메뉴 건너뛰기




Volumn 180, Issue 20, 1998, Pages 5313-5318

Conserved structural regions involved in the catalytic mechanism of Escherichia coli K-12 WaaO (RfaI)

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL ENZYME; ESCHERICHIA COLI LIPOPOLYSACCHARIDE; GLYCOSYLTRANSFERASE;

EID: 0031680539     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/jb.180.20.5313-5318.1998     Document Type: Article
Times cited : (32)

References (31)
  • 1
    • 0029858149 scopus 로고    scopus 로고
    • Genetic and chemical characterization of a mutant that disrupts synthesis of the lipopolysaccharide core tetrasaccharide in Rhizobium leguminosarum
    • Allaway, D., B. Jeyaretnam, R. W. Carlson, and P. S. Poole. 1996. Genetic and chemical characterization of a mutant that disrupts synthesis of the lipopolysaccharide core tetrasaccharide in Rhizobium leguminosarum. J. Bacteriol. 178:6403-6406.
    • (1996) J. Bacteriol. , vol.178 , pp. 6403-6406
    • Allaway, D.1    Jeyaretnam, B.2    Carlson, R.W.3    Poole, P.S.4
  • 2
  • 3
    • 0030843984 scopus 로고    scopus 로고
    • A classification of nucleotide-diphospho-sugar glycosyltransferases based on amino acid sequence similarities
    • Campbell, J. A., G. J. Davies, V. Bulone, and B. Henrissat. 1997. A classification of nucleotide-diphospho-sugar glycosyltransferases based on amino acid sequence similarities. Biochem. J. 326:929-942.
    • (1997) Biochem. J. , vol.326 , pp. 929-942
    • Campbell, J.A.1    Davies, G.J.2    Bulone, V.3    Henrissat, B.4
  • 4
    • 0028302561 scopus 로고
    • Localization of an alpha 1,2 galactosyltransferase activity to the Golgi apparatus of Schizosaccharomyces pombe
    • Chappell, T. G., M. A. Hajibagheri, K. Ayscough, M. Pierce, and G. Warren. 1994. Localization of an alpha 1,2 galactosyltransferase activity to the Golgi apparatus of Schizosaccharomyces pombe. Mol. Biol. Cell 5:519-528.
    • (1994) Mol. Biol. Cell , vol.5 , pp. 519-528
    • Chappell, T.G.1    Hajibagheri, M.A.2    Ayscough, K.3    Pierce, M.4    Warren, G.5
  • 6
    • 0023657949 scopus 로고
    • Hydrophobic cluster analysis: An efficient new way to compare and analyze amino acid sequences
    • Gaboriaud, C., V. Bissery, T. Benchetrit, and J. P. Mornon. 1987. Hydrophobic cluster analysis: an efficient new way to compare and analyze amino acid sequences. FEBS Lett. 224:149-155.
    • (1987) FEBS Lett. , vol.224 , pp. 149-155
    • Gaboriaud, C.1    Bissery, V.2    Benchetrit, T.3    Mornon, J.P.4
  • 8
    • 0028148991 scopus 로고
    • Genetic locus for the biosynthesis of the variable portion of Neisseria gonorrhoeae lipooligosaccharide
    • Gotschlich, E. C. 1994. Genetic locus for the biosynthesis of the variable portion of Neisseria gonorrhoeae lipooligosaccharide. J. Exp. Med. 180:2181-2190.
    • (1994) J. Exp. Med. , vol.180 , pp. 2181-2190
    • Gotschlich, E.C.1
  • 9
    • 0032502771 scopus 로고    scopus 로고
    • The assembly system for the lipopolysaccharide R2 core-type of Escherichia coli is a hybrid of those found in Escherichia coli K-12 and Salmonella enterica
    • Heinrichs, D. E., M. A. Monterio, M. B. Perry, and C. Whitfield. 1998. The assembly system for the lipopolysaccharide R2 core-type of Escherichia coli is a hybrid of those found in Escherichia coli K-12 and Salmonella enterica. J. Biol. Chem. 273:8849-8859.
    • (1998) J. Biol. Chem. , vol.273 , pp. 8849-8859
    • Heinrichs, D.E.1    Monterio, M.A.2    Perry, M.B.3    Whitfield, C.4
  • 10
    • 0025654530 scopus 로고
    • Weak sequence homologies among chitinases detected by clustering analysis. Protein Seq
    • Henrissat, B. 1990. Weak sequence homologies among chitinases detected by clustering analysis. Protein Seq. Data Anal. 3:523-526.
    • (1990) Data Anal. , vol.3 , pp. 523-526
    • Henrissat, B.1
  • 11
