메뉴 건너뛰기




Volumn 64, Issue 5, 1998, Pages 1644-1649

Effect of Leuconostoc mesenteroides NRRL B-512F dextransucrase carboxy- terminal deletions on dextran and oligosaccharide synthesis

Author keywords

[No Author keywords available]

Indexed keywords

DEXTRAN; OLIGOSACCHARIDE; SUCRASE;

EID: 0031832289     PISSN: 00992240     EISSN: None     Source Type: Journal    
DOI: 10.1128/aem.64.5.1644-1649.1998     Document Type: Article
Times cited : (54)

References (35)
  • 1
    • 0026024402 scopus 로고
    • Peptide sequences for sucrose splitting and glucan binding within Streptococcus sobrinus glucosyltransferase (water-insoluble glucan synthetase)
    • Abo, H., T. Matsumura, T. Kodama, H. Ohta, K. Fukui, K. Kato, and H. Kagawa. 1991. Peptide sequences for sucrose splitting and glucan binding within Streptococcus sobrinus glucosyltransferase (water-insoluble glucan synthetase). J. Bacteriol. 173:989-996.
    • (1991) J. Bacteriol. , vol.173 , pp. 989-996
    • Abo, H.1    Matsumura, T.2    Kodama, T.3    Ohta, H.4    Fukui, K.5    Kato, K.6    Kagawa, H.7
  • 2
    • 0023777735 scopus 로고
    • Tightly regulated tac promoter vectors useful for the expression of unfused and fused proteins in Escherichia coli
    • Amman, E., B. Ochs, and K. J. Abel. 1988. Tightly regulated tac promoter vectors useful for the expression of unfused and fused proteins in Escherichia coli. Gene 69:301-315.
    • (1988) Gene , vol.69 , pp. 301-315
    • Amman, E.1    Ochs, B.2    Abel, K.J.3
  • 3
    • 0025095420 scopus 로고
    • Sequence analysis of the gene for the glucan-binding protein of Streptococcus mutans Ingbritt
    • Banas, J. A., R. R. B. Russell, and J. J. Ferretti. 1990. Sequence analysis of the gene for the glucan-binding protein of Streptococcus mutans Ingbritt. Infect. Immun. 58:667-673.
    • (1990) Infect. Immun. , vol.58 , pp. 667-673
    • Banas, J.A.1    Russell, R.R.B.2    Ferretti, J.J.3
  • 5
    • 0028416802 scopus 로고
    • Kinetics of leucrose formation from sucrose by dextransucrase
    • Böker, M., H.-J. Jördening, and K. Buchholz. 1994. Kinetics of leucrose formation from sucrose by dextransucrase. Biotechnol. Bioeng. 43:856-864.
    • (1994) Biotechnol. Bioeng. , vol.43 , pp. 856-864
    • Böker, M.1    Jördening, H.-J.2    Buchholz, K.3
  • 6
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M. 1976. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72:248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 7
    • 0014239722 scopus 로고
    • Mechanism of biopolymer growth: The formation of dextran and levan
    • Ebert, K. H., and G. Schenk. 1968. Mechanism of biopolymer growth: the formation of dextran and levan. Adv. Enzymol. 30:179-221.
    • (1968) Adv. Enzymol. , vol.30 , pp. 179-221
    • Ebert, K.H.1    Schenk, G.2
  • 8
    • 0023203218 scopus 로고
    • Nucleotide sequence of a glucosyltransferase gene from Streptococcus sobrinus Mfe28
    • Ferretti, J. J., M. L. Gilpin, and R. R. B. Russell. 1987. Nucleotide sequence of a glucosyltransferase gene from Streptococcus sobrinus Mfe28. J. Bacteriol. 169:4271-4278.
    • (1987) J. Bacteriol. , vol.169 , pp. 4271-4278
    • Ferretti, J.J.1    Gilpin, M.L.2    Russell, R.R.B.3
  • 9
    • 0028453501 scopus 로고
