메뉴 건너뛰기




Volumn 181, Issue 2, 1999, Pages 375-381

Sequence analysis of the gene encoding amylosucrase from Neisseria polysaccharea and characterization of the recombinant enzyme

Author keywords

[No Author keywords available]

Indexed keywords

AMYLASE; AMYLSUCRASE; BACTERIAL ENZYME; DEXTRANSUCRASE; GLUCAN; GLUCOSE; GLUCOSYLTRANSFERASE; GLUTATHIONE TRANSFERASE; GLYCOGEN; HYBRID PROTEIN; RECOMBINANT ENZYME; SEPHAROSE; UNCLASSIFIED DRUG;

EID: 0032947594     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/jb.181.2.375-381.1999     Document Type: Article
Times cited : (114)

References (44)
  • 1
    • 84989036066 scopus 로고
    • Conformational contributions of amylose and amylopectin to the structural properties of starches from various sources
    • Aberle, T., W. Burchard, W. Vorwerg, and S. Radosta. 1994. Conformational contributions of amylose and amylopectin to the structural properties of starches from various sources. Starch 46:329-335.
    • (1994) Starch , vol.46 , pp. 329-335
    • Aberle, T.1    Burchard, W.2    Vorwerg, W.3    Radosta, S.4
  • 3
    • 0040577395 scopus 로고    scopus 로고
    • Macromolecular features of starches determined by aqueous high-performance size exclusion chromatography
    • Bello-Perez, A., P. Roger, B. Baud, and P. Colonna. 1998. Macromolecular features of starches determined by aqueous high-performance size exclusion chromatography. J. Cereal Sci. 27:267-278.
    • (1998) J. Cereal Sci. , vol.27 , pp. 267-278
    • Bello-Perez, A.1    Roger, P.2    Baud, B.3    Colonna, P.4
  • 4
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantification of microgram quantities utilizing the principle of protein-dye binding
    • Bradford, M. M. 1976. A rapid and sensitive method for the quantification of microgram quantities utilizing the principle of protein-dye binding. Anal. Biochem. 72:248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 5
    • 0142067190 scopus 로고    scopus 로고
    • Cloning and characterization of the gene for amylosucrase from Neisseria polysaccharea: Production of a linear α-1,4-glucan
    • Büttcher, V., T. Welsh, L. Willmitzer, and J. Kossmann. 1997. Cloning and characterization of the gene for amylosucrase from Neisseria polysaccharea: production of a linear α-1,4-glucan. J. Bacteriol. 179:3324-3330.
    • (1997) J. Bacteriol. , vol.179 , pp. 3324-3330
    • Büttcher, V.1    Welsh, T.2    Willmitzer, L.3    Kossmann, J.4
  • 6
    • 0031454064 scopus 로고    scopus 로고
    • Knowledge-based model of a glucosyltransferase from the oral bacterial group of mutans streptococci
    • Devulapalle, K. S., S. D. Goodman, Q. Gao, A. Hemsley, and G. Mooser. 1997. Knowledge-based model of a glucosyltransferase from the oral bacterial group of mutans streptococci. Protein Sci. 6:2489-2493.
    • (1997) Protein Sci. , vol.6 , pp. 2489-2493
    • Devulapalle, K.S.1    Goodman, S.D.2    Gao, Q.3    Hemsley, A.4    Mooser, G.5
  • 7
    • 0042302049 scopus 로고
    • Synthesis of a polysaccharide of the starch-glycogen class from sucrose by a cell-free, bacterial enzyme system (amylosucrase)
    • Hehre, E. J., D. M. Hamilton, and A. S. Carlson. 1949. Synthesis of a polysaccharide of the starch-glycogen class from sucrose by a cell-free, bacterial enzyme system (amylosucrase). J. Biol. Chem. 177:267-279.
