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Volumn 14, Issue 8, 2013, Pages 2657-2666

Mannuronan C-5 epimerases suited for tailoring of specific alginate structures obtained by high-throughput screening of an epimerase mutant library

Author keywords

[No Author keywords available]

Indexed keywords

BIOCHEMICAL ANALYSIS; CHEMICAL-PHYSICAL PROPERTIES; HIGH-THROUGHPUT SCREENING; ISOLATED ENZYMES; MANNURONAN C-5 EPIMERASES; MUTANT LIBRARIES; STRUCTURAL FEATURE; WILD-TYPE ENZYMES;

EID: 84881573027     PISSN: 15257797     EISSN: 15264602     Source Type: Journal    
DOI: 10.1021/bm4005194     Document Type: Article
Times cited : (30)

References (45)
  • 2
    • 84856581382 scopus 로고    scopus 로고
    • Production of glucuronic acid-based polysaccharides by microbial fermentation for biomedical applications
    • Cimini, D.; De Rosa, M.; Schiraldi, C. Production of glucuronic acid-based polysaccharides by microbial fermentation for biomedical applications Biotechnol. J. 2012, 7, 237-250
    • (2012) Biotechnol. J. , vol.7 , pp. 237-250
    • Cimini, D.1    De Rosa, M.2    Schiraldi, C.3
  • 3
    • 84856021760 scopus 로고    scopus 로고
    • Alginates as a useful natural polymer for microencapsulation and therapeutic applications
    • Goh, C. H.; Heng, P. W. S.; Chan, L. W. Alginates as a useful natural polymer for microencapsulation and therapeutic applications Carbohydr. Polym. 2012, 88, 1-12
    • (2012) Carbohydr. Polym. , vol.88 , pp. 1-12
    • Goh, C.H.1    Heng, P.W.S.2    Chan, L.W.3
  • 4
    • 80455173988 scopus 로고    scopus 로고
    • Alginate: Properties and biomedical applications
    • Lee, K. Y.; Mooney, D. J. Alginate: Properties and biomedical applications Prog. Polym. Sci. 2012, 37, 106-126
    • (2012) Prog. Polym. Sci. , vol.37 , pp. 106-126
    • Lee, K.Y.1    Mooney, D.J.2
  • 5
    • 33749025232 scopus 로고    scopus 로고
    • Bacterial alginates: From biosynthesis to applications
    • Remminghorst, U.; Rehm, B. H. Bacterial alginates: from biosynthesis to applications Biotechnol. Lett. 2006, 28, 1701-1712
    • (2006) Biotechnol. Lett. , vol.28 , pp. 1701-1712
    • Remminghorst, U.1    Rehm, B.H.2
  • 6
    • 0000258671 scopus 로고
    • Exocellular alginic acid from Azotobacter vinelandii
    • Gorin, P.; Spencer, J. Exocellular alginic acid from Azotobacter vinelandii Can. J. Microbiol. 1966, 44, 993-998
    • (1966) Can. J. Microbiol. , vol.44 , pp. 993-998
    • Gorin, P.1    Spencer, J.2
  • 7
    • 0019375273 scopus 로고
    • Isolation of alginate-producing mutants of Pseudomonas fluorescens, Pseudomonas putida and Pseudomonas mendocina
    • Govan, J. R.; Fyfe, J. A.; Jarman, T. R. Isolation of alginate-producing mutants of Pseudomonas fluorescens, Pseudomonas putida and Pseudomonas mendocina J. Gen. Microbiol. 1981, 125, 217-220
    • (1981) J. Gen. Microbiol. , vol.125 , pp. 217-220
    • Govan, J.R.1    Fyfe, J.A.2    Jarman, T.R.3
  • 8
    • 0002499476 scopus 로고    scopus 로고
    • Chemistry and physical properties of alginates
    • Smidsrød, O.; Draget, K. I. Chemistry and physical properties of alginates Carbohydr. Eur. 1996, 14, 6-13
    • (1996) Carbohydr. Eur. , vol.14 , pp. 6-13
    • Smidsrød, O.1    Draget, K.I.2
  • 9
    • 0034838734 scopus 로고    scopus 로고
    • Hexuronyl C5-epimerases in alginate and glycosaminoglycan biosynthesis