    • Definition of a fundamental repeating unit in streptococcal glucosyltransferase glucan-binding regions and related sequences
    • Giffard, P. M., and N. A. Jacques. 1994. Definition of a fundamental repeating unit in streptococcal glucosyltransferase glucan-binding regions and related sequences. J. Dent. Res. 73:1133-1141.
    • (1994) J. Dent. Res. , vol.73 , pp. 1133-1141
    • Giffard, P.M.1    Jacques, N.A.2
  • 10
    • 0020959710 scopus 로고
    • Studies on transformation of Escherichia coli with plasmids
    • Hanahan, D. 1983. Studies on transformation of Escherichia coli with plasmids. J. Mol. Biol. 166:557-580.
    • (1983) J. Mol. Biol. , vol.166 , pp. 557-580
    • Hanahan, D.1
  • 11
    • 0025119148 scopus 로고
    • Carboxy-terminal deletion analysis of the Streptococcus mutans glucosyltransferase-I enzyme
    • Kato, C., and H. K. Kuramitsu. 1990. Carboxy-terminal deletion analysis of the Streptococcus mutans glucosyltransferase-I enzyme. FEMS Microbiol. Lett. 72:299-302.
    • (1990) FEMS Microbiol. Lett. , vol.72 , pp. 299-302
    • Kato, C.1    Kuramitsu, H.K.2
  • 12
    • 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
  • 13
    • 0344071376 scopus 로고
    • Activation of dextransucrase from Leuconostoc mesenteroides by the substrate, dextran
    • Kobayashi, M., I. Yokoyama, and K. Matsuda. 1984. Activation of dextransucrase from Leuconostoc mesenteroides by the substrate, dextran. Agric. Biol. Chem. 48:221-223.
    • (1984) Agric. Biol. Chem. , vol.48 , pp. 221-223
    • Kobayashi, M.1    Yokoyama, I.2    Matsuda, K.3
  • 14
    • 84954976278 scopus 로고
    • Effectors differently modulating the dextransucrase activity of Leuconostoc mesenteroides evaluated by inhibition kinetics
    • Kobayashi, M., I. Yokoyama, and K. Matsuda. 1985. Effectors differently modulating the dextransucrase activity of Leuconostoc mesenteroides evaluated by inhibition kinetics. Agric. Biol. Chem. 49:3189-3195.
    • (1985) Agric. Biol. Chem. , vol.49 , pp. 3189-3195
    • Kobayashi, M.1    Yokoyama, I.2    Matsuda, K.3
  • 15
    • 0001541275 scopus 로고
    • Substrate binding sites of Leuconostoc dextransucrase evaluated by inhibition kinetics
    • Kobayashi, M., I. Yokoyama, and K. Matsuda. 1986. Substrate binding sites of Leuconostoc dextransucrase evaluated by inhibition kinetics. Agric. Biol. Chem. 50:2585-2590.
    • (1986) Agric. Biol. Chem. , vol.50 , pp. 2585-2590
    • Kobayashi, M.1    Yokoyama, I.2    Matsuda, K.3
  • 17
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature (London) 227:680-685.
    • (1970) Nature (London) , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 18
    • 0028989758 scopus 로고
    • Role of the C-terminal direct repeating units of the Streptococcus mutans glucosyltransferase-S in glucan binding
    • Lis, M., T. Shiroza, and H. K. Kuramitsu. 1995. Role of the C-terminal direct repeating units of the Streptococcus mutans glucosyltransferase-S in glucan binding. Appl. Environ. Microbiol. 61:2040-2042.
    • (1995) Appl. Environ. Microbiol. , vol.61 , pp. 2040-2042
    • Lis, M.1    Shiroza, T.2    Kuramitsu, H.K.3
  • 19
    • 0029671161 scopus 로고    scopus 로고
    • A circularly permuted α-amylase type α/β barrel structure in glucan-synthesizing glucosyltransferases
