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Volumn 209, Issue 1-2, 1998, Pages 219-228

Cloning and heterologous expression of Entamoeba histolytica adenylate kinase and uridylate/cytidylate kinase

Author keywords

Amitochondriate protist; NMP kinase; Recombinant enzyme

Indexed keywords

ADENYLATE KINASE; COMPLEMENTARY DNA; PROTEIN KINASE; RECOMBINANT ENZYME;

EID: 0344333484     PISSN: 03781119     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0378-1119(98)00053-5     Document Type: Article
Times cited : (7)

References (33)
  • 1
    • 0002367729 scopus 로고    scopus 로고
    • MOLPHY version 2.3: Programs for molecular phylogenetics based on maximum likelihood
    • Institute of Statistical Mathematics, Tokyo, Japan
    • Adachi, J., Hasegawa, M., 1996. MOLPHY Version 2.3: Programs for Molecular Phylogenetics Based on Maximum Likelihood. Computer Science Monographs, No. 28, Institute of Statistical Mathematics, Tokyo, Japan, pp. 1-150.
    • (1996) Computer Science Monographs, No. 28 , pp. 1-150
    • Adachi, J.1    Hasegawa, M.2
  • 2
    • 0027735142 scopus 로고
    • Unusual gene organization in the protozoan parasite Entamoeba histolytica
    • Bruchhaus I., Leippe M., Lioutas C., Tannich E. Unusual gene organization in the protozoan parasite Entamoeba histolytica. DNA Cell Biol. 12:1993;925-933.
    • (1993) DNA Cell Biol. , vol.12 , pp. 925-933
    • Bruchhaus, I.1    Leippe, M.2    Lioutas, C.3    Tannich, E.4
  • 3
    • 0024379859 scopus 로고
    • Simultaneous editing of multiple nucleic acid and protein sequences with ESEE
    • Cabot E.L., Beckenbach A.T. Simultaneous editing of multiple nucleic acid and protein sequences with ESEE. Comp. Appl. Biosci. 5:1989;233-234.
    • (1989) Comp. Appl. Biosci. , vol.5 , pp. 233-234
    • Cabot, E.L.1    Beckenbach, A.T.2
  • 4
    • 0023490058 scopus 로고
    • Hydrogenosomal ATP:AMP phosphotransferase of Trichomonas vaginalis
    • Declerck P.J., Müller M. Hydrogenosomal ATP:AMP phosphotransferase of Trichomonas vaginalis. Comp. Biochem. Physiol. 88B:1987;575-580.
    • (1987) Comp. Biochem. Physiol. , vol.88 , pp. 575-580
    • Declerck, P.J.1    Müller, M.2
  • 5
    • 0026079373 scopus 로고
    • The refined structure of the complex between adenylate kinase from beef heart mitochondrial matrix and its substrate AMP at 1.85 Å resolution
    • Diederichs K., Schulz G.E. The refined structure of the complex between adenylate kinase from beef heart mitochondrial matrix and its substrate AMP at 1.85 Å resolution. J. Mol. Biol. 217:1991;541-549.
    • (1991) J. Mol. Biol. , vol.217 , pp. 541-549
    • Diederichs, K.1    Schulz, G.E.2
  • 6
    • 45149146414 scopus 로고
    • Tritrichomonas foetus: Purification and characterization of hydrogenosomal ATP:AMP phosphotransferase (adenylate kinase)
    • Dinbergs I.D., Lindmark D.G. Tritrichomonas foetus: Purification and characterization of hydrogenosomal ATP:AMP phosphotransferase (adenylate kinase). Exp. Parasitol. 69:1990;150-156.
    • (1990) Exp. Parasitol. , vol.69 , pp. 150-156
    • Dinbergs, I.D.1    Lindmark, D.G.2
  • 7
    • 0016794104 scopus 로고
    • Synthetic inhibitors of adenylate kinases in the assays for ATPases and phosphokinases