    • Valla, S.; Li, J.; ErtesvaÌŠg, H.; Barbeyron, T.; Lindahl, U. Hexuronyl C5-epimerases in alginate and glycosaminoglycan biosynthesis Biochimie 2001, 83, 819-830
    • (2001) Biochimie , vol.83 , pp. 819-830
    • Valla, S.1    Li, J.2    Ertesvaìšg, H.3    Barbeyron, T.4    Lindahl, U.5
  • 10
    • 0028285749 scopus 로고
    • Cloning and expression of an Azotobacter vinelandii mannuronan C-5-epiemrase gene
    • ErtesvaÌŠg, H.; Doseth, B.; Larsen, B.; SkjaÌŠk-Bræk, G.; Valla, S. Cloning and expression of an Azotobacter vinelandii mannuronan C-5-epiemrase gene J. Bacteriol. 1994, 176, 2846-2853
    • (1994) J. Bacteriol. , vol.176 , pp. 2846-2853
    • Ertesvaìšg, H.1    Doseth, B.2    Larsen, B.3    Skjaìšk- Bræk, G.4    Valla, S.5
  • 11
    • 0029059225 scopus 로고
    • A family of modular type mannuronan C-5-epimerase genes controls alginate structure in Azotobacter vinelandii
    • ErtesvaÌŠg, H.; Høidal, H. K.; Hals, I. K.; Rian, A.; Doseth, B.; Valla, S. A family of modular type mannuronan C-5-epimerase genes controls alginate structure in Azotobacter vinelandii Mol. Microbiol. 1995, 16, 719-731
    • (1995) Mol. Microbiol. , vol.16 , pp. 719-731
    • Ertesvaìšg, H.1    Høidal, H.K.2    Hals, I.K.3    Rian, A.4    Doseth, B.5    Valla, S.6
  • 12
    • 0344196983 scopus 로고    scopus 로고
    • Cloning and expression of three new Azotobacter vinelandii genes closely related to a previously described gene family encoding mannuronan C-5-epimerases
    • Svanem, B. I. G.; SkjaÌŠk-Bræk, G.; ErtesvaÌŠg, H.; Valla, S. Cloning and expression of three new Azotobacter vinelandii genes closely related to a previously described gene family encoding mannuronan C-5-epimerases J. Bacteriol. 1999, 181, 68-77
    • (1999) J. Bacteriol. , vol.181 , pp. 68-77
    • Svanem, B.I.G.1    Skjaìšk-Bræk, G.2    Ertesvaìš g, H.3    Valla, S.4
  • 13
    • 0034541024 scopus 로고    scopus 로고
    • Mannuronan C-5 epimerases and cellular differentiation of Azotobacter vinelandii
    • Høidal, H. K.; Glærum Svanem, B. I.; Gimmestad, M.; Valla, S. Mannuronan C-5 epimerases and cellular differentiation of Azotobacter vinelandii Environ. Microbiol. 2000, 2, 27-38
    • (2000) Environ. Microbiol. , vol.2 , pp. 27-38
    • Høidal, H.K.1    Glærum Svanem, B.I.2    Gimmestad, M.3    Valla, S.4
  • 14
    • 0036165561 scopus 로고    scopus 로고
    • Mode of action of recombinant Azotobacter vinelandii mannuronan C-5 epimerases AlgE2 and AlgE4
    • Hartmann, M.; Holm, O. B.; Johansen, G. A.; SkjaÌŠk- Bræk, G.; Stokke, B. T. Mode of action of recombinant Azotobacter vinelandii mannuronan C-5 epimerases AlgE2 and AlgE4 Biopolymers 2002, 63, 77-88
    • (2002) Biopolymers , vol.63 , pp. 77-88
    • Hartmann, M.1    Holm, O.B.2    Johansen, G.A.3    Skjaìšk-Bræk, G.4    Stokke, B.T.5
  • 16
    • 0033617262 scopus 로고    scopus 로고
    • The recombinant Azotobacter vinelandii mannuronan C-5-epimerase AlgE4 epimerizes alginate by a nonrandom attack mechanism
    • Høidal, H. K.; ErtesvaÌŠg, H.; SkjaÌŠ k-Bræk, G.; Stokke, B. T.; Valla, S. The recombinant Azotobacter vinelandii mannuronan C-5-epimerase AlgE4 epimerizes alginate by a nonrandom attack mechanism J. Biol. Chem. 1999, 274, 12316-12322
    • (1999) J. Biol. Chem. , vol.274 , pp. 12316-12322
    • Høidal, H.K.1    Ertesvaìšg, H.2    Skjaìšk- Bræk, G.3    Stokke, B.T.4    Valla, S.5
  • 17
    • 0033156681 scopus 로고    scopus 로고
