메뉴 건너뛰기




Volumn 109, Issue 1, 2000, Pages 25-36

Role of alcohol dehydrogenase E (ADHE) in the energy metabolism of Giardia lamblia

Author keywords

Antisense RNA; Gene expression; Giardiavirus; Hammerhead ribozyme; Transfection

Indexed keywords

ALCOHOL DEHYDROGENASE; COMPLEMENTARY RNA; ISOENZYME; MESSENGER RNA; RIBOZYME;

EID: 0033878311     PISSN: 01666851     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0166-6851(00)00233-4     Document Type: Article
Times cited : (31)

References (39)
  • 1
    • 0024151128 scopus 로고
    • Energy metabolism of protozoa without mitochondria
    • Müller M. Energy metabolism of protozoa without mitochondria. Annu. Rev. Microbiol. 42:1988;465-488.
    • (1988) Annu. Rev. Microbiol. , vol.42 , pp. 465-488
    • Müller, M.1
  • 2
    • 2642689666 scopus 로고    scopus 로고
    • The hydrogen hypothesis for the first eukaryote [see comments]
    • Martin W., Müller M. The hydrogen hypothesis for the first eukaryote [see comments]. Nature. 392:1998;37-41.
    • (1998) Nature , vol.392 , pp. 37-41
    • Martin, W.1    Müller, M.2
  • 3
    • 0031856603 scopus 로고    scopus 로고
    • Aldehyde dehydrogenase (CoA-acetylating) and the mechanism of ethanol formation in the amitochondriate protist, Giardia lamblia
    • Sánchez L.B. Aldehyde dehydrogenase (CoA-acetylating) and the mechanism of ethanol formation in the amitochondriate protist, Giardia lamblia. Arch. Biochem. Biophys. 354:1998;57-64.
    • (1998) Arch. Biochem. Biophys. , vol.354 , pp. 57-64
    • Sánchez, L.B.1
  • 4
    • 0024849185 scopus 로고
    • Cloning and sequence analysis of the fermentative alcohol-dehydrogenase-encoding gene of Escherichia coli
    • Goodlove P.E., Cunningham P.R., Parker J., Clark D.P. Cloning and sequence analysis of the fermentative alcohol-dehydrogenase-encoding gene of Escherichia coli. Gene. 85:1989;209-214.
    • (1989) Gene , vol.85 , pp. 209-214
    • Goodlove, P.E.1    Cunningham, P.R.2    Parker, J.3    Clark, D.P.4
  • 5
    • 0027383357 scopus 로고
    • Cloning, sequencing, and molecular analysis of the sol operon of Clostridium acetobutylicum, a chromosomal locus involved in solventogenesis
    • Fischer R.J., Helms J., Dürre P. Cloning, sequencing, and molecular analysis of the sol operon of Clostridium acetobutylicum, a chromosomal locus involved in solventogenesis. J. Bacteriol. 175:1993;6959-6969.
    • (1993) J. Bacteriol. , vol.175 , pp. 6959-6969
    • Fischer, R.J.1    Helms, J.2    Dürre, P.3
  • 6
    • 0027957210 scopus 로고
    • Molecular characterization of an aldehyde/alcohol dehydrogenase gene from Clostridium acetobutylicum ATCC 824
    • Nair R.V., Bennett G.N., Papoutsakis E.T. Molecular characterization of an aldehyde/alcohol dehydrogenase gene from Clostridium acetobutylicum ATCC 824. J. Bacteriol. 176:1994;871-885.
    • (1994) J. Bacteriol. , vol.176 , pp. 871-885
    • Nair, R.V.1    Bennett, G.N.2    Papoutsakis, E.T.3
  • 7
    • 0031007112 scopus 로고    scopus 로고
    • Evidence for the bacterial origin of genes encoding fermentation enzymes of the amitochondriate protozoan parasite Entamoeba histolytica
    • Rosenthal B., Mai Z., Caplivski D., Ghosh S., de la Vega H., Graf T. et al. Evidence for the bacterial origin of genes encoding fermentation enzymes of the amitochondriate protozoan parasite Entamoeba histolytica. J. Bacteriol. 179:1997;3736-3745.
    • (1997) J. Bacteriol. , vol.179 , pp. 3736-3745
    • Rosenthal, B.1    Mai, Z.2    Caplivski, D.3    Ghosh, S.4    De La Vega, H.5    Graf, T.6
  • 8
    • 0028356258 scopus 로고
    • Entamoeba histolytica has an alcohol dehydrogenase homologous to the multifunctional adhE gene product of Escherichia coli
