameric class IIa fructose 1,6-bisphosphate aldolase from Mycobacterium tuberculosis
    • Pegan S.D., Rukseree K., Franzblau S.G., Mesecar A.D. Structural basis for catalysis of a tetrameric class IIa fructose 1,6-bisphosphate aldolase from Mycobacterium tuberculosis. J. Mol. Biol. 2009, 386:1038-1053.
    • (2009) J. Mol. Biol. , vol.386 , pp. 1038-1053
    • Pegan, S.D.1    Rukseree, K.2    Franzblau, S.G.3    Mesecar, A.D.4
  • 22
    • 4944240750 scopus 로고    scopus 로고
    • Narrowing substrate specificity in a directly evolved enzyme: the A293D mutant of aspartate aminotransferase
    • Chow M.A., McElroy K.E., Corbett K.D., Berger J.M., Kirsch J.F. Narrowing substrate specificity in a directly evolved enzyme: the A293D mutant of aspartate aminotransferase. Biochemistry 2004, 43:12780-12787.
    • (2004) Biochemistry , vol.43 , pp. 12780-12787
    • Chow, M.A.1    McElroy, K.E.2    Corbett, K.D.3    Berger, J.M.4    Kirsch, J.F.5
  • 23
    • 0033593453 scopus 로고    scopus 로고
    • Redesigning the substrate specificity of an enzyme by cumulative effects of the mutations of non-active site residues
    • Oue S., Okamoto A., Yano T., Kagamiyama H. Redesigning the substrate specificity of an enzyme by cumulative effects of the mutations of non-active site residues. J. Biol. Chem. 1999, 274:2344-2349.
    • (1999) J. Biol. Chem. , vol.274 , pp. 2344-2349
    • Oue, S.1    Okamoto, A.2    Yano, T.3    Kagamiyama, H.4
  • 24
    • 71149114259 scopus 로고    scopus 로고
    • Directed evolution and structural characterisation of a simvastatin synthase
    • Gao X., Xie X., Pashkov I., Sawaya M.R., Laidman J., Zhang W., et al. Directed evolution and structural characterisation of a simvastatin synthase. Chem. Biol. 2009, 16:1064-1074.
    • (2009) Chem. Biol. , vol.16 , pp. 1064-1074
    • Gao, X.1    Xie, X.2    Pashkov, I.3    Sawaya, M.R.4    Laidman, J.5    Zhang, W.6
  • 25
    • 67650547522 scopus 로고    scopus 로고
    • Directed evolution of an enantioselective epoxide hydrolase: uncovering the source of enantioselectivity at each evolutionary stage
    • Reetz M.T., Bocola M., Wang L.W., Sanchis J., Cronin A., Arand M., et al. Directed evolution of an enantioselective epoxide hydrolase: uncovering the source of enantioselectivity at each evolutionary stage. J. Am. Chem. Soc. 2009, 131:7334-7343.
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 7334-7343
    • Reetz, M.T.1    Bocola, M.2    Wang, L.W.3    Sanchis, J.4    Cronin, A.5    Arand, M.6
  • 26
    • 0001571983 scopus 로고
    • Comparative studies of liver and muscle aldolase: II. Immunochemical and chromatographic differentiation
    • Blostein R., Rutter W.J. Comparative studies of liver and muscle aldolase: II. Immunochemical and chromatographic differentiation. J. Biol. Chem. 1963, 238:3280-3285.
    • (1963) J. Biol. Chem. , vol.238 , pp. 3280-3285
    • Blostein, R.1    Rutter, W.J.2
  • 27
    • 33644874235 scopus 로고    scopus 로고
    • The integration of macromolecular diffraction data
    • Leslie A.G. The integration of macromolecular diffraction data. Acta Crystallogr. Sect. D 2006, 62:48-57.
    • (2006) Acta Crystallogr. Sect. D , vol.62 , pp. 48-57
    • Leslie, A.G.1
  • 28
    • 33644875355 scopus 로고    scopus 로고
    • Scaling and assessment of data quality
    • Evans P. Scaling and assessment of data quality. Acta Crystallogr. Sect. D 2006, 62:72-82.
    • (2006) Acta Crystallogr. Sect. D , vol.62 , pp. 72-82
    • Evans, P.1
  • 29
    • 0028103275 scopus 로고
    • The CCP4 suite: programs for protein crystallography
    • CCP4
    • CCP4 The CCP4 suite: programs for protein crystallography. Acta Crystallogr. Sect. D 1994, 50:760-763.
    • (1994) Acta Crystallogr. Sect. D , vol.50 , pp. 760-763
  • 30
    • 33846426122 scopus 로고    scopus 로고
    • Solving structures of protein complexes by molecular replacement with Phaser
    • McCoy A.J. Solving structures of protein complexes by molecular replacement with Phaser. Acta Crystallogr. Sect. D 2007, 63:32-41.
    • (2007) Acta Crystallogr. Sect. D , vol.63 , pp. 32-41
    • McCoy, A.J.1
  • 31
    • 0030924992 scopus 로고    scopus 로고
    • Refinement of macromolecular structures by the maximum-likelihood method
    • Murshudov G.N., Vagin A.A., Dodson E.J. Refinement of macromolecular structures by the maximum-likelihood method. Acta Crystallogr. Sect. D 1997, 53:240-255.
    • (1997) Acta Crystallogr. Sect. D , vol.53 , pp. 240-255
    • Murshudov, G.N.1    Vagin, A.A.2    Dodson, E.J.3
  • 33
    • 7544226311 scopus 로고    scopus 로고
    • PRODRG: a tool for high-throughput crystallography of protein-ligand complexes
    • Schuettelkopf A.W., van Aalten D.M.F. PRODRG: a tool for high-throughput crystallography of protein-ligand complexes. Acta Crystallogr. Sect. D 2004, 60:1355-1363.
    • (2004) Acta Crystallogr. Sect. D , vol.60 , pp. 1355-1363
    • Schuettelkopf, A.W.1    van Aalten, D.M.F.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.