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Volumn 233, Issue 1-2, 1999, Pages 225-231

Cloning and sequencing of an acetyl-CoA synthetase (ADP-forming) gene from the amitochondriate protist, Giardia lamblia

Author keywords

Acetate formation; Glycolysis; Protein family

Indexed keywords

ACETYL COENZYME A SYNTHETASE; ADENOSINE DIPHOSPHATE;

EID: 0039445025     PISSN: 03781119     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0378-1119(99)00134-1     Document Type: Article
Times cited : (28)

References (29)
  • 2
    • 0027386619 scopus 로고
    • Purification and characterization of pyruvate ferredoxin oxidoreductase from the hyperthermophilic archaeon Pyrococcus furiosus
    • Blamey J.M., Adams M.W.W. Purification and characterization of pyruvate ferredoxin oxidoreductase from the hyperthermophilic archaeon Pyrococcus furiosus. Biochim. Biophys. Acta. 1161:1993;19-27.
    • (1993) Biochim. Biophys. Acta , vol.1161 , pp. 19-27
    • Blamey, J.M.1    Adams, M.W.W.2
  • 3
    • 15444350252 scopus 로고    scopus 로고
    • The complete genome sequence of Escherichia coli K-12
    • Blattner F.R., et al. The complete genome sequence of Escherichia coli K-12. Science. 277:1997;1432-1434.
    • (1997) Science , vol.277 , pp. 1432-1434
    • Blattner, F.R.1
  • 4
    • 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
  • 5
    • 0017759929 scopus 로고
    • The enzymic interconversion of acetate and acetyl-coenzyme A in Escherichia coli
    • Brown T.D.K., Jones-Mortimer M.C., Kornberg H.L. The enzymic interconversion of acetate and acetyl-coenzyme A in Escherichia coli. J. Gen. Microbiol. 102:1977;327-336.
    • (1977) J. Gen. Microbiol. , vol.102 , pp. 327-336
    • Brown, T.D.K.1    Jones-Mortimer, M.C.2    Kornberg, H.L.3
  • 6
    • 16044367245 scopus 로고    scopus 로고
    • Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii
    • Bult C.J., et al. Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii. Science. 273:1996;1058-1073.
    • (1996) Science , vol.273 , pp. 1058-1073
    • Bult, C.J.1
  • 7
    • 0002940098 scopus 로고    scopus 로고
    • Iron and sulfur in the origin and evolution of biological energy conversion systems
    • H. Baltscheffsky. New York, NY: VCH
    • Cammack R. Iron and sulfur in the origin and evolution of biological energy conversion systems. Baltscheffsky H. Origin and Evolution of Biological Energy Conversion. 1996;43-69 VCH, New York, NY.
    • (1996) Origin and Evolution of Biological Energy Conversion , pp. 43-69
    • Cammack, R.1
  • 8
    • 0031039802 scopus 로고    scopus 로고
    • Purification and properties of acetyl-CoA synthetase (ADP-forming), an archaeal enzyme of acetate formation and ATP synthesis, from the hyperthermophile Pyrococcus furiosus
    • Glasemacher J., Bock A.-K., Schmid R., Schönheit P. Purification and properties of acetyl-CoA synthetase (ADP-forming), an archaeal enzyme of acetate formation and ATP synthesis, from the hyperthermophile Pyrococcus furiosus. Eur. J. Biochem. 244:1997;561-567.
    • (1997) Eur. J. Biochem. , vol.244 , pp. 561-567
    • Glasemacher, J.1    Bock, A.-K.2    Schmid, R.3    Schönheit, P.4
  • 9
    • 0032548159 scopus 로고    scopus 로고
    • Sequence and phylogenetic position of a class II aldolase gene in the amitochondriate protist, Giardia lamblia
    • Henze K., Morrison H.G., Sogin M.L., Müller M. Sequence and phylogenetic position of a class II aldolase gene in the amitochondriate protist, Giardia lamblia. Gene. 222:1998;163-168.
    • (1998) Gene , vol.222 , pp. 163-168
    • Henze, K.1    Morrison, H.G.2    Sogin, M.L.3    Müller, M.4
  • 10
    • 0032580064 scopus 로고    scopus 로고
    • Complete sequence and gene organization of the genome of a hyper-thermophilic archaebacterium, Pyrococcus horikoshii OT3
    • Kawarabayashi Y., et al. Complete sequence and gene organization of the genome of a hyper-thermophilic archaebacterium, Pyrococcus horikoshii OT3. DNA Res. 5:(Suppl.):1998;147-155.
    • (1998) DNA Res , vol.5 , Issue.SUPPL. , pp. 147-155
    • Kawarabayashi, Y.1
  • 11
    • 0020651210 scopus 로고
