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Volumn 188, Issue 2, 1997, Pages 221-228

Glycolytic enzyme operon of Borrelia burgdorferi: Characterization and evolutionary implications

Author keywords

Gene cluster; Glyceraldehyde 3 phosphate dehydrogenase; Phosphoglycerate kinase; Spirochetes; Triosephosphate isomerase

Indexed keywords

GLYCERALDEHYDE 3 PHOSPHATE DEHYDROGENASE; GLYCOLYTIC ENZYME; PHOSPHOGLYCERATE KINASE; TRIOSEPHOSPHATE ISOMERASE;

EID: 0030999103     PISSN: 03781119     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0378-1119(96)00811-6     Document Type: Article
Times cited : (21)

References (31)
  • 1
    • 0024324714 scopus 로고
    • Identification, molecular cloning and sequence analysis of a gene cluster encoding the class II fructose 1,6-bisphosphate aldolase, 3-phosphoglycerate kinase and a putative second glyceraldehyde-3-phosphate dehydrogenase of Escherichia coli
    • Alefounder, P.R. and Perham, R.N. (1989) Identification, molecular cloning and sequence analysis of a gene cluster encoding the class II fructose 1,6-bisphosphate aldolase, 3-phosphoglycerate kinase and a putative second glyceraldehyde-3-phosphate dehydrogenase of Escherichia coli. Mol. Microbiol. 3, 723-732.
    • (1989) Mol. Microbiol. , vol.3 , pp. 723-732
    • Alefounder, P.R.1    Perham, R.N.2
  • 2
    • 0027957775 scopus 로고
    • Epitopes shared by unrelated antigens of Borrelia burgdorferi
    • Anda, P., Backenson, P.B., Coleman, J.L. and Benach, J.L. (1994) Epitopes shared by unrelated antigens of Borrelia burgdorferi. Infect. Immun. 62, 1070-1078.
    • (1994) Infect. Immun. , vol.62 , pp. 1070-1078
    • Anda, P.1    Backenson, P.B.2    Coleman, J.L.3    Benach, J.L.4
  • 3
    • 0030050740 scopus 로고    scopus 로고
    • A glyceraldehyde-3-phosphate dehydrogenase homolog in Borrelia burgdorferi and Borrelia hermsii
    • Anda, P., Gebbia, J.A., Backenson, P.B., Coleman, J.L. and Benach, J.L. (1996) A glyceraldehyde-3-phosphate dehydrogenase homolog in Borrelia burgdorferi and Borrelia hermsii. Infect. Immun. 64, 262-268.
    • (1996) Infect. Immun. , vol.64 , pp. 262-268
    • Anda, P.1    Gebbia, J.A.2    Backenson, P.B.3    Coleman, J.L.4    Benach, J.L.5
  • 6
    • 0017576456 scopus 로고
    • Sequence and structure of D-glyceraldehyde-3-phosphate dehydrogenase from Bacillus stearothermophilus
    • Biesecker, G., Harris, J.I., Thierry, J.C., Walker J.E. and Wonacott, A.J. (1977) Sequence and structure of D-glyceraldehyde-3-phosphate dehydrogenase from Bacillus stearothermophilus. Nature 266, 328-333.
    • (1977) Nature , vol.266 , pp. 328-333
    • Biesecker, G.1    Harris, J.I.2    Thierry, J.C.3    Walker, J.E.4    Wonacott, A.J.5
  • 7
    • 0021873417 scopus 로고
    • Nt sequence of the Escherichia coli gap gene
    • Branlant, G. and Branlant, C. (1985) Nt sequence of the Escherichia coli gap gene. Eur. J. Biochem. 150, 61-66.
    • (1985) Eur. J. Biochem. , vol.150 , pp. 61-66
    • Branlant, G.1    Branlant, C.2
  • 8
    • 0024592664 scopus 로고
    • Nt sequence determination of the DNA region coding for Bacillus stearothermophilus glyceraldehyde-3-phosphate dehydrogenase and the flanking DNA regions required for its expression in Escherichia coli
    • Branlant, C., Oster, T. and Branlant, G. (1989) Nt sequence determination of the DNA region coding for Bacillus stearothermophilus glyceraldehyde-3-phosphate dehydrogenase and the flanking DNA regions required for its expression in Escherichia coli. Gene 75, 145-155.
    • (1989) Gene , vol.75 , pp. 145-155
    • Branlant, C.1    Oster, T.2    Branlant, G.3
  • 9
    • 0029039462 scopus 로고
    • Borrelia burgdorferi binds plasminogen, resulting in enhanced penetration of endothelial monolayers
    • Coleman, J.L., Sellati, T.J., Testa, J.E., Kew, R.R., Furie, M.B. and Benach, J.L. (1995) Borrelia burgdorferi binds plasminogen, resulting in enhanced penetration of endothelial monolayers. Infect. Immun. 63, 2478-2484.