    • (1949) J. Biol. Chem. , vol.177 , pp. 267-279
    • Hehre, E.J.1    Hamilton, D.M.2    Carlson, A.S.3
  • 8
    • 0025239538 scopus 로고
    • Random mutagenesis used to probe the structure and function of Bacillus stearothermophilus alpha-amylase
    • Holm, L., A. K. Koivula, P. M. Lehtovaara, A. Hemminki, and J. K. C. Knowles. 1990. Random mutagenesis used to probe the structure and function of Bacillus stearothermophilus alpha-amylase. Protein Eng. 3:181-191.
    • (1990) Protein Eng. , vol.3 , pp. 181-191
    • Holm, L.1    Koivula, A.K.2    Lehtovaara, P.M.3    Hemminki, A.4    Knowles, J.K.C.5
  • 9
    • 0026589137 scopus 로고
    • Multi-functional roles of a histidine residue in human pancreatic α-amylase
    • Ishikawa, K., I. Matsui, K. Honda, and H. Nakatani. 1992. Multi-functional roles of a histidine residue in human pancreatic α-amylase. Biochem. Biophys. Res. Commun. 183:286-291.
    • (1992) Biochem. Biophys. Res. Commun. , vol.183 , pp. 286-291
    • Ishikawa, K.1    Matsui, I.2    Honda, K.3    Nakatani, H.4
  • 10
    • 0028173219 scopus 로고
    • Parallel β/α-barrels of α-amylase, cyclodextrin glycosyl-transferase and oligo-1,6-glucosidase versus the barrel of β-amylase: Evolutionary distance is a reflection of unrelated sequences
    • Janecek, S. 1994. Parallel β/α-barrels of α-amylase, cyclodextrin glycosyl-transferase and oligo-1,6-glucosidase versus the barrel of β-amylase: evolutionary distance is a reflection of unrelated sequences. FEBS Lett. 353:119-123.
    • (1994) FEBS Lett. , vol.353 , pp. 119-123
    • Janecek, S.1
  • 11
    • 0030805437 scopus 로고    scopus 로고
    • Domain evolution in the α-amylase family
    • Janecek, S., B. Svensson, and B. Henrissat. 1997. Domain evolution in the α-amylase family. J. Mol. Evol. 45:322-331.
    • (1997) J. Mol. Evol. , vol.45 , pp. 322-331
    • Janecek, S.1    Svensson, B.2    Henrissat, B.3
  • 13
    • 0000539879 scopus 로고
    • Iodine-maltosaccharide complexes: Relation between chain-length and colour
    • John, M., J. Schmidt, and H. Kneifel. 1983. Iodine-maltosaccharide complexes: relation between chain-length and colour. Carbohydr. Res. 119:254-259.
    • (1983) Carbohydr. Res. , vol.119 , pp. 254-259
    • John, M.1    Schmidt, J.2    Kneifel, H.3
  • 14
    • 0027102598 scopus 로고
    • Molecular genetic analysis of the catalytic site of Streptococcus mutans glucosyltransferases
    • Kato, C., Y. Nakano, M. Lis, and H. K. Kuramitsu. 1992. Molecular genetic analysis of the catalytic site of Streptococcus mutans glucosyltransferases. Biochem. Biophys. Res. Commun. 189:1184-1188.
    • (1992) Biochem. Biophys. Res. Commun. , vol.189 , pp. 1184-1188
    • Kato, C.1    Nakano, Y.2    Lis, M.3    Kuramitsu, H.K.4
  • 15
    • 0026744021 scopus 로고
    • Catalytic center of cyclodextrin glycosyltransferase derived from X-ray structure analysis combined with site-directed mutagenesis
    • Klein, C., J. Hollender, H. Bender, and G. E. Schulz. 1992. Catalytic center of cyclodextrin glycosyltransferase derived from X-ray structure analysis combined with site-directed mutagenesis. Biochemistry 31:8740-8746.
    • (1992) Biochemistry , vol.31 , pp. 8740-8746
    • Klein, C.1    Hollender, J.2    Bender, H.3    Schulz, G.E.4
  • 16
    • 0344372474 scopus 로고    scopus 로고
    • Personal communication
    • Kossmann, J. 1998. Personal communication.