    • Yang W., Li E., Kairong T., Stanley S.L. Jr Entamoeba histolytica has an alcohol dehydrogenase homologous to the multifunctional adhE gene product of Escherichia coli. Mol. Biochem. Parasitol. 64:1994;253-260.
    • (1994) Mol. Biochem. Parasitol. , vol.64 , pp. 253-260
    • Yang, W.1    Li, E.2    Kairong, T.3    Stanley S.L., Jr.4
  • 9
    • 0028172059 scopus 로고
    • +-dependent acetaldehyde/alcohol dehydrogenase from Entamoeba histolytica
    • +-dependent acetaldehyde/alcohol dehydrogenase from Entamoeba histolytica. Biochem. J. 303:1994;743-748.
    • (1994) Biochem. J. , vol.303 , pp. 743-748
    • Bruchhaus, I.1    Tannich, E.2
  • 12
    • 0020414001 scopus 로고
    • Purification and properties of NADP-linked, alcohol dehydrogenase from Entamoeba histolytica
    • Lo H.-S., Chang C.-J. Purification and properties of NADP-linked, alcohol dehydrogenase from Entamoeba histolytica. J. Parasitol. 68:1982;372-377.
    • (1982) J. Parasitol. , vol.68 , pp. 372-377
    • Lo, H.-S.1    Chang, C.-J.2
  • 13
    • 0017615796 scopus 로고
    • An energy conserving pyruvate-to-acetate pathway in Entamoeba histolytica. Pyruvatesynthase and a new acetate thiokinase
    • Reeves R.E., Warren L.G., Susskind B., Lo H.-S. An energy conserving pyruvate-to-acetate pathway in Entamoeba histolytica. Pyruvatesynthase and a new acetate thiokinase. J. Biol. Chem. 252:1977;726-731.
    • (1977) J. Biol. Chem. , vol.252 , pp. 726-731
    • Reeves, R.E.1    Warren, L.G.2    Susskind, B.3    Lo, H.-S.4
  • 15
    • 0029144215 scopus 로고
    • Virus-mediated expression of firefly luciferase in the parasitic protozoan Giardia lamblia
    • Yu D.C., Wang A.L., Wu C.H., Wang C.C. Virus-mediated expression of firefly luciferase in the parasitic protozoan Giardia lamblia. Mol. Cell. Biol. 15:1995;4867-4872.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 4867-4872
    • Yu, D.C.1    Wang, A.L.2    Wu, C.H.3    Wang, C.C.4
  • 16
    • 0024291288 scopus 로고
    • Simple RNA enzymes with new and highly specific endoribonuclease activities
    • Haseloff J., Gerlach W.L. Simple RNA enzymes with new and highly specific endoribonuclease activities. Nature. 334:1988;585-591.
    • (1988) Nature , vol.334 , pp. 585-591
    • Haseloff, J.1    Gerlach, W.L.2
  • 17
    • 0023221419 scopus 로고
    • A small catalytic oligoribonucleotide
    • Uhlenbeck O.C. A small catalytic oligoribonucleotide. Nature. 328:1987;596-600.
    • (1987) Nature , vol.328 , pp. 596-600
    • Uhlenbeck, O.C.1
  • 18
    • 0034011325 scopus 로고    scopus 로고
    • Inhibition of pyruvate-ferredoxin oxidoreductase gene expression in Giardia lamblia by virus-mediated hammerhead ribozyme
    • Dan M., Wang A.L., Wang C.C. Inhibition of pyruvate-ferredoxin oxidoreductase gene expression in Giardia lamblia by virus-mediated hammerhead ribozyme. Mol. Microbiol. 36:2000;447-456.
    • (2000) Mol. Microbiol. , vol.36 , pp. 447-456
    • Dan, M.1    Wang, A.L.2    Wang, C.C.3
  • 19
    • 0020651210 scopus 로고
    • Axenic culture of Giardia lamblia in TYI-S-33 medium supplemented with bile
    • Keister D.B. Axenic culture of Giardia lamblia in TYI-S-33 medium supplemented with bile. Trans. Roy. Soc. Trop. Med. Hyg. 77:1983;487-488.
    • (1983) Trans. Roy. Soc. Trop. Med. Hyg. , vol.77 , pp. 487-488
    • Keister, D.B.1
  • 20
    • 0000477426 scopus 로고    scopus 로고
    • Steady-state kinetics of the hypoxanthine-guanine-xanthine phosphoribosyltransferase from Tritrichomonas foetus: The role of threonine-47
    • Munagala N.R., Chin M.S., Wang C.C. Steady-state kinetics of the hypoxanthine-guanine-xanthine phosphoribosyltransferase from Tritrichomonas foetus: the role of threonine-47. Biochemistry. 37:1998;4045-4051.