    • (1995) Infect. Immun. , vol.63 , pp. 2478-2484
    • Coleman, J.L.1    Sellati, T.J.2    Testa, J.E.3    Kew, R.R.4    Furie, M.B.5    Benach, J.L.6
  • 10
    • 0023989688 scopus 로고
    • Phosphoglycerate kinase gene from Zymomonas mobilis: Cloning, sequencing and localization within the gap operon
    • Conway, T. and Ingraham, L.O. (1988) Phosphoglycerate kinase gene from Zymomonas mobilis: cloning, sequencing and localization within the gap operon, J. Bacteriol. 170, 1926-1933.
    • (1988) J. Bacteriol. , vol.170 , pp. 1926-1933
    • Conway, T.1    Ingraham, L.O.2
  • 11
    • 0023465112 scopus 로고
    • Glyceraldehyde-3-phoshate dehydrogenase gene from Zymomonas mobilis: Cloning, sequencing and identification of promoter region
    • Conway, T., Sewell G.W. and Ingraham, L.O. (1987) Glyceraldehyde-3-phoshate dehydrogenase gene from Zymomonas mobilis: cloning, sequencing and identification of promoter region, J. Bacteriol. 169, 5653-5662.
    • (1987) J. Bacteriol. , vol.169 , pp. 5653-5662
    • Conway, T.1    Sewell, G.W.2    Ingraham, L.O.3
  • 12
    • 0025720556 scopus 로고
    • Sequence and expression of the gene encoding 3-phosphoglycerate kinase from Bacillus stearothermophilus
    • Davies, G.J., Littlechild, J.A., Watson, H.C. and Hall, L. (1991) Sequence and expression of the gene encoding 3-phosphoglycerate kinase from Bacillus stearothermophilus. Gene 109, 39-45.
    • (1991) Gene , vol.109 , pp. 39-45
    • Davies, G.J.1    Littlechild, J.A.2    Watson, H.C.3    Hall, L.4
  • 13
    • 0026706449 scopus 로고
    • Identification, sequence analysis and expression of a Corynebacterium glutamicum gene cluster encoding the three glycolytic enzymes glyceraldehyde-3-phosphate, 3-phosphoglycerate kinase and triosephosphate isomerase
    • Eikmanns, B.J. (1992) Identification, sequence analysis and expression of a Corynebacterium glutamicum gene cluster encoding the three glycolytic enzymes glyceraldehyde-3-phosphate, 3-phosphoglycerate kinase and triosephosphate isomerase, J. Bacteriol. 174, 6076-6086.
    • (1992) J. Bacteriol. , vol.174 , pp. 6076-6086
    • Eikmanns, B.J.1
  • 15
  • 16
    • 0028593448 scopus 로고
    • The outer surface protein a of the spirochete Borrelia burgdorferi is a plasmin (ogen) receptor
    • Fuchs, H., Wallich, R., Simon, M.M. and Kramer, M.D. (1994) The outer surface protein A of the spirochete Borrelia burgdorferi is a plasmin (ogen) receptor. Proc. Natl. Acad. Sci. USA 91, 12594-12598.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 12594-12598
    • Fuchs, H.1    Wallich, R.2    Simon, M.M.3    Kramer, M.D.4
  • 17
    • 0342595861 scopus 로고
    • Clustal: A package for performing sequence alignments on a microcomputer
    • Higgins, D.G. and Sharp, P.M. (1988) Clustal: a package for performing sequence alignments on a microcomputer. Gene 146, 57-65.
    • (1988) Gene , vol.146 , pp. 57-65
    • Higgins, D.G.1    Sharp, P.M.2
  • 18
    • 84959806880 scopus 로고
    • Binding of human plasminogen and urokinase-type plasminogen activator to the Lyme disease spirochete, Borrelia burgdorferi
    • Klempner, M.S., Noring, R., Epstein, M.P., McCloud, B., Hu, R., Limentani, S.A. and Rogers, R.A. (1995) Binding of human plasminogen and urokinase-type plasminogen activator to the Lyme disease spirochete, Borrelia burgdorferi. J. Infect. Dis. 171, 1258-1265.
    • (1995) J. Infect. Dis. , vol.171 , pp. 1258-1265
    • Klempner, M.S.1    Noring, R.2    Epstein, M.P.3    McCloud, B.4    Hu, R.5    Limentani, S.A.6    Rogers, R.A.7
  • 19
    • 0028089206 scopus 로고
    • Capturing host plasmin (ogen): A common mechanism for invasive pathogens?
    • Lottenberg, R., Minning-Wenz, D. and Boyle, M.D.P. (1994) Capturing host plasmin (ogen): a common mechanism for invasive pathogens? Trends Microbiol. 2, 20-24.