    • Axenic culture of Giardia lamblia in TYI-S-33 medium supplemented with bile
    • Keister D. Axenic culture of Giardia lamblia in TYI-S-33 medium supplemented with bile. Trans. R. Soc. Trop. Med. Hyg. 77:1983;487-488.
    • (1983) Trans. R. Soc. Trop. Med. Hyg. , vol.77 , pp. 487-488
    • Keister, D.1
  • 12
    • 0031458333 scopus 로고    scopus 로고
    • The complete genome sequence of the hyperthermophilic, sulfate-reducing archaeon Archaeoglobus fulgidus
    • Klenk H.-P., et al. The complete genome sequence of the hyperthermophilic, sulfate-reducing archaeon Archaeoglobus fulgidus. Nature. 390:1997;364-370.
    • (1997) Nature , vol.390 , pp. 364-370
    • Klenk, H.-P.1
  • 13
    • 0029009026 scopus 로고
    • Cloning, characterization, and functional expression of acs, the gene which encodes acetyl cenzyme A synthetase in Escherichia coli
    • Kumari S., Tishel R., Eisenbach M., Wolfe A.J. Cloning, characterization, and functional expression of acs, the gene which encodes acetyl cenzyme A synthetase in Escherichia coli. J. Bacteriol. 177:1995;2878-2886.
    • (1995) J. Bacteriol. , vol.177 , pp. 2878-2886
    • Kumari, S.1    Tishel, R.2    Eisenbach, M.3    Wolfe, A.J.4
  • 14
    • 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
  • 15
    • 0028244070 scopus 로고
    • Indolepyruvate:ferredoxin oxidoreductase from the hyperthermophilic archaeon Pyrococcus furiosus
    • Mai X., Adams M.W.W. Indolepyruvate:ferredoxin oxidoreductase from the hyperthermophilic archaeon Pyrococcus furiosus. J. Biol. Chem. 269:1994;16726-16732.
    • (1994) J. Biol. Chem. , vol.269 , pp. 16726-16732
    • Mai, X.1    Adams, M.W.W.2
  • 16
    • 0029846960 scopus 로고    scopus 로고
    • Characterization of a fourth type of 2-keto acid-oxidizing enzyme from a hyperthermophilic archaeon: 2-ketoglutarate ferredoxin oxidoreductase from Thermococcus litoralis
    • Mai X., Adams M.W.W. Characterization of a fourth type of 2-keto acid-oxidizing enzyme from a hyperthermophilic archaeon: 2-ketoglutarate ferredoxin oxidoreductase from Thermococcus litoralis. J. Bacteriol. 178:1996;5890-5896.
    • (1996) J. Bacteriol. , vol.178 , pp. 5890-5896
    • Mai, X.1    Adams, M.W.W.2
  • 17
    • 0029794709 scopus 로고    scopus 로고
    • Purification and characterization of two reversible and ADP-dependent acetyl coenzyme A synthetases from the hyperthermophilic archaeon Pyrococcus furiosus
    • Mai X., Adams M.W.W. Purification and characterization of two reversible and ADP-dependent acetyl coenzyme A synthetases from the hyperthermophilic archaeon Pyrococcus furiosus. J. Bacteriol. 178:1996;5897-5903.
    • (1996) J. Bacteriol. , vol.178 , pp. 5897-5903
    • Mai, X.1    Adams, M.W.W.2
  • 18
    • 2642689666 scopus 로고    scopus 로고
    • The hydrogen hypothesis of the first eukaryote
    • Martin W.F., Müller M. The hydrogen hypothesis of the first eukaryote. Nature. 392:1998;37-41.
    • (1998) Nature , vol.392 , pp. 37-41
    • Martin, W.F.1    Müller, M.2
  • 19
    • 0000143331 scopus 로고    scopus 로고
    • Enzymes and compartmentation of core energy metabolism of anaerobic protists - A special case in eukaryotic evolution?
    • G.H. Coombs, K. Vickerman, M.A. Sleigh, & A. Warren. Dordrecht: Kluwer
    • Müller M. Enzymes and compartmentation of core energy metabolism of anaerobic protists - a special case in eukaryotic evolution? Coombs G.H., Vickerman K., Sleigh M.A., Warren A. Evolutionary Relationships among Protozoa. 1998;109-131 Kluwer, Dordrecht.
    • (1998) Evolutionary Relationships among Protozoa , pp. 109-131
    • Müller, M.1
  • 20
    • 0027494836 scopus 로고
    • MUST, a computer package of Management Utilities for Sequences and Trees
    • Philippe H. MUST, a computer package of Management Utilities for Sequences and Trees. Nucleic Acids Res. 21:1993;5264-5272.
    • (1993) Nucleic Acids Res. , vol.21 , pp. 5264-5272
    • Philippe, H.1
  • 21
    • 0025347097 scopus 로고
    • Purification and properties of acetyl-CoA synthetase from Bradyrhizobium japonicum bacteroids