    • (1998) Biochemistry , vol.37 , pp. 4045-4051
    • Munagala, N.R.1    Chin, M.S.2    Wang, C.C.3
  • 21
    • 0023267608 scopus 로고
    • Cloning and sequencing of the alcohol dehydrogenase II gene from Zymomonas mobilis
    • Conway T., Sewell G.W., Osman Y.A., Ingram L.O. Cloning and sequencing of the alcohol dehydrogenase II gene from Zymomonas mobilis. J. Bacteriol. 169:1987;2591-2597.
    • (1987) J. Bacteriol. , vol.169 , pp. 2591-2597
    • Conway, T.1    Sewell, G.W.2    Osman, Y.A.3    Ingram, L.O.4
  • 22
    • 0029010741 scopus 로고
    • AldB, an RpoS-dependent gene in Escherichia coli encoding an aldehyde dehydrogenase that is repressed by Fis and activated by Crp
    • Xu J., Johnson R.C. aldB, an RpoS-dependent gene in Escherichia coli encoding an aldehyde dehydrogenase that is repressed by Fis and activated by Crp. J. Bacteriol. 177:1995;3166-3175.
    • (1995) J. Bacteriol. , vol.177 , pp. 3166-3175
    • Xu, J.1    Johnson, R.C.2
  • 23
    • 0024342186 scopus 로고
    • Molecular analysis and nucleotide sequence of the adh1 gene encoding an NADPH-dependent butanol dehydrogenase in the Gram-positive anaerobe Clostridium acetobutylicum
    • Youngleson J.S., Jones W.A., Jones D.T., Woods D.R. Molecular analysis and nucleotide sequence of the adh1 gene encoding an NADPH-dependent butanol dehydrogenase in the Gram-positive anaerobe Clostridium acetobutylicum. Gene. 78:1989;355-364.
    • (1989) Gene , vol.78 , pp. 355-364
    • Youngleson, J.S.1    Jones, W.A.2    Jones, D.T.3    Woods, D.R.4
  • 24
    • 0021028885 scopus 로고
    • Purine salvage networks in Giardia lamblia
    • Wang C.C., Aldritt S. Purine salvage networks in Giardia lamblia. J. Exp. Med. 158:1983;1703-1712.
    • (1983) J. Exp. Med. , vol.158 , pp. 1703-1712
    • Wang, C.C.1    Aldritt, S.2
  • 25
    • 0032988857 scopus 로고    scopus 로고
    • The mitosome, a novel organelle related to mitochondria in the amitochondrial parasite Entamoeba histolytica
    • Tovar J., Fischer A., Clark C.G. The mitosome, a novel organelle related to mitochondria in the amitochondrial parasite Entamoeba histolytica. Mol. Microbiol. 32:1999;1013-1021.
    • (1999) Mol. Microbiol. , vol.32 , pp. 1013-1021
    • Tovar, J.1    Fischer, A.2    Clark, C.G.3
  • 26
    • 0030221888 scopus 로고    scopus 로고
    • Characterisation and purification of pyruvate:ferredoxin oxidoreductase from Giardia duodenalis
    • Townsen S.M., Upcroft J.A., Upcroft P. Characterisation and purification of pyruvate:ferredoxin oxidoreductase from Giardia duodenalis. Mol. Biochem. Parasitol. 79:1996;183-193.
    • (1996) Mol. Biochem. Parasitol. , vol.79 , pp. 183-193
    • Townsen, S.M.1    Upcroft, J.A.2    Upcroft, P.3
  • 27
    • 0030566707 scopus 로고    scopus 로고
    • Stable co-expression of a drug-resistance gene and a heterologous gene in an ancient parasitic protozoan Giardia lamblia
    • Yu D.C., Wang A.L., Wang C.C. Stable co-expression of a drug-resistance gene and a heterologous gene in an ancient parasitic protozoan Giardia lamblia. Mol. Biochem. Parasitol. 83:1996;81-91.
    • (1996) Mol. Biochem. Parasitol. , vol.83 , pp. 81-91
    • Yu, D.C.1    Wang, A.L.2    Wang, C.C.3
  • 28
    • 0025831040 scopus 로고
    • The biology of Giardia spp.
    • Adam R.D. The biology of Giardia spp. Microbiol. Rev. 55:1991;706-732.
    • (1991) Microbiol. Rev. , vol.55 , pp. 706-732
    • Adam, R.D.1
  • 29
    • 0031812552 scopus 로고    scopus 로고
    • Molecular comparison of Giardia lamblia isolates
    • Lu S.Q., Baruch A.C., Adam R.D. Molecular comparison of Giardia lamblia isolates. Int. J. Parasitol. 28:1998;1341-1345.
    • (1998) Int. J. Parasitol. , vol.28 , pp. 1341-1345
    • Lu, S.Q.1    Baruch, A.C.2    Adam, R.D.3