    • (1998)
    • Kossmann, J.1
  • 17
    • 0345235226 scopus 로고
    • Analysis of the active center of Bacillus stearothermophilus neopullulanase
    • Kuriki, T., H. Takata, S. Okada, and T. Imanaka. 1991. Analysis of the active center of Bacillus stearothermophilus neopullulanase. J. Bacteriol. 135:1521-1528.
    • (1991) J. Bacteriol. , vol.135 , pp. 1521-1528
    • Kuriki, T.1    Takata, H.2    Okada, S.3    Imanaka, T.4
  • 18
    • 0028359337 scopus 로고
    • Refined molecular structure of pig pancreatic α-amylase at 2.1 Å resolution
    • Larson, S. B., A. Greenwood, D. Cascio, J. Day, and A. McPherson. 1994. Refined molecular structure of pig pancreatic α-amylase at 2.1 Å resolution. J. Mol. Biol. 235:1560-1584.
    • (1994) J. Mol. Biol. , vol.235 , pp. 1560-1584
    • Larson, S.B.1    Greenwood, A.2    Cascio, D.3    Day, J.4    McPherson, A.5
  • 19
    • 0029671161 scopus 로고    scopus 로고
    • A circular permuted α-amylase-type α/β-barrel structure in glucan-synthesizing glucosyltransferases
    • MacGregor, E. A., H. M. Jespersen, and B. Svensson. 1996. A circular permuted α-amylase-type α/β-barrel structure in glucan-synthesizing glucosyltransferases. FEBS Lett. 378:263-266.
    • (1996) FEBS Lett. , vol.378 , pp. 263-266
    • MacGregor, E.A.1    Jespersen, H.M.2    Svensson, B.3
  • 20
    • 0017759947 scopus 로고
    • Glycogen synthesis by amylosucrase from Neisseria perflava
    • MacKenzie, C. R., K. G. Johnson, and I. J. McDonald. 1977. Glycogen synthesis by amylosucrase from Neisseria perflava. Can. J. Microbiol. 23: 1303-1307.
    • (1977) Can. J. Microbiol. , vol.23 , pp. 1303-1307
    • MacKenzie, C.R.1    Johnson, K.G.2    McDonald, I.J.3
  • 21
    • 0017840322 scopus 로고
    • Glycogen metabolism in the genus Neisseria: Synthesis from sucrose by amylosucrase
    • MacKenzie, C. R., I. J. McDonald, and K. G. Johnson. 1978. Glycogen metabolism in the genus Neisseria: synthesis from sucrose by amylosucrase. Can. J. Microbiol. 24:357-362.
    • (1978) Can. J. Microbiol. , vol.24 , pp. 357-362
    • MacKenzie, C.R.1    McDonald, I.J.2    Johnson, K.G.3
  • 23
    • 0021395910 scopus 로고
    • Structure and possible catalytic residues of Taka-amylase A
    • Matsuura, Y., M. Kusunoki, W. Harada, and M. Kakudo. 1984. Structure and possible catalytic residues of Taka-amylase A. J. Biochem. 95:697-702.
    • (1984) J. Biochem. , vol.95 , pp. 697-702
    • Matsuura, Y.1    Kusunoki, M.2    Harada, W.3    Kakudo, M.4
  • 24
    • 0030666665 scopus 로고    scopus 로고
    • Characterization of Leuconostoc mesenteroides NRRI. B-512F dextransucrase (DSRS) and identification of amino-acid residues playing a key role in enzyme activity
    • Monchois, V., M. Remaud-Simeon, R. R. B. Russel, P. Monsan, and R. M. Willemot. 1997. Characterization of Leuconostoc mesenteroides NRRI. B-512F dextransucrase (DSRS) and identification of amino-acid residues playing a key role in enzyme activity. Appl. Microbiol. Biotechnol. 48:465-472.
