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Volumn 77, Issue 7, 2011, Pages 2471-2478

Molecular characterization of a novel N-acetylneuraminate lyase from Lactobacillus plantarum WCFS1

Author keywords

[No Author keywords available]

Indexed keywords

ALDOLASES; ALKALINE PH; CATALYTIC EFFICIENCIES; EXPRESSION LEVELS; HIGH STABILITY; HUMAN GUTS; LACTOBACILLUS PLANTARUM; MANNOSAMINE; MOLECULAR CHARACTERIZATION; N-ACETYLNEURAMINIC ACID; PYRUVATES; SIALIC ACIDS; STABILIZING ADDITIVES; STRUCTURAL GROUPS; TEMPERATURE STABILITY;

EID: 79953291322     PISSN: 00992240     EISSN: 10985336     Source Type: Journal    
DOI: 10.1128/AEM.02927-10     Document Type: Article
Times cited : (39)

References (46)
  • 1
    • 0025860553 scopus 로고
    • Purification, crystallization and characterization of N-acetylneuraminate lyase from Escherichia coli
    • Aisaka, K., A. Igarashi, K. Yamaguchi, and T. Uwajima. 1991. Purification, crystallization and characterization of N-acetylneuraminate lyase from Escherichia coli. Biochem. J. 276:541-546.
    • (1991) Biochem. J. , vol.276 , pp. 541-546
    • Aisaka, K.1    Igarashi, A.2    Yamaguchi, K.3    Uwajima, T.4
  • 2
    • 0022626587 scopus 로고
    • Cloning and constitutive expression of the N-acetylneuraminate lyase gene of Escherichia coli
    • Aisaka, K., and T. Uwajima. 1986. Cloning and constitutive expression of the N-acetylneuraminate lyase gene of Escherichia coli. Appl. Environ. Microbiol. 51:562-565.
    • (1986) Appl. Environ. Microbiol. , vol.51 , pp. 562-565
    • Aisaka, K.1    Uwajima, T.2
  • 3
    • 67449122992 scopus 로고    scopus 로고
    • Insights into the evolution of sialic acid catabolism among bacteria
    • Almagro-Moreno, S., and E. F. Boyd. 2009. Insights into the evolution of sialic acid catabolism among bacteria. BMC Evol. Biol. 9:118-133.
    • (2009) BMC Evol. Biol. , vol.9 , pp. 118-133
    • Almagro-Moreno, S.1    Boyd, E.F.2
  • 6
    • 0033214082 scopus 로고    scopus 로고
    • Bacterial lipolytic enzymes: classification and properties
    • Arpigny, J. L., and K. E. Jaeger. 1999. Bacterial lipolytic enzymes: classification and properties. Biochem. J. 343:177-183.
    • (1999) Biochem. J. , vol.343 , pp. 177-183
    • Arpigny, J.L.1    Jaeger, K.E.2
  • 7
    • 0034721945 scopus 로고    scopus 로고
    • Active site modulation in the N-acetylneuraminate lyase sub-family as revealed by the structure of the inhibitor-complexed Haemophilus influenzae enzyme
    • Barbosa, J. A., et al. 2000. Active site modulation in the N-acetylneuraminate lyase sub-family as revealed by the structure of the inhibitor-complexed Haemophilus influenzae enzyme. J. Mol. Biol. 303:405-421.
    • (2000) J. Mol. Biol. , vol.303 , pp. 405-421
    • Barbosa, J.A.1
  • 8
    • 0032586151 scopus 로고    scopus 로고
    • Alkaline biocatalysis for the direct synthesis of N-acetyl-D-neuraminic acid (Neu5Ac) from N-acetyl-D-glucosamine (GlcNAc)
    • Blayer, S., J. M. Woodley, M. J. Dawson, and M. D. Lilly. 1999. Alkaline biocatalysis for the direct synthesis of N-acetyl-D-neuraminic acid (Neu5Ac) from N-acetyl-D-glucosamine (GlcNAc). Biotechnol. Bioeng. 66:131-136.
    • (1999) Biotechnol. Bioeng. , vol.66 , pp. 131-136
    • Blayer, S.1    Woodley, J.M.2    Dawson, M.J.3    Lilly, M.D.4
  • 9
    • 0030293657 scopus 로고    scopus 로고
    • Characterization of the chemoenzymatic synthesis of N-acetyl-D-neuraminic acid (Neu5Ac)
    • Blayer, S., J. M. Woodley, and M. D. Lilly. 1996. Characterization of the chemoenzymatic synthesis of N-acetyl-D-neuraminic acid (Neu5Ac). Biotechnol. Prog. 12:758-763.
