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Volumn 132, Issue 4, 2002, Pages 565-572

Identification of functionally important amino acid residues in Zymomonas mobilis levansucrase

Author keywords

Catalytic mechanism; Fructosyltransferase; Glycosyltransferase; Levansucrase; Zymomonas mobilis

Indexed keywords

AMINO ACID; ASPARTIC ACID; BACTERIAL ENZYME; FRUCTOFURANOSIDASE; FRUCTOSYLTRANSFERASE; GLUTAMINE; HISTIDINE; LEVANSUCRASE; SUCROSE; UNCLASSIFIED DRUG; FRUCTOSE; GLYCOSYLTRANSFERASE; PRIMER DNA;

EID: 0036775911     PISSN: 0021924X     EISSN: None     Source Type: Journal    
DOI: 10.1093/oxfordjournals.jbchem.a003258     Document Type: Article
Times cited : (59)

References (21)
  • 1
    • 0017251470 scopus 로고
    • Levansucrase of Bacillus subtilis: Kinetic and thermodynamic aspects of transfructosylation processes
    • Chambert, R. and Gonzy-Treboul, G. (1976) Levansucrase of Bacillus subtilis: Kinetic and thermodynamic aspects of transfructosylation processes. Eur. J. Biochem. 62, 55-64
    • (1976) Eur. J. Biochem. , vol.62 , pp. 55-64
    • Chambert, R.1    Gonzy-Treboul, G.2
  • 2
    • 0018877572 scopus 로고
    • Levansucrase of Bacillus subtilis. Characterization of a form isolated from phenol-treated cells and activated by Triton X100
    • Petit-Glatron, M.F., Chambert, R., and Steinmetz, M. (1980) Levansucrase of Bacillus subtilis. Characterization of a form isolated from phenol-treated cells and activated by Triton X100. Eur. J. Biochem. 103, 189-195
    • (1980) Eur. J. Biochem. , vol.103 , pp. 189-195
    • Petit-Glatron, M.F.1    Chambert, R.2    Steinmetz, M.3
  • 3
    • 0019276376 scopus 로고
    • The structure of Bacillus subtilis levansucrase at 3.8 Å resolution
    • LeBrun, E. and Van Rapenbusch, R. (1980) The structure of Bacillus subtilis levansucrase at 3.8 Å resolution. J. Biol. Chem. 255, 12034-12036
    • (1980) J. Biol. Chem. , vol.255 , pp. 12034-12036
    • LeBrun, E.1    Van Rapenbusch, R.2
  • 4
    • 0021160222 scopus 로고
    • Formation of sorbitol by Zymomonas mobilis
    • Viikari, L. (1984) Formation of sorbitol by Zymomonas mobilis. Appl. Microbiol. Biotechnol. 20, 118-123
    • (1984) Appl. Microbiol. Biotechnol. , vol.20 , pp. 118-123
    • Viikari, L.1
  • 5
    • 0013888124 scopus 로고
    • Sucrose utilization by Zymomonas mobilis: Formation of a levan
    • Dawes, E.A., Ribbons, D.W., and Rees, D.A. (1966) Sucrose utilization by Zymomonas mobilis: formation of a levan. Biochem. J. 98, 804-812
    • (1966) Biochem. J. , vol.98 , pp. 804-812
    • Dawes, E.A.1    Ribbons, D.W.2    Rees, D.A.3
  • 6
    • 0020574539 scopus 로고
    • Levansucrase from Zymomonas mobilis
    • Lyness, E.W. and Doelle, H.W. (1983) Levansucrase from Zymomonas mobilis. Biotechnol. Lett. 5, 345-350
    • (1983) Biotechnol. Lett. , vol.5 , pp. 345-350
    • Lyness, E.W.1    Doelle, H.W.2
  • 7
    • 0026164177 scopus 로고
    • Cloning, sequencing, and characterization of the intracellular invertase gene from Zymomonas mobilis
    • Yanase, H., Fukushi, H., Ueda, N., Maeda, Y., Toyoda, A., and Tonomura, K. (1991) Cloning, sequencing, and characterization of the intracellular invertase gene from Zymomonas mobilis. Agric. Biol. Chem. 55, 1383-1390
    • (1991) Agric. Biol. Chem. , vol.55 , pp. 1383-1390