    • Preston G.G., Wall J.D., Emerich D.W. Purification and properties of acetyl-CoA synthetase from Bradyrhizobium japonicum bacteroids. Biochem. J. 267:1990;179-183.
    • (1990) Biochem. J. , vol.267 , pp. 179-183
    • Preston, G.G.1    Wall, J.D.2    Emerich, D.W.3
  • 22
    • 0030035418 scopus 로고    scopus 로고
    • A set of ordered cosmids and a detailed genetic and physical map for the 8 Mb Streptomyces coelicolor A3(2) chromosome
    • Redenbach M., Kieser H.M., Denapaite D., Eichner A., Cullum J., Kinashi H., Hopwood D.A. A set of ordered cosmids and a detailed genetic and physical map for the 8 Mb Streptomyces coelicolor A3(2) chromosome. Mol. Microbiol. 21:1996;77-96.
    • (1996) Mol. Microbiol. , vol.21 , pp. 77-96
    • Redenbach, M.1    Kieser, H.M.2    Denapaite, D.3    Eichner, A.4    Cullum, J.5    Kinashi, H.6    Hopwood, D.A.7
  • 23
    • 0021729633 scopus 로고
    • Metabolism of Entamoeba histolytica Schaudinn, 1903
    • Reeves R.E. Metabolism of Entamoeba histolytica Schaudinn, 1903. Adv. Parasitol. 23:1984;105-142.
    • (1984) Adv. Parasitol. , vol.23 , pp. 105-142
    • Reeves, R.E.1
  • 24
    • 0017615796 scopus 로고
    • An energy-conserving pyruvate-to-acetate pathway in Entamoeba histolytica. Pyruvate synthase 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. Pyruvate synthase 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
  • 25
    • 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., Caplivksi D., Ghosh S., De la Vega H., Graf T., Samuelson J. Evidence for the bacterial origin of genes encoding fermentation enzymes of the amitochondriate protozoan parasite Entamoeba histolytica. J. Bacteriol. 179:1997;3736-3747.
    • (1997) J. Bacteriol. , vol.179 , pp. 3736-3747
    • Rosenthal, B.1    Mai, Z.2    Caplivksi, D.3    Ghosh, S.4    De La Vega, H.5    Graf, T.6    Samuelson, J.7
  • 26
    • 0343290301 scopus 로고    scopus 로고
    • Purification and characterization of the acetate forming enzyme, acetyl-CoA synthetase (ADP-forming) from the amitochondriate protist, Giardia lamblia
    • Sánchez L.B., Müller M. Purification and characterization of the acetate forming enzyme, acetyl-CoA synthetase (ADP-forming) from the amitochondriate protist, Giardia lamblia. FEBS Lett. 378:1996;240-244.
    • (1996) FEBS Lett. , vol.378 , pp. 240-244
    • Sánchez, L.B.1    Müller, M.2
  • 27
    • 0026083153 scopus 로고
    • Pyruvate metabolism of the hyperthermophilic archaebacterium Pyrococcus furiosus. Acetate formation from acetyl-CoA and ATP synthesis are catalysed by an acetyl-CoA synthetase (ADP forming)
    • Schafer T., Schönheit P. Pyruvate metabolism of the hyperthermophilic archaebacterium Pyrococcus furiosus. Acetate formation from acetyl-CoA and ATP synthesis are catalysed by an acetyl-CoA synthetase (ADP forming). Arch. Microbiol. 155:1991;366-377.
    • (1991) Arch. Microbiol. , vol.155 , pp. 366-377
    • Schafer, T.1    Schönheit, P.2
  • 28
    • 0031002263 scopus 로고    scopus 로고
    • Comparative analysis of Embden-Meyerhof and Entner-Doudoroff glycolytic pathways in hyperthermophilic archaea and the bacterium Thermotoga
    • Selig M., Xavier K.B., Santos H., Schönheit P. Comparative analysis of Embden-Meyerhof and Entner-Doudoroff glycolytic pathways in hyperthermophilic archaea and the bacterium Thermotoga. Arch. Microbiol. 167:1997;217-232.
    • (1997) Arch. Microbiol. , vol.167 , pp. 217-232
    • Selig, M.1    Xavier, K.B.2    Santos, H.3    Schönheit, P.4
  • 29
    • 0028049261 scopus 로고
    • Pyruvate ferredoxin oxidoreductases of the hyperthermophilic archaeon, Pyrococcus furiosus, and the hyperthermophilic bacterium, Thermotoga maritima, have different catalytic mechanisms
    • Smith E.T., Blamey J.M., Adams M.W.W. Pyruvate ferredoxin oxidoreductases of the hyperthermophilic archaeon, Pyrococcus furiosus, and the hyperthermophilic bacterium, Thermotoga maritima, have different catalytic mechanisms. Biochemistry. 33:1994;1008-1016.
    • (1994) Biochemistry , vol.33 , pp. 1008-1016
    • Smith, E.T.1    Blamey, J.M.2    Adams, M.W.W.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.