    • (1996) Biotechnol. Prog. , vol.12 , pp. 758-763
    • Blayer, S.1    Woodley, J.M.2    Lilly, M.D.3
  • 10
    • 44549085536 scopus 로고    scopus 로고
    • Directed evolution of aldolases for exploitation in synthetic organic chemistry
    • Bolt, A., A. Berry, and A. Nelson. 2008. Directed evolution of aldolases for exploitation in synthetic organic chemistry. Arch. Biochem. Biophys. 474: 318-330.
    • (2008) Arch. Biochem. Biophys. , vol.474 , pp. 318-330
    • Bolt, A.1    Berry, A.2    Nelson, A.3
  • 11
    • 78049434868 scopus 로고    scopus 로고
    • Structural insights into substrate specificity in variants of N-acetylneuraminic acid lyase produced by directed evolution
    • Campeotto, I., et al. 2010. Structural insights into substrate specificity in variants of N-acetylneuraminic acid lyase produced by directed evolution. J. Mol. Biol. 404:56-69.
    • (2010) J. Mol. Biol. , vol.404 , pp. 56-69
    • Campeotto, I.1
  • 12
    • 73449100770 scopus 로고    scopus 로고
    • Structure of an Escherichia coli N-acetyl-D-neuraminic acid lyase mutant, E192N, in complex with pyruvate at 1.45 Å resolution. Acta Crystallogr
    • Campeotto, I., et al. 2009. Structure of an Escherichia coli N-acetyl-D-neuraminic acid lyase mutant, E192N, in complex with pyruvate at 1.45 Å resolution. Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 65:1088-1090.
    • (2009) Sect. F Struct. Biol. Cryst. Commun. , vol.65 , pp. 1088-1090
    • Campeotto, I.1
  • 13
    • 33748929006 scopus 로고    scopus 로고
    • Thermofluor-based high-throughput stability optimization of proteins for structural studies
    • Ericsson, U. B., B. M. Hallberg, G. T. DeTitta, N. Dekker, and P. Nordlund. 2006. Thermofluor-based high-throughput stability optimization of proteins for structural studies. Anal. Biochem. 357:289-298.
    • (2006) Anal. Biochem. , vol.357 , pp. 289-298
    • Ericsson, U.B.1    Hallberg, B.M.2    DeTitta, G.T.3    Dekker, N.4    Nordlund, P.5
  • 14
    • 0029902767 scopus 로고    scopus 로고
    • N-Acetyl-D-neuraminic acid lyase generates the sialic acid for colominic acid biosynthesis in Escherichia coli K1
    • Ferrero, M. A., A. Reglero, M. Fernandez-Lopez, R. Ordas, and L. B. Rodriguez-Aparicio. 1996. N-Acetyl-D-neuraminic acid lyase generates the sialic acid for colominic acid biosynthesis in Escherichia coli K1. Biochem. J. 317:157-165.
    • (1996) Biochem. J. , vol.317 , pp. 157-165
    • Ferrero, M.A.1    Reglero, A.2    Fernandez-Lopez, M.3    Ordas, R.4    Rodriguez-Aparicio, L.B.5
  • 15
    • 4043182006 scopus 로고    scopus 로고
    • Directed evolution of aldolases
    • Franke, D., C. C. Hsu, and C. H. Wong. 2004. Directed evolution of aldolases. Methods Enzymol. 388:224-238.
    • (2004) Methods Enzymol , vol.388 , pp. 224-238
    • Franke, D.1    Hsu, C.C.2    Wong, C.H.3
  • 16
    • 0032961270 scopus 로고    scopus 로고
    • ESPript: multiple sequence alignment in PostScript
    • Gouet, P., E. Courcelle, D. I. Stuart, and F. Metoz. 1999. ESPript: multiple sequence alignment in PostScript. Bioinformatics 15:305-308.
    • (1999) Bioinformatics , vol.15 , pp. 305-308
    • Gouet, P.1    Courcelle, E.2    Stuart, D.I.3    Metoz, F.4
  • 17
    • 21544473154 scopus 로고    scopus 로고
    • Directed evolution of D-sialic acid aldolase to L-3-deoxy-manno-2-octulosonic acid (L-KDO) aldolase
    • Hsu, C. C., Z. Hong, M. Wada, D. Franke, and C. H. Wong. 2005. Directed evolution of D-sialic acid aldolase to L-3-deoxy-manno-2-octulosonic acid (L-KDO) aldolase. Proc. Natl. Acad. Sci. U. S. A. 102:9122-9126.