    • Mannuronan C-5-epimerases and their application for in vitro and in vivo design of new alginates useful in biotechnology
    • ErtesvaÌŠg, H.; Høidal, H. K.; Schjerven, H.; Svanem, B. I.; Valla, S. Mannuronan C-5-epimerases and their application for in vitro and in vivo design of new alginates useful in biotechnology Metab. Eng. 1999, 1, 262-269
    • (1999) Metab. Eng. , vol.1 , pp. 262-269
    • Ertesvaìšg, H.1    Høidal, H.K.2    Schjerven, H.3    Svanem, B.I.4    Valla, S.5
  • 18
    • 0035943715 scopus 로고    scopus 로고
    • The catalytic activities of the bifunctional Azotobacter vinelandii mannuronan C-5-epimerase and alginate lyase AlgE7 probably originate from the same active site in the enzyme
    • Svanem, B. I. G.; Strand, W. I.; ErtesvaÌŠg, H.; SkjaÌŠk-Bræk, G.; Hartmann, M.; Barbeyron, T.; Valla, S. The catalytic activities of the bifunctional Azotobacter vinelandii mannuronan C-5-epimerase and alginate lyase AlgE7 probably originate from the same active site in the enzyme J. Biol. Chem. 2001, 276, 31542-31550
    • (2001) J. Biol. Chem. , vol.276 , pp. 31542-31550
    • Svanem, B.I.G.1    Strand, W.I.2    Ertesvaìšg, H.3    Skjaìšk-Bræk, G.4    Hartmann, M.5    Barbeyron, T.6    Valla, S.7
  • 19
    • 53049084215 scopus 로고    scopus 로고
    • Structural and mutational characterization of the catalytic A-module of the mannuronan C-5-epimerase AlgE4 from Azotobacter vinelandii
    • Rozeboom, H. J.; Bjerkan, T. M.; Kalk, K. H.; ErtesvaÌŠg, H.; Holtan, S.; Aachmann, F. L.; Valla, S.; Dijkstra, B. W. Structural and mutational characterization of the catalytic A-module of the mannuronan C-5-epimerase AlgE4 from Azotobacter vinelandii J. Biol. Chem. 2008, 283, 23819-23828
    • (2008) J. Biol. Chem. , vol.283 , pp. 23819-23828
    • Rozeboom, H.J.1    Bjerkan, T.M.2    Kalk, K.H.3    Ertesvaìšg, H.4    Holtan, S.5    Aachmann, F.L.6    Valla, S.7    Dijkstra, B.W.8
  • 20
    • 33646364570 scopus 로고    scopus 로고
    • NMR structure of the R-module - A parallel beta-roll subunit from an Azotobacter vinelandii mannuronan C-5 epimerase
    • Aachmann, F. L.; Svanem, B. I. G.; Guntert, P.; Petersen, S. B.; Valla, S.; Wimmer, R. NMR structure of the R-module-A parallel beta-roll subunit from an Azotobacter vinelandii mannuronan C-5 epimerase J. Biol. Chem. 2006, 281, 7350-7356
    • (2006) J. Biol. Chem. , vol.281 , pp. 7350-7356
    • Aachmann, F.L.1    Svanem, B.I.G.2    Guntert, P.3    Petersen, S.B.4    Valla, S.5    Wimmer, R.6
  • 21
    • 84881599665 scopus 로고    scopus 로고
    • Alginates: Existing and Potential Biotechnological and Medical Applications
    • Royal Society of Chemistry: Cambridge, U.K.
    • Draget, K. I.;; SkjaÌŠk-Bræk, G. Alginates: Existing and Potential Biotechnological and Medical Applications. In Renewable Resources for Functional Polymers and Biomaterials; Royal Society of Chemistry: Cambridge, U.K., 2011.
    • (2011) Renewable Resources for Functional Polymers and Biomaterials
    • Draget, K.I.1    Skjaìšk-Bræk, G.2
  • 22
    • 84881570489 scopus 로고    scopus 로고
    • Alginate structure function relationships relevant to their use for cell encapsulation
    • Transworld Research Network: Kerala, India
    • Mørck, Y. A.;; Strand, B. L.;; SkjaÌŠk-Bræk, G. Alginate structure function relationships relevant to their use for cell encapsulation. In The Bioartificial Endocrine Pancreas; Transworld Research Network: Kerala, India, 2009; pp 51-66.