    • 0024419181 scopus 로고
    • Cellulase families revealed by hydrophobic cluster analysis
    • Henrissat, B., M. Claeyssens, P. Tomme, L. Lemesle, and J. P. Mornon. 1989. Cellulase families revealed by hydrophobic cluster analysis. Gene 81: 83-95.
    • (1989) Gene , vol.81 , pp. 83-95
    • Henrissat, B.1    Claeyssens, M.2    Tomme, P.3    Lemesle, L.4    Mornon, J.P.5
  • 12
    • 0020536197 scopus 로고
    • Morphological heterogeneity among Salmonella lipopolysaccharide chemotypes in silver-stained polyacrylamide gels
    • Hitchcock, P. J., and T. M. Brown. 1983. Morphological heterogeneity among Salmonella lipopolysaccharide chemotypes in silver-stained polyacrylamide gels. J. Bacteriol. 154:269-277.
    • (1983) J. Bacteriol. , vol.154 , pp. 269-277
    • Hitchcock, P.J.1    Brown, T.M.2
  • 13
    • 0026204944 scopus 로고
    • Structural analysis of the heptose/hexose region of the lipopolysaccharide from Escherichia coli K-12 strain W3100
    • Holst, O., U. Zahringer, H. Brade, and A. Zamojski. 1991. Structural analysis of the heptose/hexose region of the lipopolysaccharide from Escherichia coli K-12 strain W3100. Carbohydr. Res. 215:323-335.
    • (1991) Carbohydr. Res. , vol.215 , pp. 323-335
    • Holst, O.1    Zahringer, U.2    Brade, H.3    Zamojski, A.4
  • 14
    • 0019793345 scopus 로고
    • Rapid, automated analysis of monosaccharides by high-performance anion-exchange chromatography of borate complexes with fluorimetric detection using 2-cyanoacetamide
    • Honda, S., M. Takahashi, K. Kakehi, and S. Ganno. 1981. Rapid, automated analysis of monosaccharides by high-performance anion-exchange chromatography of borate complexes with fluorimetric detection using 2-cyanoacetamide. Anal. Biochem. 113:130-138.
    • (1981) Anal. Biochem. , vol.113 , pp. 130-138
    • Honda, S.1    Takahashi, M.2    Kakehi, K.3    Ganno, S.4
  • 15
    • 0019882080 scopus 로고
    • Sensitive ultraviolet monitoring of aldoses in automated borate complex anion-exchange chromatography with 2-cyanoacetamide
    • Honda, S., M. Takahashi, Y. Nishimura, K. Kakehi, and S. Ganno. 1981. Sensitive ultraviolet monitoring of aldoses in automated borate complex anion-exchange chromatography with 2-cyanoacetamide. Anal. Biochem. 118:162-167.
    • (1981) Anal. Biochem. , vol.118 , pp. 162-167
    • Honda, S.1    Takahashi, M.2    Nishimura, Y.3    Kakehi, K.4    Ganno, S.5
  • 16
    • 0019430334 scopus 로고
    • Structural studies on the hexose region of the core in lipopolysaccharides from Enterobacteriaceae
    • Jansson, P. E., A. A. Lindberg, B. Lindberg, and R. Wollin. 1981. Structural studies on the hexose region of the core in lipopolysaccharides from Enterobacteriaceae. Eur. J. Biochem. 115:571-577.
    • (1981) Eur. J. Biochem. , vol.115 , pp. 571-577
    • Jansson, P.E.1    Lindberg, A.A.2    Lindberg, B.3    Wollin, R.4
  • 17
    • 0021906528 scopus 로고
    • Cloning of rfaG, B, I, and J genes for glycosyltransferase enzymes for synthesis of the lipopolysaccharide core of Salmonella typhimurium
    • Kadam, S. K., A. Rehemtulla, and K. E. Sanderson. 1985. Cloning of rfaG, B, I, and J genes for glycosyltransferase enzymes for synthesis of the lipopolysaccharide core of Salmonella typhimurium. J. Bacteriol. 161:277-284.
    • (1985) J. Bacteriol. , vol.161 , pp. 277-284
    • Kadam, S.K.1    Rehemtulla, A.2    Sanderson, K.E.3
  • 18
    • 0029855772 scopus 로고    scopus 로고
    • A novel pathway for O-polysaccharide biosynthesis in Salmonella enterica serovar Borreze
    • Keenleyside, W. J., and C. Whitfield. 1996. A novel pathway for O-polysaccharide biosynthesis in Salmonella enterica serovar Borreze. J. Biol. Chem. 271:28581-28592.
    • (1996) J. Biol. Chem. , vol.271 , pp. 28581-28592
    • Keenleyside, W.J.1    Whitfield, C.2
  • 19
    • 0025771472 scopus 로고