    • Feldhaus P., Frohlich T., Goody R.S., Isakov M., Schirmer R.H. Synthetic inhibitors of adenylate kinases in the assays for ATPases and phosphokinases. Eur. J. Biochem. 57:1975;197-204.
    • (1975) Eur. J. Biochem. , vol.57 , pp. 197-204
    • Feldhaus, P.1    Frohlich, T.2    Goody, R.S.3    Isakov, M.4    Schirmer, R.H.5
  • 8
    • 84959798530 scopus 로고
    • Cases in which parsimony or compatibility methods will be positively misleading
    • Felsenstein J. Cases in which parsimony or compatibility methods will be positively misleading. Syst. Zool. 27:1978;401-410.
    • (1978) Syst. Zool. , vol.27 , pp. 401-410
    • Felsenstein, J.1
  • 9
    • 0021259619 scopus 로고
    • Mitochondrial adenylate kinase (AK2) from bovine heart. Homology with the cytosolic isoenzyme in the catalytic region
    • Frank R., Trosin M., Tomasselli A.G., Schulz G.E., Schirmer R.H. Mitochondrial adenylate kinase (AK2) from bovine heart. Homology with the cytosolic isoenzyme in the catalytic region. Eur. J. Biochem. 141:1984;629-636.
    • (1984) Eur. J. Biochem. , vol.141 , pp. 629-636
    • Frank, R.1    Trosin, M.2    Tomasselli, A.G.3    Schulz, G.E.4    Schirmer, R.H.5
  • 10
    • 0029937408 scopus 로고    scopus 로고
    • Ancient divergence of long and short isoforms of adenylate kinase: Molecular evolution of the nucleoside monphosphate kinase family
    • Fukami-Kobayashi K., Nosaka M., Nakazawa A., Go M. Ancient divergence of long and short isoforms of adenylate kinase: molecular evolution of the nucleoside monphosphate kinase family. FEBS Lett. 385:1996;214-220.
    • (1996) FEBS Lett. , vol.385 , pp. 214-220
    • Fukami-Kobayashi, K.1    Nosaka, M.2    Nakazawa, A.3    Go, M.4
  • 12
    • 0030606607 scopus 로고    scopus 로고
    • Sequence analysis of the genome of the unicellular cyanobacterium Synechocystis sp. strain PCC6803. II. Sequence determination of the entire genome and assignment of potential protein-coding regions
    • Kaneko T., Sato S., Kotani H., Asamizu E., Nakamura Y. Sequence analysis of the genome of the unicellular cyanobacterium Synechocystis sp. strain PCC6803. II. Sequence determination of the entire genome and assignment of potential protein-coding regions. DNA Res. 3:1996;109-136.
    • (1996) DNA Res. , vol.3 , pp. 109-136
    • Kaneko, T.1    Sato, S.2    Kotani, H.3    Asamizu, E.4    Nakamura, Y.5
  • 13
    • 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
  • 14
    • 0025181359 scopus 로고
    • Maximum likelihood inference of protein phylogeny and the origin of chloroplasts
    • Kishino H., Miyata T., Hasegawa M. Maximum likelihood inference of protein phylogeny and the origin of chloroplasts. J. Mol. Evol. 30:1990;151-160.
    • (1990) J. Mol. Evol. , vol.30 , pp. 151-160
    • Kishino, H.1    Miyata, T.2    Hasegawa, M.3
  • 15
    • 0020528140 scopus 로고
    • Studies on adenosine triphosphate transphosphorylases. Human isoenzymes of adenylate kinase: Isolation and physicochemical comparison of the crystalline human ATP:AMP transphosphorylases from muscle and liver
    • Kuby S.A., Fleming G., Frischat A., Cress M.C., Hamada M. Studies on adenosine triphosphate transphosphorylases. Human isoenzymes of adenylate kinase: isolation and physicochemical comparison of the crystalline human ATP:AMP transphosphorylases from muscle and liver. J. Biol. Chem. 258:1983;1901-1907.