    • (2005) Proc. Natl. Acad. Sci. U. S. A. , vol.102 , pp. 9122-9126
    • Hsu, C.C.1    Hong, Z.2    Wada, M.3    Franke, D.4    Wong, C.H.5
  • 18
    • 34250366289 scopus 로고    scopus 로고
    • Disaccharides as sialic acid aldolase substrates: synthesis of disaccharides containing a sialic acid at the reducing end
    • Huang, S., H. Yu, and X. Chen. 2007. Disaccharides as sialic acid aldolase substrates: synthesis of disaccharides containing a sialic acid at the reducing end. Angew. Chem. Int. Ed. Engl. 46:2249-2253.
    • (2007) Angew. Chem. Int. Ed. Engl. , vol.46 , pp. 2249-2253
    • Huang, S.1    Yu, H.2    Chen, X.3
  • 19
    • 0028773463 scopus 로고
    • The three-dimensional structure of N-acetylneuraminate lyase from Escherichia coli
    • Izard, T., M. C. Lawrence, R. L. Malby, G. G. Lilley, and P. M. Colman. 1994. The three-dimensional structure of N-acetylneuraminate lyase from Escherichia coli. Structure 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
  • 20
    • 0038625074 scopus 로고    scopus 로고
    • Mimicking natural evolution in vitro: an N-acetylneuraminate lyase mutant with an increased dihydrodipicolinate synthase activity
    • Joerger, A. C., S. Mayer, and A. R. Fersht. 2003. Mimicking natural evolution in vitro: an N-acetylneuraminate lyase mutant with an increased dihydrodipicolinate synthase activity. Proc. Natl. Acad. Sci. U. S. A. 100:5694-5699.
    • (2003) Proc. Natl. Acad. Sci. U. S. A. , vol.100 , pp. 5694-5699
    • Joerger, A.C.1    Mayer, S.2    Fersht, A.R.3
  • 21
    • 0019299355 scopus 로고
    • The protection role of pyruvate against heat inactivation of N-acetylneuraminate lyase
    • Kolisis, F. N., T. G. Sotiroudis, and A. E. Evangelopoulos. 1980. The protection role of pyruvate against heat inactivation of N-acetylneuraminate lyase. FEBS Lett. 121:280-282.
    • (1980) FEBS Lett , vol.121 , pp. 280-282
    • Kolisis, F.N.1    Sotiroudis, T.G.2    Evangelopoulos, A.E.3
  • 22
    • 0034819577 scopus 로고    scopus 로고
    • Characterization and mutagenesis of the recombinant N-acetylneuraminate lyase from Clostridium perfringens: insights into the reaction mechanism
    • Kruger, D., R. Schauer, and C. Traving. 2001. Characterization and mutagenesis of the recombinant N-acetylneuraminate lyase from Clostridium perfringens: insights into the reaction mechanism. Eur. J. Biochem. 268:3831-3839.
    • (2001) Eur. J. Biochem. , vol.268 , pp. 3831-3839
    • Kruger, D.1    Schauer, R.2    Traving, C.3
  • 23
    • 0031581884 scopus 로고    scopus 로고
    • Structure and mechanism of a sub-family of enzymes related to N-acetylneuraminate lyase
    • Lawrence, M. C., et al. 1997. Structure and mechanism of a sub-family of enzymes related to N-acetylneuraminate lyase. J. Mol. Biol. 266:381-399.
    • (1997) J. Mol. Biol. , vol.266 , pp. 381-399
    • Lawrence, M.C.1
  • 24
    • 46149103147 scopus 로고    scopus 로고
    • Pasteurella multocida sialic acid aldolase: a promising biocatalyst
    • Li, Y., et al. 2008. Pasteurella multocida sialic acid aldolase: a promising biocatalyst. Appl. Microbiol. Biotechnol. 79:963-970.
    • (2008) Appl. Microbiol. Biotechnol. , vol.79 , pp. 963-970
    • Li, Y.1
  • 25
    • 0032053303 scopus 로고    scopus 로고
    • Expression in Escherichia coli of the putative N-acetylneuraminate lyase gene (nanA) from Haemophilus influenzae: overproduction, purification, and crystallization
    • Lilley, G. G., J. A. Barbosa, and L. A. Pearce. 1998. Expression in Escherichia coli of the putative N-acetylneuraminate lyase gene (nanA) from Haemophilus influenzae: overproduction, purification, and crystallization. Protein Expr. Purif. 12:295-304.