    • (2009) The Bioartificial Endocrine Pancreas , pp. 51-66
    • Mørck, Y.A.1    Strand, B.L.2    Skjaìšk-Bræk, G.3
  • 23
    • 34948910804 scopus 로고    scopus 로고
    • Molecular engineering as an approach to design new functional properties of alginate
    • Morch, Y. A.; Donati, I.; Strand, B. L.; SkjaÌŠk- Bræk, G. Molecular engineering as an approach to design new functional properties of alginate Biomacromolecules 2007, 8, 2809-2814
    • (2007) Biomacromolecules , vol.8 , pp. 2809-2814
    • Morch, Y.A.1    Donati, I.2    Strand, B.L.3    Skjaìšk-Bræk, G.4
  • 24
    • 3142708162 scopus 로고    scopus 로고
    • Construction and analyses of hybrid Azotobacter vinelandii mannuronan C-5 epimerases with new epimerization pattern characteristics
    • Bjerkan, T. M.; Lillehov, B. E.; Strand, W. I.; SkjaÌŠk- Bræk, G.; Valla, S.; ErtesvaÌŠg, H. Construction and analyses of hybrid Azotobacter vinelandii mannuronan C-5 epimerases with new epimerization pattern characteristics Biochem. J. 2004, 381, 813-821
    • (2004) Biochem. J. , vol.381 , pp. 813-821
    • Bjerkan, T.M.1    Lillehov, B.E.2    Strand, W.I.3    Skjaìšk-Bræk, G.4    Valla, S.5    Ertesvaìšg, H.6
  • 27
    • 33746280344 scopus 로고    scopus 로고
    • Characterization of the hydrolysis mechanism of polyalternating alginate in weak acid and assignment of the resulting MG-oligosaccharides by NMR spectroscopy and ESI-mass spectrometry
    • Holtan, S.; Zhang, Q.; Strand, W. I.; SkjaÌŠk-Bræk, G. Characterization of the hydrolysis mechanism of polyalternating alginate in weak acid and assignment of the resulting MG-oligosaccharides by NMR spectroscopy and ESI-mass spectrometry Biomacromolecules 2006, 7, 2108-2121
    • (2006) Biomacromolecules , vol.7 , pp. 2108-2121
    • Holtan, S.1    Zhang, Q.2    Strand, W.I.3    Skjaìšk-Bræk, G.4
  • 28
    • 0000673566 scopus 로고
    • Studies on the sequence of uronic acid residues in alginic acid
    • Haug, A.; Larsen, B.; Smidsrød, O. Studies on the sequence of uronic acid residues in alginic acid Acta Chem. Scand. 1967, 21, 691-704
    • (1967) Acta Chem. Scand. , vol.21 , pp. 691-704
    • Haug, A.1    Larsen, B.2    Smidsrød, O.3
  • 29
    • 49549148780 scopus 로고
    • Uronic acid sequence in alginate from different sources
    • Haug, A.; Larsen, B.; Smidsrød, O. Uronic acid sequence in alginate from different sources Carbohydr. Res. 1974, 32, 217-225
    • (1974) Carbohydr. Res. , vol.32 , pp. 217-225
    • Haug, A.1    Larsen, B.2    Smidsrød, O.3
  • 30
    • 84855572226 scopus 로고    scopus 로고
    • Alginate sequencing: An analysis of block distribution in alginates using novel specific alginate degrading enzymes
    • Aarstad, O. A.; Tøndervik, A.; Sletta, H.; SkjaÌŠk- Bræk, G. Alginate sequencing: An analysis of block distribution in alginates using novel specific alginate degrading enzymes Biomacromolecules 2012, 113, 106-116
    • (2012) Biomacromolecules , vol.113 , pp. 106-116
    • Aarstad, O.A.1    Tøndervik, A.2    Sletta, H.3    Skjaìšk- Bræk, G.4
  • 33
    • 32144432437 scopus 로고    scopus 로고
    • The Swiss-Model workspace: A web-based environment for protein structure homology modelling
    • Arnold, K.; Bordoli, L.; Kopp, J.; Schwede, T. The Swiss-Model workspace: a web-based environment for protein structure homology modelling Bioinformatics 2006, 22, 195-201
    • (2006) Bioinformatics , vol.22 , pp. 195-201
    • Arnold, K.1    Bordoli, L.2    Kopp, J.3    Schwede, T.4
  • 35
    • 0029004590 scopus 로고
    • Protein modeling by e-mail
    • Peitsch, M. C. Protein modeling by e-mail Nat. Biotechnol. 1995, 13, 658-660
    • (1995) Nat. Biotechnol. , vol.13 , pp. 658-660
    • Peitsch, M.C.1
  • 36
    • 84881567099 scopus 로고    scopus 로고
    • DeLano Scientific: San Carlos, CA
    • DeLano, W. L. The PyMOL User's Manual; DeLano Scientific: San Carlos, CA, 2002; Vol. 228, pp 313-314.
