메뉴 건너뛰기




Volumn 179, Issue 11, 1997, Pages 3736-3745

Evidence for the bacterial origin of genes encoding fermentation enzymes of the amitochondriate protozoan parasite Entamoeba histolytica

Author keywords

[No Author keywords available]

Indexed keywords

ALCOHOL DEHYDROGENASE; FERREDOXIN; HEAT SHOCK PROTEIN 60; NICOTINAMIDE ADENINE DINUCLEOTIDE (PHOSPHATE) TRANSHYDROGENASE; PYRUVATE SYNTHASE; SUPEROXIDE DISMUTASE;

EID: 0031007112     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/jb.179.11.3736-3745.1997     Document Type: Article
Times cited : (95)

References (69)
  • 1
    • 1842313285 scopus 로고
    • The biology of Giardia sp
    • Adam, R. D. 1991. The biology of Giardia sp. Microbiol. Rev. 42:465-488.
    • (1991) Microbiol. Rev. , vol.42 , pp. 465-488
    • Adam, R.D.1
  • 4
    • 0023701258 scopus 로고
    • Nucleotide sequence of a 24,206-base-pair DNA fragment carrying the entire nitrogen fixation gene cluster of Klebsiella pneumoniae
    • Arnold, W., A. Rump, W. Klipp, U. B. Priefer, and A. Puhler. 1988. Nucleotide sequence of a 24,206-base-pair DNA fragment carrying the entire nitrogen fixation gene cluster of Klebsiella pneumoniae. J. Mol. Biol. 203: 715-738.
    • (1988) J. Mol. Biol. , vol.203 , pp. 715-738
    • Arnold, W.1    Rump, A.2    Klipp, W.3    Priefer, U.B.4    Puhler, A.5
  • 5
    • 0025882349 scopus 로고
    • PROSITE: A dictionary of sites and patterns in proteins
    • Bairoch, A. 1991. PROSITE: a dictionary of sites and patterns in proteins. Nucleic Acids Res. 19:2241-2245.
    • (1991) Nucleic Acids Res. , vol.19 , pp. 2241-2245
    • Bairoch, A.1
  • 6
    • 0027498463 scopus 로고
    • Entamoeba histolytica as a model for the primitive eukaryotic cell
    • Bakker-Grunwald, T., and C. Wostmann. 1993. Entamoeba histolytica as a model for the primitive eukaryotic cell. Parasitol. Today 9:27-31.
    • (1993) Parasitol. Today , vol.9 , pp. 27-31
    • Bakker-Grunwald, T.1    Wostmann, C.2
  • 7
    • 0027735142 scopus 로고
    • Unusual gene organization in the protozoan parasite Entamoeba histolytica
    • Bruchhaus, I., M. Leippe, M. Lioutas, and E. Tannich. 1993. Unusual gene organization in the protozoan parasite Entamoeba histolytica. DNA Cell Biol. 12:925-933.
    • (1993) DNA Cell Biol. , vol.12 , pp. 925-933
    • Bruchhaus, I.1    Leippe, M.2    Lioutas, M.3    Tannich, E.4
  • 8
    • 0027507966 scopus 로고
    • Primary structure of the pyruvate phosphate dikinase in Entamoeba histolytica
    • Bruchhaus, I., and E. Tannich. 1993. Primary structure of the pyruvate phosphate dikinase in Entamoeba histolytica. Mol. Biochem. Parasitol. 62: 153-156.
    • (1993) Mol. Biochem. Parasitol. , vol.62 , pp. 153-156
    • Bruchhaus, I.1    Tannich, E.2
  • 9
    • 0028172059 scopus 로고
    • +-dependent acetaldehyde/alcohol dehydrogenase from Entamoeba histolytica
    • +-dependent acetaldehyde/alcohol dehydrogenase from Entamoeba histolytica. Biochem. J. 303:743-748.