    • Yanase, H.1    Fukushi, H.2    Ueda, N.3    Maeda, Y.4    Toyoda, A.5    Tonomura, K.6
  • 8
    • 0000802609 scopus 로고
    • Purification, crystallization, and properties of the extracellular levansucrase from Zymomonas mobilis
    • Yanase, H., Iwata, M., Nakahigashi, R., Kita, K., and Tonomura, K. (1992) Purification, crystallization, and properties of the extracellular levansucrase from Zymomonas mobilis. Biosci. Biotechnol. Biochem. 56, 1335-1337
    • (1992) Biosci. Biotechnol. Biochem. , vol.56 , pp. 1335-1337
    • Yanase, H.1    Iwata, M.2    Nakahigashi, R.3    Kita, K.4    Tonomura, K.5
  • 9
    • 85007744299 scopus 로고
    • Cloning and characterization of Zymomonas mobilis genes encoding extracellular levansucrase and invertase
    • Kyono, K., Yanase, H., Tonomura, K., Kawasaki, H., and Sakai, T. (1995) Cloning and characterization of Zymomonas mobilis genes encoding extracellular levansucrase and invertase. Biosci. Biotechnol. Biochem. 59, 289-293
    • (1995) Biosci. Biotechnol. Biochem. , vol.59 , pp. 289-293
    • Kyono, K.1    Yanase, H.2    Tonomura, K.3    Kawasaki, H.4    Sakai, T.5
  • 10
    • 0029035733 scopus 로고
    • Purification, crystallization, and characterization of the extracellular invertase from Zymomonas mobilis
    • Yanase, H., Iwata, M., Kita, K., Kato, N., and Tonomura, K. (1995) Purification, crystallization, and characterization of the extracellular invertase from Zymomonas mobilis. J. Ferment. Bioeng. 79, 367-369
    • (1995) J. Ferment. Bioeng. , vol.79 , pp. 367-369
    • Yanase, H.1    Iwata, M.2    Kita, K.3    Kato, N.4    Tonomura, K.5
  • 11
    • 0025861055 scopus 로고
    • Polymerase and hydrolase activities of Bacillus subtilis levansucrase can be separately modulated by site-directed mutagenesis
    • Chambert, R. and Petit-Glatron, M.F. (1991) Polymerase and hydrolase activities of Bacillus subtilis levansucrase can be separately modulated by site-directed mutagenesis. Biochem. J. 279, 35-41
    • (1991) Biochem. J. , vol.279 , pp. 35-41
    • Chambert, R.1    Petit-Glatron, M.F.2
  • 12
    • 0039848317 scopus 로고    scopus 로고
    • Substitution of Asp-309 by Asn in the Arg-Asp-Pro (RDP) motif of Acetobacter diazotrophicus levansucrase affects sucrose hydrolysis, but not enzyme specificity
    • Batista, F.R., Hernandez, L., Fernandez, J.R., Arrieta, J., Menendez, C., Gomez, R., Tambara, Y., and Pons, T. (1999) Substitution of Asp-309 by Asn in the Arg-Asp-Pro (RDP) motif of Acetobacter diazotrophicus levansucrase affects sucrose hydrolysis, but not enzyme specificity. Biochem. J. 3, 503-506
    • (1999) Biochem. J. , vol.3 , pp. 503-506
    • Batista, F.R.1    Hernandez, L.2    Fernandez, J.R.3    Arrieta, J.4    Menendez, C.5    Gomez, R.6    Tambara, Y.7    Pons, T.8
  • 13
    • 0032151693 scopus 로고    scopus 로고
    • Expression of the extracellular levansucrase and invertase genes from Zymomonas mobilis in Escherichia coli cells
    • Yanase, H., Fujimoto, J., Maeda, M., Okamoto, K., Kita, K., and Tonomura, K. (1998) Expression of the extracellular levansucrase and invertase genes from Zymomonas mobilis in Escherichia coli cells. Biosci. Biotech. Biochem. 62, 1802-1805
    • (1998) Biosci. Biotech. Biochem. , vol.62 , pp. 1802-1805