    • (2002) The PyMOL User's Manual , vol.228 , pp. 313-314
    • Delano, W.L.1
  • 37
    • 0027968068 scopus 로고
    • ClustalW-improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson, J. D.; Higgins, D. G.; Gibson, T. J. ClustalW-improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice Nucleic Acids Res. 1994, 22, 4673-4680
    • (1994) Nucleic Acids Res. , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 38
    • 0030203863 scopus 로고    scopus 로고
    • TreeView: An application to display phylogenetic trees on personal computers
    • Page, R. D. M. TreeView: An application to display phylogenetic trees on personal computers Comput. Appl. Biosci. 1996, 12, 357-358
    • (1996) Comput. Appl. Biosci. , vol.12 , pp. 357-358
    • Page, R.D.M.1
  • 39
    • 0035943715 scopus 로고    scopus 로고
    • The catalytic activities of the bifunctional Azotobacter vinelandii mannuronan C-5-epimerase and alginate lyase AlgE7 probably originate from the same active site in the enzyme
    • Svanem, B. I. G.; Strand, W. I.; ErtesvaÌŠg, H.; SkjaÌŠk-Bræk, G.; Hartmann, M.; Barbeyron, T.; Valla, S. The catalytic activities of the bifunctional Azotobacter vinelandii mannuronan C-5-epimerase and alginate lyase AlgE7 probably originate from the same active site in the enzyme J. Biol. Chem. 2001, 276, 31542-31550
    • (2001) J. Biol. Chem. , vol.276 , pp. 31542-31550
    • Svanem, B.I.G.1    Strand, W.I.2    Ertesvaìšg, H.3    Skjaìšk-Bræk, G.4    Hartmann, M.5    Barbeyron, T.6    Valla, S.7
  • 40
    • 0025698196 scopus 로고
    • Kinetics and specificity of alginate lyases: Part I, a case study
    • Haugen, F.; Kortner, F.; Larsen, B. Kinetics and specificity of alginate lyases: Part I, a case study Carbohydr. Res. 1990, 198, 101-109
    • (1990) Carbohydr. Res. , vol.198 , pp. 101-109
    • Haugen, F.1    Kortner, F.2    Larsen, B.3
  • 41
    • 0017521669 scopus 로고
    • Isolation of poly-alpha-L-guluronate lyase from Klebsiella aerogenes
    • Boyd, J.; Turvey, J. R. Isolation of poly-alpha-L-guluronate lyase from Klebsiella aerogenes Carbohydr. Res. 1977, 57, 163-171
    • (1977) Carbohydr. Res. , vol.57 , pp. 163-171
    • Boyd, J.1    Turvey, J.R.2
  • 43
    • 17344382101 scopus 로고    scopus 로고
    • Catalytic properties and specificity of a recombinant, overexpressed D-mannuronate lyase
    • Chavagnat, F.; Heyraud, A.; Colin-Morel, P.; Guinand, M.; Wallach, J. Catalytic properties and specificity of a recombinant, overexpressed D-mannuronate lyase Carbohydr. Res. 1998, 308, 409-415
    • (1998) Carbohydr. Res. , vol.308 , pp. 409-415
    • Chavagnat, F.1    Heyraud, A.2    Colin-Morel, P.3    Guinand, M.4    Wallach, J.5
  • 44
    • 33645756079 scopus 로고    scopus 로고
    • Mode of action and subsite studies of the guluronan block-forming mannuronan C-5 epimerases AlgE1 and AlgE6
    • Holtan, S.; Bruheim, P.; SkjaÌŠk-Bræk, G. Mode of action and subsite studies of the guluronan block-forming mannuronan C-5 epimerases AlgE1 and AlgE6 Biochem. J. 2006, 395, 319-329
    • (2006) Biochem. J. , vol.395 , pp. 319-329
    • Holtan, S.1    Bruheim, P.2    Skjaìšk-Bræk, G.3


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