    • (1983) J. Biol. Chem. , vol.258 , pp. 1901-1907
    • Kuby, S.A.1    Fleming, G.2    Frischat, A.3    Cress, M.C.4    Hamada, M.5
  • 16
    • 0021768747 scopus 로고
    • Studies on adenosine triphosphate transphosphorylases. Amino acid sequence of rabbit muscle ATP-AMP transphosphorylase
    • Kuby S.A., Palmieri R.H., Frischat A., Fischer A.H., Wu L.H., Maland L., Manship M. Studies on adenosine triphosphate transphosphorylases. Amino acid sequence of rabbit muscle ATP-AMP transphosphorylase. Biochemistry. 23:1984;2393-2399.
    • (1984) Biochemistry , vol.23 , pp. 2393-2399
    • Kuby, S.A.1    Palmieri, R.H.2    Frischat, A.3    Fischer, A.H.4    Wu, L.H.5    Maland, L.6    Manship, M.7
  • 17
    • 0028132843 scopus 로고
    • Primary structure of the hydrogenosomal adenylate kinase of Trichomonas vaginalis and its phylogenetic relationships
    • Lange S., Rozario C., Müller M. Primary structure of the hydrogenosomal adenylate kinase of Trichomonas vaginalis and its phylogenetic relationships. Mol. Biochem. Parasitol. 66:1994;297-308.
    • (1994) Mol. Biochem. Parasitol. , vol.66 , pp. 297-308
    • Lange, S.1    Rozario, C.2    Müller, M.3
  • 18
    • 0021931861 scopus 로고
    • +-linked) and adenylate kinase as core and integral membrane enzymes respectively in the glycosomes of Trypanosoma rhodesiense
    • +-linked) and adenylate kinase as core and integral membrane enzymes respectively in the glycosomes of Trypanosoma rhodesiense. Mol. Biochem. Parasitol. 14:1985;219-230.
    • (1985) Mol. Biochem. Parasitol. , vol.14 , pp. 219-230
    • McLaughlin, J.1
  • 19
    • 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
  • 20
    • 0028327709 scopus 로고
    • The structure of uridylate kinase with its substrates, showing the transition state geometry
    • Müller-Dickmann H.J., Schulz G.E. The structure of uridylate kinase with its substrates, showing the transition state geometry. J. Mol. Biol. 236:1994;361-367.
    • (1994) J. Mol. Biol. , vol.236 , pp. 361-367
    • Müller-Dickmann, H.J.1    Schulz, G.E.2
  • 22
    • 0024469545 scopus 로고
    • Spectinomycin operon of Micrococcus luteus: Evolutionary implications of organization and novel codon usage
    • Ohama T., Muto A., Osawa S. Spectinomycin operon of Micrococcus luteus: Evolutionary implications of organization and novel codon usage. J. Mol. Evol. 29:1989;381-395.
    • (1989) J. Mol. Evol. , vol.29 , pp. 381-395
    • Ohama, T.1    Muto, A.2    Osawa, S.3
  • 23
    • 0029047080 scopus 로고
    • Cloning, sequencing, and expression in Escherichia coli of cDNA encoding porcine brain UMP-CMP kinase
    • Okajima T., Goto S., Tanizawa K., Tagaya M., Fukui T., Shimofuruya H., Suzuki J. Cloning, sequencing, and expression in Escherichia coli of cDNA encoding porcine brain UMP-CMP kinase. J. Biochem. 117:1995;980-986.
    • (1995) J. Biochem. , vol.117 , pp. 980-986
    • Okajima, T.1    Goto, S.2    Tanizawa, K.3    Tagaya, M.4    Fukui, T.5    Shimofuruya, H.6    Suzuki, J.7
  • 24
    • 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. Nucl. Acids Res. 21:1993;5264-5272.
    • (1993) Nucl. Acids Res. , vol.21 , pp. 5264-5272
    • Philippe, H.1
  • 25
    • 0343267810 scopus 로고    scopus 로고
    • Upstream regulatory elements controlling expression of the Entamoeba histolytica lectin