  • 30
    • 0032879297 scopus 로고    scopus 로고
    • Acetate utilization in Lactococcus lactis deficient in lactate dehydrogenase: A rescue pathway for maintaining redox balance
    • Hols P., Ramos A., Hugenholtz J., Delcour J., de Vos W.M., Santos H. et al. Acetate utilization in Lactococcus lactis deficient in lactate dehydrogenase: a rescue pathway for maintaining redox balance. J. Bacteriol. 181:1999;5521-5526.
    • (1999) J. Bacteriol. , vol.181 , pp. 5521-5526
    • Hols, P.1    Ramos, A.2    Hugenholtz, J.3    Delcour, J.4    De Vos, W.M.5    Santos, H.6
  • 31
    • 0030696219 scopus 로고    scopus 로고
    • +-dependent D-lactate dehydrogenase and insertional inactivation in a glycopeptide-resistant isolate
    • +-dependent D-lactate dehydrogenase and insertional inactivation in a glycopeptide-resistant isolate. J. Bacteriol. 179:1997;6756-6763.
    • (1997) J. Bacteriol. , vol.179 , pp. 6756-6763
    • Boyle-Vavra, S.1    De Jonge, B.L.2    Ebert, C.C.3    Daum, R.S.4
  • 32
    • 0024485336 scopus 로고
    • Mutants of Escherichia coli deficient in the fermentative lactate dehydrogenase
    • Mat-Jan F., Alam K.Y., Clark D.P. Mutants of Escherichia coli deficient in the fermentative lactate dehydrogenase. J. Bacteriol. 171:1989;342-348.
    • (1989) J. Bacteriol. , vol.171 , pp. 342-348
    • Mat-Jan, F.1    Alam, K.Y.2    Clark, D.P.3
  • 33
    • 0018995165 scopus 로고
    • Energy metabolism of the anaerobic protozoon Giardia lamblia
    • Lindmark D.G. Energy metabolism of the anaerobic protozoon Giardia lamblia. Mol. Biochem. Parasitol. 1:1980;1-12.
    • (1980) Mol. Biochem. Parasitol. , vol.1 , pp. 1-12
    • Lindmark, D.G.1
  • 34
    • 0032054650 scopus 로고    scopus 로고
    • Episomal and integrated maintenance of foreign DNA in Giardia lamblia
    • Singer S.M., Yee J., Nash T.E. Episomal and integrated maintenance of foreign DNA in Giardia lamblia. Mol. Biochem. Parasitol. 92:1998;59-69.
    • (1998) Mol. Biochem. Parasitol. , vol.92 , pp. 59-69
    • Singer, S.M.1    Yee, J.2    Nash, T.E.3
  • 35
    • 0031893062 scopus 로고    scopus 로고
    • Anaerobic bacterial metabolism in the ancient eukaryote Giardia duodenalis
    • Brown D.M., Upcroft J.A., Edwards M.R., Upcroft P. Anaerobic bacterial metabolism in the ancient eukaryote Giardia duodenalis. Int. J. Parasitol. 28:1998;149-164.
    • (1998) Int. J. Parasitol. , vol.28 , pp. 149-164
    • Brown, D.M.1    Upcroft, J.A.2    Edwards, M.R.3    Upcroft, P.4
  • 37
    • 0029661970 scopus 로고    scopus 로고
    • 2O-producing NADH oxidase from the protozoan parasite Giardia duodenalis
    • 2O-producing NADH oxidase from the protozoan parasite Giardia duodenalis. Eur. J. Biochem. 241:1996;155-161.
    • (1996) Eur. J. Biochem. , vol.241 , pp. 155-161
    • Brown, D.M.1    Upcroft, J.A.2    Upcroft, P.3
  • 38
    • 0343943477 scopus 로고    scopus 로고
    • Sánchez, L.B., personal communication
    • Sánchez, L.B., personal communication.
  • 39
    • 0033568692 scopus 로고    scopus 로고
    • Cloning and over-expression in Escherichia coli of the gene encoding NADPH group III alcohol dehydrogenase from Thermococcus hydrothermalis. Characterization and comparison of the native and the recombinant enzymes
    • Antoine E., Rolland J.L., Raffin J.P., Dietrich J. Cloning and over-expression in Escherichia coli of the gene encoding NADPH group III alcohol dehydrogenase from Thermococcus hydrothermalis. Characterization and comparison of the native and the recombinant enzymes. Eur. J. Biochem. 264:1999;880-889.
    • (1999) Eur. J. Biochem. , vol.264 , pp. 880-889
    • Antoine, E.1    Rolland, J.L.2    Raffin, J.P.3    Dietrich, J.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.