    • (1994) Biochem. J. , vol.303 , pp. 743-748
    • Bruchhaus, I.1    Tannich, E.2
  • 10
    • 0028914574 scopus 로고
    • Identification of an Entamoeba histolytica gene encoding a protein homologous to prokaryotic disulphide oxidoreductases
    • Bruchhaus, I., and E. Tannich. 1995. Identification of an Entamoeba histolytica gene encoding a protein homologous to prokaryotic disulphide oxidoreductases. Mol. Biochem. Parasitol. 70:187-195.
    • (1995) Mol. Biochem. Parasitol. , vol.70 , pp. 187-195
    • Bruchhaus, I.1    Tannich, E.2
  • 11
    • 0029817685 scopus 로고    scopus 로고
    • A common evolutionary origin for mitochondria and hydrogenosomes
    • Bui, E. T. N., P. J. Bradley, and P. J. Johnson. 1996. A common evolutionary origin for mitochondria and hydrogenosomes. Proc. Natl. Acad. Sci. USA 93:9651-9656.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 9651-9656
    • Bui, E.T.N.1    Bradley, P.J.2    Johnson, P.J.3
  • 12
    • 0024483266 scopus 로고
    • Fluorescent labeling of mitochondria
    • Chen, L. B. 1989. Fluorescent labeling of mitochondria. Methods Cell Biol. 29:103-123.
    • (1989) Methods Cell Biol. , vol.29 , pp. 103-123
    • Chen, L.B.1
  • 13
    • 0029068423 scopus 로고
    • Direct evidence for secondary loss of mitochondria in Entamoeba histolytica
    • Clark, C. G., and A. J. Rogers. 1995. Direct evidence for secondary loss of mitochondria in Entamoeba histolytica. Proc. Natl. Acad. Sci. USA 92:6518-6521.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 6518-6521
    • Clark, C.G.1    Rogers, A.J.2
  • 14
    • 0000228203 scopus 로고
    • A model of evolutionary change in proteins
    • M. O. Dayhoff (ed.) National Biomedical Research Foundation, Washington, D.C.
    • Dayhoff, M. O., R. M. Schwartz, and B. C. Orcutt. 1978. A model of evolutionary change in proteins, p. 345-352. In M. O. Dayhoff (ed.) Atlas of protein sequence structure, vol. 5, suppl. 3. National Biomedical Research Foundation, Washington, D.C.
    • (1978) Atlas of Protein Sequence Structure , vol.5 , Issue.3 SUPPL. , pp. 345-352
    • Dayhoff, M.O.1    Schwartz, R.M.2    Orcutt, B.C.3
  • 15
    • 0024062264 scopus 로고
    • Multiple aligned sequence editor (MASE)
    • Faulkner, D. V., and J. Jurka. 1988. Multiple aligned sequence editor (MASE). Trends Biochem. Sci. 13:321-322.
    • (1988) Trends Biochem. Sci. , vol.13 , pp. 321-322
    • Faulkner, D.V.1    Jurka, J.2
  • 16
    • 0000122573 scopus 로고
    • PHYLIP - Phylogeny inference package
    • Felsenstein, J. 1989. PHYLIP - phylogeny inference package (version 3.2). Cladistics 5:164-166.
    • (1989) Cladistics , vol.5 , pp. 164-166
    • Felsenstein, J.1
  • 17
    • 0024849185 scopus 로고
    • Cloning and sequence analysis of the fermentative alcohol-dehydrogenase-encoding gene of Escherichia coli
    • Goodlove, P. E., P. R. Cunningham, J. Parker, and D. P. Clark. 1989. Cloning and sequence analysis of the fermentative alcohol-dehydrogenase-encoding gene of Escherichia coli. Gene 85:209-214.
    • (1989) Gene , vol.85 , pp. 209-214
    • Goodlove, P.E.1    Cunningham, P.R.2    Parker, J.3    Clark, D.P.4
  • 18
    • 0024444559 scopus 로고
    • The evolutionary origins of organelles
    • Gray, M. W. 1989. The evolutionary origins of organelles. Trends Genet. 5:294-299.