    • Yanase, H.1    Fujimoto, J.2    Maeda, M.3    Okamoto, K.4    Kita, K.5    Tonomura, K.6
  • 14
    • 0027244755 scopus 로고
    • The cellbound fructosyltransferase of Streptococcus salivarius: The carboxyl terminus specifies attachment in a Streptococcus gordonii model system
    • Rathsam, C., Giffard, P.M., and Jacques, N.A. (1993) The cellbound fructosyltransferase of Streptococcus salivarius: The carboxyl terminus specifies attachment in a Streptococcus gordonii model system. J. Bacteriol. 175, 4520-4527
    • (1993) J. Bacteriol. , vol.175 , pp. 4520-4527
    • Rathsam, C.1    Giffard, P.M.2    Jacques, N.A.3
  • 15
    • 0033571281 scopus 로고    scopus 로고
    • Mutation of aspartic acid residues in the fructosyltransferase of Streptococcus salivarius ATCC 25975
    • Song, D.D. and Jacques, N.A. (1999) Mutation of aspartic acid residues in the fructosyltransferase of Streptococcus salivarius ATCC 25975. Biochem. J. 1, 259-264
    • (1999) Biochem. J. , vol.1 , pp. 259-264
    • Song, D.D.1    Jacques, N.A.2
  • 16
    • 0023661282 scopus 로고
    • Three dimensional structure of porcine pancreatic alpha-amylase at 2.9 Å resolution. Role of calcium in structure and activity
    • Buisson, G., Duee, E., Haser, R., and Payan, F. (1987) Three dimensional structure of porcine pancreatic alpha-amylase at 2.9 Å resolution. Role of calcium in structure and activity. EMBO J. 6, 3909-3916
    • (1987) EMBO J. , vol.6 , pp. 3909-3916
    • Buisson, G.1    Duee, E.2    Haser, R.3    Payan, F.4
  • 17
    • 0024307344 scopus 로고
    • Three-dimensional structure of cyclodextrin glycosyltransferase from Bacillus circulans at 3.4 Å resolution
    • Hofmann, B.E., Bender, H., and Schulz, G.E. (1989) Three-dimensional structure of cyclodextrin glycosyltransferase from Bacillus circulans at 3.4 Å resolution. J. Mol. Biol. 209, 793-800
    • (1989) J. Mol. Biol. , vol.209 , pp. 793-800
    • Hofmann, B.E.1    Bender, H.2    Schulz, G.E.3
  • 18
    • 0026726797 scopus 로고
    • Crystal structure of glucoamylase from Aspergillus awamori var. X100 to 2.2-Å resolution
    • Aleshin, A., Golubev, A., Firsov, L.M., and Honzatko, R.B. (1992) Crystal structure of glucoamylase from Aspergillus awamori var. X100 to 2.2-Å resolution. J. Biol. Chem. 267, 19291-19298
    • (1992) J. Biol. Chem. , vol.267 , pp. 19291-19298
    • Aleshin, A.1    Golubev, A.2    Firsov, L.M.3    Honzatko, R.B.4
  • 19
    • 0027176843 scopus 로고
    • Polypeptide folding of Bacillus cereus ATCC7064 oligo-1,6-glucosidase revealed by 3.0 Å resolution X-ray analysis
    • Kizaki, H., Hata, Y., Watanabe, K., Katsube, Y., and Suzuki, Y. (1993) Polypeptide folding of Bacillus cereus ATCC7064 oligo-1,6-glucosidase revealed by 3.0 Å resolution X-ray analysis. J. Biochem. 113, 646-649
    • (1993) J. Biochem. , vol.113 , pp. 646-649
    • Kizaki, H.1    Hata, Y.2    Watanabe, K.3    Katsube, Y.4    Suzuki, Y.5
  • 21
    • 0028229326 scopus 로고
    • Crystal and molecular structure of barley α-amylase
    • Kadziola, A., Abe, J., Svensson, B., and Haser, R. (1994) Crystal and molecular structure of barley α-amylase. J. Mol. Biol. 239, 104-121
    • (1994) J. Mol. Biol. , vol.239 , pp. 104-121
    • Kadziola, A.1    Abe, J.2    Svensson, B.3    Haser, R.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.