    • Cloning and expression of the rfe-rff gene cluster of Escherichia coli
    • Ohta, M., K. Ina, K. Kusuzaki, N. Kido, Y. Arakawa, and N. Kato. 1991. Cloning and expression of the rfe-rff gene cluster of Escherichia coli. Mol. Microbiol. 5:1853-1862.
    • (1991) Mol. Microbiol. , vol.5 , pp. 1853-1862
    • Ohta, M.1    Ina, K.2    Kusuzaki, K.3    Kido, N.4    Arakawa, Y.5    Kato, N.6
  • 20
    • 0028987945 scopus 로고
    • Drosophila UDP-glucose:glycoprotein glucosyltransferase: Sequence and characterization of an enzyme that distinguishes between denatured and native proteins
    • Parker, C. G., L. I. Fessler, R. E. Nelson, and J. H. Fessler. 1995. Drosophila UDP-glucose:glycoprotein glucosyltransferase: sequence and characterization of an enzyme that distinguishes between denatured and native proteins. EMBO J. 14:1294-1303.
    • (1995) EMBO J. , vol.14 , pp. 1294-1303
    • Parker, C.G.1    Fessler, L.I.2    Nelson, R.E.3    Fessler, J.H.4
  • 21
    • 0026741550 scopus 로고
    • Structures of the rfaB, rfaI, rfaJ, and rfaS genes of Escherichia coli K-12 and their roles in assembly of the lipopolysaccharide core
    • Pradel, E., C. T. Parker, and C. A. Schnaitman. 1992. Structures of the rfaB, rfaI, rfaJ, and rfaS genes of Escherichia coli K-12 and their roles in assembly of the lipopolysaccharide core. J. Bacteriol. 174:4736-4745.
    • (1992) J. Bacteriol. , vol.174 , pp. 4736-4745
    • Pradel, E.1    Parker, C.T.2    Schnaitman, C.A.3
  • 23
    • 0026682461 scopus 로고
    • Genetic analysis of the genes involved in synthesis of the lipopolysaccharide core in Escherichia coli K-12: Three operons in the rfa locus
    • Roncero, C., and M. J. Casadaban. 1992. Genetic analysis of the genes involved in synthesis of the lipopolysaccharide core in Escherichia coli K-12: three operons in the rfa locus. J. Bacteriol. 174:3250-3260.
    • (1992) J. Bacteriol. , vol.174 , pp. 3250-3260
    • Roncero, C.1    Casadaban, M.J.2
  • 24
    • 0015027195 scopus 로고
    • Role of lipids in the biosynthesis of the bacterial cell envelope
    • Rothfield, L., and D. Romeo. 1971. Role of lipids in the biosynthesis of the bacterial cell envelope. Bacteriol. Rev. 35:14-38.
    • (1971) Bacteriol. Rev. , vol.35 , pp. 14-38
    • Rothfield, L.1    Romeo, D.2
  • 26
    • 0028986927 scopus 로고
    • Multidomain architecture of β-glycosyl transferases: Implications for mechanism of action
    • Saxena, I. M., R. M. Brown, Jr., M. Fevre, R. A. Geremia, and B. Henrissat. 1995. Multidomain architecture of β-glycosyl transferases: implications for mechanism of action. J. Bacteriol. 177:1419-1424.
    • (1995) J. Bacteriol. , vol.177 , pp. 1419-1424
    • Saxena, I.M.1    Brown Jr., R.M.2    Fevre, M.3    Geremia, R.A.4    Henrissat, B.5
  • 28
    • 11944256494 scopus 로고
    • Catalytic mechanisms of enzymic glycosyl transfer
    • Sinnott, M. L. 1990. Catalytic mechanisms of enzymic glycosyl transfer. Chem. Rev. 90:1171-1202.
    • (1990) Chem. Rev. , vol.90 , pp. 1171-1202
    • Sinnott, M.L.1
  • 30
    • 0020055346 scopus 로고
    • A sensitive silver stain for detecting lipopolysaccharides in polyacrylamide gels
    • Tsai, C. M., and C. E. Frasch. 1982. A sensitive silver stain for detecting lipopolysaccharides in polyacrylamide gels. Anal. Biochem. 119:115-119.
    • (1982) Anal. Biochem. , vol.119 , pp. 115-119
    • Tsai, C.M.1    Frasch, C.E.2
  • 31
    • 0024046461 scopus 로고
    • Analysis and prediction of the location of catalytic residues in enzymes
    • Zvelebil, M. J. J. M., and M. J. E. Sternberg. 1988. Analysis and prediction of the location of catalytic residues in enzymes. Protein Eng. 2:127-138.
    • (1988) Protein Eng. , vol.2 , pp. 127-138
    • Zvelebil, M.J.J.M.1    Sternberg, M.J.E.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.