    • (1989) Trends Genet. , vol.5 , pp. 294-299
    • Gray, M.W.1
  • 19
    • 0020047207 scopus 로고
    • Has the endosymbiont hypothesis been proven?
    • Gray, M. W., and W. F. Doolittle. 1982. Has the endosymbiont hypothesis been proven? Microbiol. Rev. 46:1-42.
    • (1982) Microbiol. Rev. , vol.46 , pp. 1-42
    • Gray, M.W.1    Doolittle, W.F.2
  • 20
    • 0028960169 scopus 로고
    • Evolution of the chaperonin families (Hsp60, Hsp10 and Tcp-1) of proteins and the origin of eukaryotic cells
    • Gupta, R. S. 1995. Evolution of the chaperonin families (Hsp60, Hsp10 and Tcp-1) of proteins and the origin of eukaryotic cells. Mol. Microbiol. 15:1-11.
    • (1995) Mol. Microbiol. , vol.15 , pp. 1-11
    • Gupta, R.S.1
  • 21
    • 0027565033 scopus 로고
    • Relative efficiencies of maximum likelihood, maximum parsimony, and neighbor-joining methods for estimating protein phylogeny
    • Hasegawa, M., and M. Fujiwara. 1993. Relative efficiencies of maximum likelihood, maximum parsimony, and neighbor-joining methods for estimating protein phylogeny. Mol. Phylogenet. Evol. 2:1-5.
    • (1993) Mol. Phylogenet. Evol. , vol.2 , pp. 1-5
    • Hasegawa, M.1    Fujiwara, M.2
  • 22
    • 0029096504 scopus 로고
    • Phylogenetic place of mitochondrion-lacking protozoan, Giardia lamblia, inferred from amino acid sequences of elongation factor 2
    • Hashimoto, T., Y. Nakamura, T. Kamaishi, F. Nakamura, J. Adachi, K.-I. Okamoto, and M. Hasegawa. 1995. Phylogenetic place of mitochondrion-lacking protozoan, Giardia lamblia, inferred from amino acid sequences of elongation factor 2. Mol. Biol. Evol. 12:782-793.
    • (1995) Mol. Biol. Evol. , vol.12 , pp. 782-793
    • Hashimoto, T.1    Nakamura, Y.2    Kamaishi, T.3    Nakamura, F.4    Adachi, J.5    Okamoto, K.-I.6    Hasegawa, M.7
  • 23
    • 0024432768 scopus 로고
    • A common structural motif in thiamin pyrophosphate-binding enzymes
    • Hawkins, C. F., A. Borges, and R. N. Perham. 1989. A common structural motif in thiamin pyrophosphate-binding enzymes. FEBS Lett. 255:77-82.
    • (1989) FEBS Lett. , vol.255 , pp. 77-82
    • Hawkins, C.F.1    Borges, A.2    Perham, R.N.3
  • 25
    • 0028874227 scopus 로고
    • Primary structure and eubacterial relationship of the pyruvate:ferredoxin oxidoreductase of the amitochondriate eukaryote, Trichomonas vaginalis
    • Hrdy, I., and M. Muller. 1995. Primary structure and eubacterial relationship of the pyruvate:ferredoxin oxidoreductase of the amitochondriate eukaryote, Trichomonas vaginalis. J. Mol. Evol. 41:388-396.
    • (1995) J. Mol. Evol. , vol.41 , pp. 388-396
    • Hrdy, I.1    Muller, M.2
  • 26
    • 0028928862 scopus 로고
    • Cloning and sequencing of a putative pyrophosphate-dependent phospho-fructokinase gene from Entamoeba histolytica
    • Huang, M., R. A. Albach, K. P. Chang, R. L. Tripathi, and R. G. Kemp. 1995. Cloning and sequencing of a putative pyrophosphate-dependent phospho-fructokinase gene from Entamoeba histolytica. Biochim. Biophys. Acta 1260: 215-217.