    • (1994) Trends Microbiol. , vol.2 , pp. 20-24
    • Lottenberg, R.1    Minning-Wenz, D.2    Boyle, M.D.P.3
  • 20
    • 0027423316 scopus 로고
    • A glyceraldehyde-3-phosphate dehydrogenase with eubacterial features in the amitochondriate eukaryote, Trichomonas vaginalis
    • Markos, A., Miretsky, A. and Muller, M. (1993) A glyceraldehyde-3-phosphate dehydrogenase with eubacterial features in the amitochondriate eukaryote, Trichomonas vaginalis. J. Mol. Evol. 37, 631-643.
    • (1993) J. Mol. Evol. , vol.37 , pp. 631-643
    • Markos, A.1    Miretsky, A.2    Muller, M.3
  • 21
    • 0027970963 scopus 로고
    • Conservaton of gene arrangement and an unusual organization of rRNA genes in the linear chromosomes of the Lyme disease spirochaetes Borrelia burgdorferi, B. garinii and B. afzelli
    • Ojaimi, C., Davidson, B.E., Saint Girons, I. and Old, I.G. (1994) Conservaton of gene arrangement and an unusual organization of rRNA genes in the linear chromosomes of the Lyme disease spirochaetes Borrelia burgdorferi, B. garinii and B. afzelli. Microbiology 140, 2931-2940.
    • (1994) Microbiology , vol.140 , pp. 2931-2940
    • Ojaimi, C.1    Davidson, B.E.2    Saint Girons, I.3    Old, I.G.4
  • 22
    • 0026682564 scopus 로고
    • A major surface protein on group a streptococci is a glyceraldehyde-3-phosphate- Dehydrogenase with multiple binding activity
    • Pancholi, V. and Fischetti, V.A. (1992) A major surface protein on group A streptococci is a glyceraldehyde-3-phosphate- dehydrogenase with multiple binding activity, J. Exp. Med. 176, 415-426.
    • (1992) J. Exp. Med. , vol.176 , pp. 415-426
    • Pancholi, V.1    Fischetti, V.A.2
  • 25
    • 0021212892 scopus 로고
    • Nt sequence of the triose phosphate isomerase gene of Escherichia coli
    • Pichersky, E., Gottlieb, L.D. and Hess, J.F. (1984) Nt sequence of the triose phosphate isomerase gene of Escherichia coli. Mol. Gen. Genet. 195, 314-320.
    • (1984) Mol. Gen. Genet. , vol.195 , pp. 314-320
    • Pichersky, E.1    Gottlieb, L.D.2    Hess, J.F.3
  • 26
    • 0023644310 scopus 로고
    • Structure of the holo-glyceraldehyde-3-phosphate dehydrogenase from Bacillus stearothermophilus at 1.8 Å resolution
    • Skarzynski, T., Moody, P.C.E. and Wonacott, A.J. (1987) Structure of the holo-glyceraldehyde-3-phosphate dehydrogenase from Bacillus stearothermophilus at 1.8 Å resolution, J. Mol. Biol. 193, 171-187.
    • (1987) J. Mol. Biol. , vol.193 , pp. 171-187
    • Skarzynski, T.1    Moody, P.C.E.2    Wonacott, A.J.3
  • 27
    • 0024555940 scopus 로고
    • Role of the histidine 176 residue in glyceraldehyde-3-phosphate dehydrogenase as probed by site-directed mutagenesis
    • Soukri, A., Mougin, A., Corbier, C., Wonacott, A., Branlant, C. and Branlant, G. (1989) Role of the histidine 176 residue in glyceraldehyde-3-phosphate dehydrogenase as probed by site-directed mutagenesis. Biochemistry 28, 2586-2592.
    • (1989) Biochemistry , vol.28 , pp. 2586-2592
    • Soukri, A.1    Mougin, A.2    Corbier, C.3    Wonacott, A.4    Branlant, C.5    Branlant, G.6
  • 30
    • 0026519169 scopus 로고
    • Comparison of the refined crystal structures of liganded and unliganded chicken, yeast, and trypanosomal triosephosphate isomerase
    • Wierenga, R.K., Noble, M.E.M. and Davenport, R.C. (1992) Comparison of the refined crystal structures of liganded and unliganded chicken, yeast, and trypanosomal triosephosphate isomerase, J. Mol. Biol. 224, 1115-1126.
    • (1992) J. Mol. Biol. , vol.224 , pp. 1115-1126
    • Wierenga, R.K.1    Noble, M.E.M.2    Davenport, R.C.3
  • 31
    • 0023184331 scopus 로고
    • Bacterial evolution
    • Woese, C.R. (1987) Bacterial evolution. Microbiol. Rev. 51, 221-271.
    • (1987) Microbiol. Rev. , vol.51 , pp. 221-271
    • Woese, C.R.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.