    • (1997) Appl. Microbiol. Biotechnol. , vol.48 , pp. 465-472
    • Monchois, V.1    Remaud-Simeon, M.2    Russel, R.R.B.3    Monsan, P.4    Willemot, R.M.5
  • 26
    • 0026567912 scopus 로고
    • Functional relationships between cyclodextrin glucanotransferases from an alkalophilic Bacillus and α-amylases
    • Nakamura, A., K. Haga, S. Ogawa, K. Kuwano, K. Kimura, and K. Yamane. 1992. Functional relationships between cyclodextrin glucanotransferases from an alkalophilic Bacillus and α-amylases. FEBS Lett. 296:37-40.
    • (1992) FEBS Lett. , vol.296 , pp. 37-40
    • Nakamura, A.1    Haga, K.2    Ogawa, S.3    Kuwano, K.4    Kimura, K.5    Yamane, K.6
  • 27
    • 0027303381 scopus 로고
    • Three histidine residues in the active center of cyclodextrin glucanotransferase from alkalophilic Bacillus sp. 1011: Effects of the replacement on pH dependence and transition-state stabilization
    • Nakamura, A., K. Haga, and K. Yamane. 1993. Three histidine residues in the active center of cyclodextrin glucanotransferase from alkalophilic Bacillus sp. 1011: effects of the replacement on pH dependence and transition-state stabilization. Biochemistry 32:6624-6631.
    • (1993) Biochemistry , vol.32 , pp. 6624-6631
    • Nakamura, A.1    Haga, K.2    Yamane, K.3
  • 28
    • 0000674033 scopus 로고
    • A photometric adaptation of the Somogyi method for the determination of glucose
    • Nelson, H. 1944. A photometric adaptation of the Somogyi method for the determination of glucose. J. Biol. Chem. 153:375-380.
    • (1944) J. Biol. Chem. , vol.153 , pp. 375-380
    • Nelson, H.1
  • 29
    • 0015536967 scopus 로고
    • De novo synthesis of glycosidic linkages hy glycosylases: Utilization of α-D-glucopyranosyl fluoride by amylosucrase
    • Okada, G., and E. J. Hehre. 1973. De novo synthesis of glycosidic linkages hy glycosylases: utilization of α-D-glucopyranosyl fluoride by amylosucrase. Carbohydr. Res. 26:240-243.
    • (1973) Carbohydr. Res. , vol.26 , pp. 240-243
    • Okada, G.1    Hehre, E.J.2
  • 30
    • 0015984405 scopus 로고
    • New studies on amylosucrase, a bacterial α-D-glucosylase that directly converts sucrose to a glycogen-like α-glucan
    • Okada, G., and E. J. Hehre. 1974. New studies on amylosucrase, a bacterial α-D-glucosylase that directly converts sucrose to a glycogen-like α-glucan. J. Biol. Chem. 249:126-135.
    • (1974) J. Biol. Chem. , vol.249 , pp. 126-135
    • Okada, G.1    Hehre, E.J.2
  • 31
    • 0002422156 scopus 로고
    • Further studies by light scattering of amylose aggregates. Particle weight under various conditions
    • Pashall, E. F., and J. F. Foster. 1952. Further studies by light scattering of amylose aggregates. Particle weight under various conditions. J. Polym. Sci. 9:85-52.
    • (1952) J. Polym. Sci. , vol.9 , pp. 85-152
    • Pashall, E.F.1    Foster, J.F.2
  • 33
    • 0015705433 scopus 로고
    • ADPG synthetase and ADPG-α-glucan-4-glucosyltransferase: Enzymes involved in bacterial glycogen and plant starch biosynthesis
    • Preiss, J., J. L. Ozbun, J. S. Hawker, E. Greenberg, and C. Lammel. 1973. ADPG synthetase and ADPG-α-glucan-4-glucosyltransferase: enzymes involved in bacterial glycogen and plant starch biosynthesis. Ann. N. Y. Acad. Sci. 210:265-277.