    • (1995) Biochim. Biophys. Acta , vol.1260 , pp. 215-217
    • Huang, M.1    Albach, R.A.2    Chang, K.P.3    Tripathi, R.L.4    Kemp, R.G.5
  • 28
    • 0025180595 scopus 로고
    • Molecular analysis of the hydrogenosomal ferredoxin of the anaerobic protist Trichomonas vaginalis
    • Johnson, P. J., C. E. D'Oliveira, T. E. Gorrell, and M. Muller. 1990. Molecular analysis of the hydrogenosomal ferredoxin of the anaerobic protist Trichomonas vaginalis. Proc. Natl. Acad. Sci. USA 87:6097-6101.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 6097-6101
    • Johnson, P.J.1    D'Oliveira, C.E.2    Gorrell, T.E.3    Muller, M.4
  • 29
    • 0030050611 scopus 로고    scopus 로고
    • Molecular and phylogenetic characterization of pyruvate and 2-ketoisovalerate ferredoxin oxidoreductases from Pyrococcus furiosus and pyruvate ferredoxin oxidoreductase from Thermotoga maritima
    • Kletzin, A., and M. W. W. Adams. 1996. Molecular and phylogenetic characterization of pyruvate and 2-ketoisovalerate ferredoxin oxidoreductases from Pyrococcus furiosus and pyruvate ferredoxin oxidoreductase from Thermotoga maritima. J. Bacteriol. 178:248-257.
    • (1996) J. Bacteriol. , vol.178 , pp. 248-257
    • Kletzin, A.1    Adams, M.W.W.2
  • 32
    • 0023941841 scopus 로고
    • Generation of cDNA probes directed by amino acid sequence: Cloning of urate oxidase
    • Lee, C. C., X. Wu, R. A. Gibbs, R. G. Cook, D. M. Muzny, and C. T. Caskey. 1988. Generation of cDNA probes directed by amino acid sequence: cloning of urate oxidase. Science 239:1288-1291.
    • (1988) Science , vol.239 , pp. 1288-1291
    • Lee, C.C.1    Wu, X.2    Gibbs, R.A.3    Cook, R.G.4    Muzny, D.M.5    Caskey, C.T.6
  • 33
    • 0025777891 scopus 로고
    • Aldehyde dehydrogenases: What can be learned from a baker's dozen sequences?
    • Lindahl, R, and J. Hempel. 1991. Aldehyde dehydrogenases: what can be learned from a baker's dozen sequences? Adv. Exp. Med. Biol. 284:1-8.
    • (1991) Adv. Exp. Med. Biol. , vol.284 , pp. 1-8
    • Lindahl, R.1    Hempel, J.2
  • 34
    • 0027943212 scopus 로고
    • Tracing the spread of fibroneclin type III domains in bacterial glycohydolases
    • Little, E., P. Bork, and R. F. Doolittle. 1994. Tracing the spread of fibroneclin type III domains in bacterial glycohydolases. J. Mol. Evol. 39:631-643.
    • (1994) J. Mol. Evol. , vol.39 , pp. 631-643
    • Little, E.1    Bork, P.2    Doolittle, R.F.3
  • 36
    • 0027423316 scopus 로고
    • A glyceraldehyde-3-phosphate dehydrogenase with eubacterial features in the amitochondriate eukaryote, Trichomonas vaginalis
    • Markos, A., A. Miretsky, and M. Muller. 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
  • 37
    • 0345730599 scopus 로고
    • Cell biology
    • K. N. Brown (ed.), John Wiley, Research Studies Press, New York, N.Y.
    • Martinez-Palomo, A. 1982. Cell biology, p. 5-59. In K. N. Brown (ed.), The biology of Entamoeba histolytica. John Wiley, Research Studies Press, New York, N.Y.