    • MacGregor, A. E., H. M. Jespersen, and B. Svensson. 1996. A circularly 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, A.E.1    Jespersen, H.M.2    Svensson, B.3
  • 21
    • 0030666665 scopus 로고    scopus 로고
    • Characterization of Leuconostoc mesenteroides NRRL B-512F dextransucrase (DSR-S) and identification of amino-acid residues playing a key role in enzyme activity
    • Monchois, V., M. Remaud-Simeon, R. R. B. Russell, P. Monsan, and R. M. Willemot. 1997. Characterization of Leuconostoc mesenteroides NRRL B-512F dextransucrase (DSR-S) 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    Russell, R.R.B.3    Monsan, P.4    Willemot, R.M.5
  • 22
    • 0025827032 scopus 로고
    • Isolation and sequence of an active-site peptide containing a catalytic aspartic acid from two Streptococcus sobrinus glucosyltransferases
    • Mooser, G., S. A. Hefta, R. J. Paxton, J. E. Shively, and T. D. Lee. 1991. Isolation and sequence of an active-site peptide containing a catalytic aspartic acid from two Streptococcus sobrinus glucosyltransferases. J. Biol. Chem. 266:8916-8922.
    • (1991) J. Biol. Chem. , vol.266 , pp. 8916-8922
    • Mooser, G.1    Hefta, S.A.2    Paxton, R.J.3    Shively, J.E.4    Lee, T.D.5
  • 23
    • 0026787839 scopus 로고
    • Mechanism of Streptococcus mutans glucosyltransferases: Hybrid-enzyme analysis
    • Nakano, Y. J., and H. K. Kuramitsu. 1992. Mechanism of Streptococcus mutans glucosyltransferases: hybrid-enzyme analysis. J. Bacteriol. 174:5639-5646.
    • (1992) J. Bacteriol. , vol.174 , pp. 5639-5646
    • Nakano, Y.J.1    Kuramitsu, H.K.2
  • 24
    • 0003816265 scopus 로고
    • Acceptor reaction of a highly purified dextransucrase with maltose and oligosaccharides. Application to the synthesis of controlled-molecular-weight dextrans
    • Paul, F., E. Oriol, D. Auriol, and P. Monsan. 1986. Acceptor reaction of a highly purified dextransucrase with maltose and oligosaccharides. Application to the synthesis of controlled-molecular-weight dextrans. Carbohydr. Res. 149:433-441.
    • (1986) Carbohydr. Res. , vol.149 , pp. 433-441
    • Paul, F.1    Oriol, E.2    Auriol, D.3    Monsan, P.4
  • 25
    • 0028203770 scopus 로고
    • Cloning of the D-lactate deshydrogenase gene from Leuconostoc mesenteroides subsp. cremoris
    • Phalip, V., V. Dartois, P. Schmitt, and C. Divies. 1994. Cloning of the D-lactate deshydrogenase gene from Leuconostoc mesenteroides subsp. cremoris. Biotechnol. Lett. 16:221-226.
    • (1994) Biotechnol. Lett. , vol.16 , pp. 221-226
    • Phalip, V.1    Dartois, V.2    Schmitt, P.3    Divies, C.4
  • 26
    • 0025643586 scopus 로고
    • Kinetics of oligosaccharide synthesis by dextransucrase
    • Reh, K.-D., H. J. Jördening, and K. Buchholz. 1994. Kinetics of oligosaccharide synthesis by dextransucrase. Ann. N. Y. Acad. Sci. 613:723-729.
    • (1994) Ann. N. Y. Acad. Sci. , vol.613 , pp. 723-729
    • Reh, K.-D.1    Jördening, H.J.2    Buchholz, K.3
  • 27
    • 0016363519 scopus 로고
    • The mechanism of dextransucrase action. Direction of dextran biosynthesis
    • Robyt, J. F., B. K. Kimble, and T. F. Walseth. 1974. The mechanism of dextransucrase action. Direction of dextran biosynthesis. Arch. Biochem. Biophys. 165:634-640.