    • (1998) Protein Expr. Purif. , vol.12 , pp. 295-304
    • Lilley, G.G.1    Barbosa, J.A.2    Pearce, L.A.3
  • 26
    • 0031127901 scopus 로고    scopus 로고
    • An efficient process for production of Nacetylneuraminic acid using N-acetylneuraminic acid aldolase
    • Mahmoudian, M., et al. 1997. An efficient process for production of Nacetylneuraminic acid using N-acetylneuraminic acid aldolase. Enzyme Microb. Technol. 20:393-400.
    • (1997) Enzyme Microb. Technol. , vol.20 , pp. 393-400
    • Mahmoudian, M.1
  • 27
    • 33751542139 scopus 로고    scopus 로고
    • Identifying protein construct variants with increased crystallization propensity-a case study
    • Malawaski, G. A., et al. 2006. Identifying protein construct variants with increased crystallization propensity-a case study. Protein Sci. 15:2718-2728.
    • (2006) Protein Sci , vol.15 , pp. 2718-2728
    • Malawaski, G.A.1
  • 28
    • 0029913472 scopus 로고    scopus 로고
    • Molecular characterization and expression of a N-acetylneuraminate lyase gene from Trichomonas vaginalis
    • Meysick, K. C., K. Dimock, and G. E. Garber. 1996. Molecular characterization and expression of a N-acetylneuraminate lyase gene from Trichomonas vaginalis. Mol. Biochem. Parasitol. 76:289-292.
    • (1996) Mol. Biochem. Parasitol. , vol.76 , pp. 289-292
    • Meysick, K.C.1    Dimock, K.2    Garber, G.E.3
  • 30
    • 65549128344 scopus 로고    scopus 로고
    • Characterization of a novel thermostable carboxylesterase from Geobacillus kaustophilus HTA426 shows the existence of a new carboxylesterase family
    • Montoro-García, S., et al. 2009. Characterization of a novel thermostable carboxylesterase from Geobacillus kaustophilus HTA426 shows the existence of a new carboxylesterase family. J. Bacteriol. 191:3076-3085.
    • (2009) J. Bacteriol. , vol.191 , pp. 3076-3085
    • Montoro-García, S.1
  • 31
    • 0017066374 scopus 로고
    • Purification and characterization of N-acetylneuraminate lyase from Clostridium perfringens
    • Nees, S., R. Schauer, and F. Mayer. 1976. Purification and characterization of N-acetylneuraminate lyase from Clostridium perfringens. Hoppe-Seylers Z. Physiol. Chem. 357:839-853.
    • (1976) Hoppe-Seylers Z. Physiol. Chem. , vol.357 , pp. 839-853
    • Nees, S.1    Schauer, R.2    Mayer, F.3
  • 33
    • 0022429765 scopus 로고
    • Complete nucleotide sequence of the E. coli N-acetylneuraminate lyase
    • Ohta, Y., K. Watanabe, and A. Kimura. 1985. Complete nucleotide sequence of the E. coli N-acetylneuraminate lyase. Nucleic Acids Res. 13:8843-8852.
    • (1985) Nucleic Acids Res , vol.13 , pp. 8843-8852
    • Ohta, Y.1    Watanabe, K.2    Kimura, A.3
  • 34
    • 0036172167 scopus 로고    scopus 로고
    • Geno3D: automatic comparative molecular modelling of protein
    • Ombet, C., M. Jambon, G. Deléage, and G. C. Geourjon. 2002. Geno3D: automatic comparative molecular modelling of protein. Bioinformatics 18: 213-214.
    • (2002) Bioinformatics , vol.18 , pp. 213-214
    • Ombet, C.1    Jambon, M.2    Deléage, G.3    Geourjon, G.C.4
  • 35
    • 58149187896 scopus 로고    scopus 로고
    • MODBASE, a database of annotated comparative protein structure models and associated resources
    • Pieper, U., et al. 2009. MODBASE, a database of annotated comparative protein structure models and associated resources. Nucleic Acids Res. 37: D347-D354.
    • (2009) Nucleic Acids Res , vol.37
    • Pieper, U.1
  • 37
    • 0020348005 scopus 로고
    • Chemistry, metabolism, and biological functions of sialic acids
    • Schauer, R. 1982. Chemistry, metabolism, and biological functions of sialic acids. Adv. Carbohydr. Chem. Biochem. 40:131-234.