    • (1973) Ann. N. Y. Acad. Sci. , vol.210 , pp. 265-277
    • Preiss, J.1    Ozbun, J.L.2    Hawker, J.S.3    Greenberg, E.4    Lammel, C.5
  • 34
    • 77957076580 scopus 로고
    • Studies on a recombinant amylosucrase
    • S. B. Petersen, B. Svensson, and S. Pedersen (ed.). Elsevier Science B.V., Amsterdam, The Netherlands
    • Remaud-Simeon, M., F. Albaret, B. Canard, I. Varlet, P. Colonna, R. M. Willemot, and P. Monsan. 1995. Studies on a recombinant amylosucrase, p. 313-320. In S. B. Petersen, B. Svensson, and S. Pedersen (ed.), Carbohydrate bioengineering. Elsevier Science B.V., Amsterdam, The Netherlands.
    • (1995) Carbohydrate Bioengineering , pp. 313-320
    • Remaud-Simeon, M.1    Albaret, F.2    Canard, B.3    Varlet, I.4    Colonna, P.5    Willemot, R.M.6    Monsan, P.7
  • 37
    • 0029931417 scopus 로고    scopus 로고
    • Molecular weight distribution of amylose fractions obtained by aqueous leaching of maize starch
    • Roger, P., and P. Colonna. 1996. Molecular weight distribution of amylose fractions obtained by aqueous leaching of maize starch. Int. J. Biol. Macromol. 19:51-61.
    • (1996) Int. J. Biol. Macromol. , vol.19 , pp. 51-61
    • Roger, P.1    Colonna, P.2
  • 40
    • 0002890621 scopus 로고
    • A method for determination of invertase activity
    • Sumner, J. B., and S. F. Howell. 1935. A method for determination of invertase activity. J. Biol. Chem. 108:51-54.
    • (1935) J. Biol. Chem. , vol.108 , pp. 51-54
    • Sumner, J.B.1    Howell, S.F.2
  • 41
    • 0028429952 scopus 로고
    • Protein engineering in the α-amylase family: Catalytic mechanism, substrate specificity, and stability
    • Svensson, B. 1994. Protein engineering in the α-amylase family: catalytic mechanism, substrate specificity, and stability. Plant Mol. Biol. 25:141-157.
    • (1994) Plant Mol. Biol. , vol.25 , pp. 141-157
    • Svensson, B.1
  • 42
    • 77957048535 scopus 로고
    • Mutational analysis of catalytic mechanism and specificity in amylolytic enzymes
    • S. B. Petersen, B. Svensson, and S. Pedersen (ed.). Elsevier Science B.V., Amsterdam. The Netherlands
    • Svensson, B., T. P. Frandsen, J. Matsui, N. Juge, H. P. Fierobe, B. Stoffer, and K. W. Rodenburg. 1995. Mutational analysis of catalytic mechanism and specificity in amylolytic enzymes, p. 125-145. In S. B. Petersen, B. Svensson, and S. Pedersen (ed.), Carbohydrate bioengineering. Elsevier Science B.V., Amsterdam. The Netherlands.
    • (1995) Carbohydrate Bioengineering , pp. 125-145
    • Svensson, B.1    Frandsen, T.P.2    Matsui, J.3    Juge, N.4    Fierobe, H.P.5    Stoffer, B.6    Rodenburg, K.W.7
  • 43
    • 0024097706 scopus 로고
    • Neisseria amylosucrase: Characterization of its product polysaccharide and a study of its inhibition by sucrose derivatives
    • Tao, B. Y., P. J. Reilly, and J. F. Robyt. 1988. Neisseria amylosucrase: characterization of its product polysaccharide and a study of its inhibition by sucrose derivatives. Carbohydr. Res. 181:163-173.
    • (1988) Carbohydr. Res. , vol.181 , pp. 163-173
    • Tao, B.Y.1    Reilly, P.J.2    Robyt, J.F.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.