    • Purdy J.E., Pho L.T., Mann B.J., Petri W.A. Jr. Upstream regulatory elements controlling expression of the Entamoeba histolytica lectin. Mol. Biochem. Parasitol. 78:1996;91-103.
    • (1996) Mol. Biochem. Parasitol. , vol.78 , pp. 91-103
    • Purdy, J.E.1    Pho, L.T.2    Mann, B.J.3    Petri W.A., Jr.4
  • 26
    • 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
  • 27
    • 0029024433 scopus 로고
    • Primary structure of a putative adenylate kinase gene of Giardia lamblia
    • Rozario C., Müller M. Primary structure of a putative adenylate kinase gene of Giardia lamblia. Mol. Biochem. Parasitol. 71:1995;279-283.
    • (1995) Mol. Biochem. Parasitol. , vol.71 , pp. 279-283
    • Rozario, C.1    Müller, M.2
  • 29
    • 0015496583 scopus 로고
    • Sensitivity of adenylate kinase isozymes from normal and dystrophic human muscle to sulfhydryl reagents
    • Schirmer R.H., Thuma E. Sensitivity of adenylate kinase isozymes from normal and dystrophic human muscle to sulfhydryl reagents. Biochim. Biophys. Acta. 268:1972;92-97.
    • (1972) Biochim. Biophys. Acta , vol.268 , pp. 92-97
    • Schirmer, R.H.1    Thuma, E.2
  • 30
    • 0026471317 scopus 로고
    • The adenylate kinase family in yeast: Identification of URA6 as a multicopy suppressor of deficiency in major AMP kinase
    • Schricker R., Magdolen V., Kaniak A., Wolf K., Banlow W. The adenylate kinase family in yeast: identification of URA6 as a multicopy suppressor of deficiency in major AMP kinase. Gene. 122:1992;111-118.
    • (1992) Gene , vol.122 , pp. 111-118
    • Schricker, R.1    Magdolen, V.2    Kaniak, A.3    Wolf, K.4    Banlow, W.5
  • 31
    • 0026680259 scopus 로고
    • A new member of the adenylate kinase family in yeast: PAK3 is highly homologous to mammalian AK3 and is targeted to mitochondria
    • Schricker R., Magdolen V., Bandlow W. A new member of the adenylate kinase family in yeast: PAK3 is highly homologous to mammalian AK3 and is targeted to mitochondria. Mol. Gen. Genet. 233:1992;363-371.
    • (1992) Mol. Gen. Genet. , vol.233 , pp. 363-371
    • Schricker, R.1    Magdolen, V.2    Bandlow, W.3
  • 32
    • 0023677818 scopus 로고
    • Mechanism of adenylate kinase. Histidine-36 is not directly involved in catalysis, but protects cysteine-25 and stabilizes the tertiary structure
    • Tian G., Sanders C.R., Kishi F., Nakazawa A., Tsai M.D. Mechanism of adenylate kinase. Histidine-36 is not directly involved in catalysis, but protects cysteine-25 and stabilizes the tertiary structure. Biochemistry. 27:1988;5544-5552.
    • (1988) Biochemistry , vol.27 , pp. 5544-5552
    • Tian, G.1    Sanders, C.R.2    Kishi, F.3    Nakazawa, A.4    Tsai, M.D.5
  • 33
    • 0025256093 scopus 로고
    • CDNA-derived sequence of UMP-CMP kinase from Dictyostelium discoideum and expression of the enzyme in Escherichia coli
    • Wiesmüller L., Noegel A.A., Barzu O., Gerisch G., Schleicher M. cDNA-derived sequence of UMP-CMP kinase from Dictyostelium discoideum and expression of the enzyme in Escherichia coli. J. Biol. Chem. 265:1990;6339-6345.
    • (1990) J. Biol. Chem. , vol.265 , pp. 6339-6345
    • Wiesmüller, L.1    Noegel, A.A.2    Barzu, O.3    Gerisch, G.4    Schleicher, M.5


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