    • (1982) Adv. Carbohydr. Chem. Biochem. , vol.40 , pp. 131-234
    • Schauer, R.1
  • 38
    • 0033496523 scopus 로고    scopus 로고
    • The terminal enzymes of sialic acid metabolism: acylneuraminate pyruvatelyases
    • Schauer, R., U. Sommer, D. Krüger, H. van Unen, and C. Traving. 1999. The terminal enzymes of sialic acid metabolism: acylneuraminate pyruvatelyases. Biosci. Rep. 19:373-383.
    • (1999) Biosci. Rep. , vol.19 , pp. 373-383
    • Schauer, R.1    Sommer, U.2    Krüger, D.3    van Unen, H.4    Traving C5
  • 39
    • 34547781750 scopus 로고    scopus 로고
    • MEGA4: Molecular Evolutionary Genetics Analysis (MEGA) software version 4.0
    • Tamura, K., J. Dudley, M. Nei, and S. Kumar. 2007. MEGA4: Molecular Evolutionary Genetics Analysis (MEGA) software version 4.0. Mol. Biol. Evol. 24:1596-1599.
    • (2007) Mol. Biol. Evol. , vol.24 , pp. 1596-1599
    • Tamura, K.1    Dudley, J.2    Nei, M.3    Kumar, S.4
  • 40
    • 0027968068 scopus 로고
    • CLUSTAL-W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position specific gap penalties and weight matrix choice
    • Thompson, J. D., D. G. Higgins, and T. J. Gibson. 1994. CLUSTAL-W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position specific gap penalties and weight matrix choice. Nucleic Acids Res. 22:4673-4680.
    • (1994) Nucleic Acids Res , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 41
    • 0030729815 scopus 로고    scopus 로고
    • Cloning, sequencing and expression of the acylneuraminate lyase gene from Clostridium perfringens A99
    • Traving, C., P. Roggentin, and R. Schauer. 1997. Cloning, sequencing and expression of the acylneuraminate lyase gene from Clostridium perfringens A99. Glycoconj. J. 14:821-830.
    • (1997) Glycoconj. J. , vol.14 , pp. 821-830
    • Traving, C.1    Roggentin, P.2    Schauer, R.3
  • 42
    • 0022344062 scopus 로고
    • Regulation of sialic acid metabolism in Escherichia coli: role of N-acetylneuraminate pyruvate-lyase
    • Vimr, E. R., and F. A. Troy. 1985. Regulation of sialic acid metabolism in Escherichia coli: role of N-acetylneuraminate pyruvate-lyase. J. Bacteriol. 164:854-860.
    • (1985) J. Bacteriol. , vol.164 , pp. 854-860
    • Vimr, E.R.1    Troy, F.A.2
  • 43
    • 33644983895 scopus 로고    scopus 로고
    • Production of 2-keto-3-deoxy-D-glycero-D-galacto-nonopyranulosonic acid (KDN) using fusion protein of N-acetyl-D-neuraminic acid aldolase
    • Wang, T. H., and W. C. Lee. 2005. Production of 2-keto-3-deoxy-D-glycero-D-galacto-nonopyranulosonic acid (KDN) using fusion protein of N-acetyl-D-neuraminic acid aldolase. Biochem. Eng. J. 29:75-80.
    • (2005) Biochem. Eng. J. , vol.29 , pp. 75-80
    • Wang, T.H.1    Lee, W.C.2
  • 45
    • 33745683530 scopus 로고    scopus 로고
    • Aldolase-catalyzed synthesis of beta-D-galp-(1→9)-D-KDN: a novel acceptor for sialyltransferases
    • Yu, H., and X. Chen. 2006. Aldolase-catalyzed synthesis of beta-D-galp-(1→9)-D-KDN: a novel acceptor for sialyltransferases. Org. Lett. 8:2393-2396.
    • (2006) Org. Lett. , vol.8 , pp. 2393-2396
    • Yu, H.1    Chen, X.2
  • 46
    • 8844258685 scopus 로고    scopus 로고
    • Chemoenzymatic synthesis of CMP-sialic acid derivatives by a one-pot two-enzyme system: comparison of substrate flexibility of three microbial CMP-sialic acid synthetases
    • Yu, H., H. Yu, R. Karpel, and X. Chen. 2004. Chemoenzymatic synthesis of CMP-sialic acid derivatives by a one-pot two-enzyme system: comparison of substrate flexibility of three microbial CMP-sialic acid synthetases. Bioorg. Med. Chem. 12:6427-6433.
    • (2004) Bioorg. Med. Chem. , vol.12 , pp. 6427-6433
    • Yu, H.1    Yu, H.2    Karpel, R.3    Chen, X.4


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