    • (1982) The Biology of Entamoeba Histolytica , pp. 5-59
    • Martinez-Palomo, A.1
  • 39
    • 0027057393 scopus 로고
    • Energy metabolism of ancestral eukaryotes: A hypothesis based on the biochemistry of amitochondriate parasitic proteins
    • Muller, M. 1992. Energy metabolism of ancestral eukaryotes: a hypothesis based on the biochemistry of amitochondriate parasitic proteins. BioSystems 28:33-40.
    • (1992) BioSystems , vol.28 , pp. 33-40
    • Muller, M.1
  • 40
    • 0027787578 scopus 로고
    • The hydrogenosome
    • Muller, M. 1993. The hydrogenosome. J. Gen. Microbiol. 139:2879-2889.
    • (1993) J. Gen. Microbiol. , vol.139 , pp. 2879-2889
    • Muller, M.1
  • 41
    • 0027957210 scopus 로고
    • Molecular characterization of an aldehyde/alcohol dehydrogenase gene from Clostridium acetobutylicum ATCC 824
    • Nair, R. V., G. N. Bennett, and E. Papoutsakis. 1994. Molecular characterization of an aldehyde/alcohol dehydrogenase gene from Clostridium acetobutylicum ATCC 824. J. Bacteriol. 176:871-885.
    • (1994) J. Bacteriol. , vol.176 , pp. 871-885
    • Nair, R.V.1    Bennett, G.N.2    Papoutsakis, E.3
  • 43
    • 0029018229 scopus 로고
    • Amebiasis. State-of-the-art clinical article
    • Ravdin, J. I. 1995. Amebiasis. State-of-the-art clinical article. Clin. Infect. Dis. 20:1453.
    • (1995) Clin. Infect. Dis. , vol.20 , pp. 1453
    • Ravdin, J.I.1
  • 44
    • 0021729633 scopus 로고
    • Metabolism of Entamoeba histolytica Schaudinn, 1903
    • Reeves, R. E. 1984. Metabolism of Entamoeba histolytica Schaudinn, 1903. Adv. Parasitol. 23:105-142.
    • (1984) Adv. Parasitol. , vol.23 , pp. 105-142
    • Reeves, R.E.1
  • 46
    • 0342561564 scopus 로고    scopus 로고
    • Cloning and characterization of the Entamoeba histolytica pyruvate:ferredoxin oxidoreductase gene
    • Rodriguez, M. A., M. E. Hidalgo, T. Sanchez, and E. Orozco. 1996. Cloning and characterization of the Entamoeba histolytica pyruvate:ferredoxin oxidoreductase gene. Mol. Biochem. Parasitol. 78:273-277.
    • (1996) Mol. Biochem. Parasitol. , vol.78 , pp. 273-277
    • Rodriguez, M.A.1    Hidalgo, M.E.2    Sanchez, T.3    Orozco, E.4
  • 47
    • 0029024433 scopus 로고
    • Primary structure of a putative adenylate kinase gene of Giardia lamblia
    • Rozario, C., and M. Muller. 1995. Primary structure of a putative adenylate kinase gene of Giardia lamblia. Mol. Biochem. Parasitol. 71:279-283.
    • (1995) Mol. Biochem. Parasitol. , vol.71 , pp. 279-283
    • Rozario, C.1    Muller, M.2
  • 48
    • 0028921499 scopus 로고
    • Primary sequence of a putative pyrophosphate-linked phosphofructokinase gene of Giardia lamblia
    • Rozario, C., M. W. Smith, and M. Muller. 1995. Primary sequence of a putative pyrophosphate-linked phosphofructokinase gene of Giardia lamblia. Biochim. Biophys. Acta 1260:218-222.
    • (1995) Biochim. Biophys. Acta , vol.1260 , pp. 218-222
    • Rozario, C.1    Smith, M.W.2    Muller, M.3
  • 49
    • 0023277329 scopus 로고
    • Signals guiding proteins to their correct locations in mitochondria
    • Schatz, G. 1987. Signals guiding proteins to their correct locations in mitochondria. Eur. J. Biochem. 165:1-6.