    • (1974) Arch. Biochem. Biophys. , vol.165 , pp. 634-640
    • Robyt, J.F.1    Kimble, B.K.2    Walseth, T.F.3
  • 28
    • 0017950850 scopus 로고
    • The mechanism of acceptor reaction of Leuconostoc mesenteroides NRRL B-512F dextransucrase
    • Robyt, J. F., and T. F. Walseth. 1978. The mechanism of acceptor reaction of Leuconostoc mesenteroides NRRL B-512F dextransucrase. Carbohydr. Res. 61:433-445.
    • (1978) Carbohydr. Res. , vol.61 , pp. 433-445
    • Robyt, J.F.1    Walseth, T.F.2
  • 29
    • 0021106318 scopus 로고
    • Relatives quantitative effects of acceptors in the reaction of Leuconostoc mesenteroides B 512-F dextransucrase action
    • Robyt, J. F., and S. H. Eklund. 1983. Relatives quantitative effects of acceptors in the reaction of Leuconostoc mesenteroides B 512-F dextransucrase action. Carbohydr. Res. 121:279-286.
    • (1983) Carbohydr. Res. , vol.121 , pp. 279-286
    • Robyt, J.F.1    Eklund, S.H.2
  • 30
    • 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
  • 31
    • 0027108518 scopus 로고
    • Inhibition of dextran synthesis by acceptor reactions of dextransucrase and the demonstration of a separate acceptor binding site
    • Tarivseven, A., and J. F. Robyt. 1992. Inhibition of dextran synthesis by acceptor reactions of dextransucrase and the demonstration of a separate acceptor binding site. Carbohydr. Res. 225:321-329.
    • (1992) Carbohydr. Res. , vol.225 , pp. 321-329
    • Tarivseven, A.1    Robyt, J.F.2
  • 32
    • 0029806935 scopus 로고    scopus 로고
    • Changes in the carboxy-terminal repeat region affect extracellular activity and glucan products of Streptococcus gordonii glucosyltransferase
    • Vickerman, M. M., M. C. Sulavik, P. E. Minick, and D. B. Clewell. 1996. Changes in the carboxy-terminal repeat region affect extracellular activity and glucan products of Streptococcus gordonii glucosyltransferase. Infect. Immun. 64:5117-5128.
    • (1996) Infect. Immun. , vol.64 , pp. 5117-5128
    • Vickerman, M.M.1    Sulavik, M.C.2    Minick, P.E.3    Clewell, D.B.4
  • 33
    • 0026702564 scopus 로고
    • Evidence for a modular structure of the homologous repetitive C-terminal carbohydrate-binding sites of Clostridium difficile toxins and Streptococcus mutans glucosyltransferases
    • Von Eichel-Streiber, C., M. Sauerborn, and H. K. Kuramitsu. 1992. Evidence for a modular structure of the homologous repetitive C-terminal carbohydrate-binding sites of Clostridium difficile toxins and Streptococcus mutans glucosyltransferases. J. Bacteriol. 174:6707-6710.
    • (1992) J. Bacteriol. , vol.174 , pp. 6707-6710
    • Von Eichel-Streiber, C.1    Sauerborn, M.2    Kuramitsu, H.K.3
  • 35
    • 0025365829 scopus 로고
    • Size and subdomain architecture of the glucan-binding domain of sucrose: 3-α-D-glucosyltransferase from Streptococcus sobrinus
    • Wong, C., A. H. Stanley, R. J. Paxton, J. E. Shively, and G. Mooser. 1990. Size and subdomain architecture of the glucan-binding domain of sucrose: 3-α-D-glucosyltransferase from Streptococcus sobrinus. Infect. Immun. 58: 2165-2170.
    • (1990) Infect. Immun. , vol.58 , pp. 2165-2170
    • Wong, C.1    Stanley, A.H.2    Paxton, R.J.3    Shively, J.E.4    Mooser, G.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.