    • (1987) Eur. J. Biochem. , vol.165 , pp. 1-6
    • Schatz, G.1
  • 50
    • 0026490002 scopus 로고
    • Evolution by acquisition: The case for horizontal gene transfers
    • Smith, M. W., D.-F. Feng, and R. F. Doolittle. 1992. Evolution by acquisition: the case for horizontal gene transfers. Trends Biochem. Sci. 17:489-493.
    • (1992) Trends Biochem. Sci. , vol.17 , pp. 489-493
    • Smith, M.W.1    Feng, D.-F.2    Doolittle, R.F.3
  • 51
    • 0026527758 scopus 로고
    • Pattern-induced multi-sequence alignment (PIMA) algorithm employing secondary structure-dependent gap penalties for use in comparative protein modeling
    • Smith, R. F., and T. F. Smith. 1992. Pattern-induced multi-sequence alignment (PIMA) algorithm employing secondary structure-dependent gap penalties for use in comparative protein modeling. Protein Eng. 5:35-41.
    • (1992) Protein Eng. , vol.5 , pp. 35-41
    • Smith, R.F.1    Smith, T.F.2
  • 52
    • 0026282909 scopus 로고
    • Early evolution and the origin of eukaryoties
    • Sogin, M. L. 1991. Early evolution and the origin of eukaryoties. Curr. Opin. Genet. Dev. 1:457-163.
    • (1991) Curr. Opin. Genet. Dev. , vol.1 , pp. 457-1163
    • Sogin, M.L.1
  • 53
    • 0024962760 scopus 로고
    • Phylogenetic meaning of a kingdom concept: An unusual ribosomal RNA for Parasitol
    • Sogin, M. L., J. H. Gunderson, H. J. Elwood, and D. A. Peattie. 1989. Phylogenetic meaning of a kingdom concept: an unusual ribosomal RNA for Parasitol. Science 243:75-77.
    • (1989) Science , vol.243 , pp. 75-77
    • Sogin, M.L.1    Gunderson, J.H.2    Elwood, H.J.3    Peattie, D.A.4
  • 54
    • 0030047157 scopus 로고    scopus 로고
    • Molecular analysis of the anaerobic succinate degradation pathway in Clostridium kluyveri
    • Sohling, B., and G. Gottschalk. 1996. Molecular analysis of the anaerobic succinate degradation pathway in Clostridium kluyveri. J. Bacteriol. 178:871-880.
    • (1996) J. Bacteriol. , vol.178 , pp. 871-880
    • Sohling, B.1    Gottschalk, G.2
  • 55
    • 0025946099 scopus 로고
    • Pathogenic and nonpathogenic Entamoeba histolytica: Identification and molecular cloning of an iron-containing superoxide dismutase
    • Tannich, E., I. Bruchhaus, R. D. Walter, and R. D. Horstmann. 1992. Pathogenic and nonpathogenic Entamoeba histolytica: identification and molecular cloning of an iron-containing superoxide dismutase. Mol. Biochem. Parasitol. 49:61-72.
    • (1992) Mol. Biochem. Parasitol. , vol.49 , pp. 61-72
    • Tannich, E.1    Bruchhaus, I.2    Walter, R.D.3    Horstmann, R.D.4
  • 57
    • 0030221888 scopus 로고    scopus 로고
    • Characterization and purification of pyruvate:ferredoxin oxidoreductase from Giardia duodenalis
    • Townson, S. M., J. A. Upcroft, and P. Upcroft. 1996. Characterization and purification of pyruvate:ferredoxin oxidoreductase from Giardia duodenalis. Mol. Biochem. Parasitol. 79:183-193.
    • (1996) Mol. Biochem. Parasitol. , vol.79 , pp. 183-193
    • Townson, S.M.1    Upcroft, J.A.2    Upcroft, P.3
  • 58
    • 0027937054 scopus 로고
    • Evolutionary relationships of lactate dehydrogenases (LDHs) from mammals, birds, an amphibian, fish, barley, and bacteria: LDH cDNA sequences from Xenopus, pig, and rat
    • Tsuji, S., M. A. Qureshi, E. W. Hou, W. M. Fitch, and S. S.-L. Li. 1994. Evolutionary relationships of lactate dehydrogenases (LDHs) from mammals, birds, an amphibian, fish, barley, and bacteria: LDH cDNA sequences from Xenopus, pig, and rat. Proc. Natl. Acad. Sci. USA 91:9392-9396.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 9392-9396
    • Tsuji, S.1    Qureshi, M.A.2    Hou, E.W.3    Fitch, W.M.4    Li, S.S.-L.5
  • 60
    • 0020697189 scopus 로고
    • The mammalian pyruvate dehydrogenase complex: Structure, and regulation
    • Wieland, O. H. 1983. The mammalian pyruvate dehydrogenase complex: structure, and regulation. Rev. Biochem. Physiol. Pharmacol. 96:123-170.
    • (1983) Rev. Biochem. Physiol. Pharmacol. , vol.96 , pp. 123-170
    • Wieland, O.H.1
  • 61
    • 0023404237 scopus 로고
    • Homology of Saccharomyces cerevisiae ADH4 to an iron-activated alcohol dehydrogenase from Zymomonas mobilis
    • Williamson, V. M., and C. E. Paquin. 1987. Homology of Saccharomyces cerevisiae ADH4 to an iron-activated alcohol dehydrogenase from Zymomonas mobilis. Mol. Gen. Genet. 209:374-381.
    • (1987) Mol. Gen. Genet. , vol.209 , pp. 374-381
    • Williamson, V.M.1    Paquin, C.E.2
  • 62
    • 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
  • 64
    • 0028356258 scopus 로고
    • Entamoeba histolytica has an alcohol dehydrogenase homologous to the multifunctional adhE gene product of Escherichia coli
    • Yang, W., E. Li, T. Kairong, and S. L. Stanley, Jr. 1994. Entamoeba histolytica has an alcohol dehydrogenase homologous to the multifunctional adhE gene product of Escherichia coli. Mol. Biochem. Parasitol. 64:253-260.
    • (1994) Mol. Biochem. Parasitol. , vol.64 , pp. 253-260
    • Yang, W.1    Li, E.2    Kairong, T.3    Stanley Jr., S.L.4
  • 65
    • 0026648964 scopus 로고
    • Isolation and characterization of a NADP-dependent glutamate dehydrogenase from the primitive eukaryote Giardia lamblia
    • Yee, J., and P. F. Dennis. 1992. Isolation and characterization of a NADP-dependent glutamate dehydrogenase from the primitive eukaryote Giardia lamblia. J. Biol. Chem. 267:7539-7544.
    • (1992) J. Biol. Chem. , vol.267 , pp. 7539-7544
    • Yee, J.1    Dennis, P.F.2
  • 66
    • 0025361065 scopus 로고
    • Molecular evolution of zinc-containing long-chain alcohol genes
    • Yokoyama, S., R. Yokoyama, C. S. Kinlaw, and D. E. Harry. 1990. Molecular evolution of zinc-containing long-chain alcohol genes. Mol. Biol. Evol. 7:143-154.
    • (1990) Mol. Biol. Evol. , vol.7 , pp. 143-154
    • Yokoyama, S.1    Yokoyama, R.2    Kinlaw, C.S.3    Harry, D.E.4
  • 68
    • 0028574158 scopus 로고
    • Primary structure of an Entamoeba histolytica nicotinamide nucleotide transhydrogenase
    • Yu, Y., and J. Samuelson. 1994. Primary structure of an Entamoeba histolytica nicotinamide nucleotide transhydrogenase. Mol. Biochem. Parasitol. 68:323-328.
    • (1994) Mol. Biochem. Parasitol. , vol.68 , pp. 323-328
    • Yu, Y.1    Samuelson, J.2
  • 69


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.