메뉴 건너뛰기




Volumn 48, Issue 4, 1999, Pages 421-426

Close evolutionary relatedness of α-amylases from archaea and plants

Author keywords

Archaeons; Conserved sequence regions; Eubacteria; Eukaryotes; Evolutionary relationships; Thermococcus hydrothermalis; Amylase

Indexed keywords

AMYLASE;

EID: 0033025132     PISSN: 00222844     EISSN: None     Source Type: Journal    
DOI: 10.1007/PL00006486     Document Type: Article
Times cited : (55)

References (45)
  • 1
    • 0031864543 scopus 로고    scopus 로고
    • The SWISS-PROT protein sequence data bank and its supplement TrEMBL in 1998
    • Bairoch A, Apweiler R (1998) The SWISS-PROT protein sequence data bank and its supplement TrEMBL in 1998. Nucleic Acids Res 26:38-42
    • (1998) Nucleic Acids Res , vol.26 , pp. 38-42
    • Bairoch, A.1    Apweiler, R.2
  • 2
    • 0031925343 scopus 로고    scopus 로고
    • Glycosyl hydrolases from hyperthermophilic microorganisms
    • Bauer MW, Driskill LE, Kelly RM (1998) Glycosyl hydrolases from hyperthermophilic microorganisms. Curr Opin Biotechnol 9:141-145
    • (1998) Curr Opin Biotechnol , vol.9 , pp. 141-145
    • Bauer, M.W.1    Driskill, L.E.2    Kelly, R.M.3
  • 5
    • 0023047173 scopus 로고
    • The α-amylase gene in Drosophila melanogaster: Nucleotide sequence, gene structure and expression motifs
    • Boer PH, Hickey DA (1986) The α-amylase gene in Drosophila melanogaster: nucleotide sequence, gene structure and expression motifs. Nucleic Acids Res 14:8399-8411
    • (1986) Nucleic Acids Res , vol.14 , pp. 8399-8411
    • Boer, P.H.1    Hickey, D.A.2
  • 6
    • 0029563128 scopus 로고
    • Hyperthermostable mutants of Bacillus lichenifurmis α-amylase: Multiple amino acid replacements and molecular modelling
    • Declerck N, Joyet P, Trosset J-Y, Garnier J, Gaillardin C (1995) Hyperthermostable mutants of Bacillus lichenifurmis α-amylase: multiple amino acid replacements and molecular modelling. Protein Eng 8:1029-1037
    • (1995) Protein Eng , vol.8 , pp. 1029-1037
    • Declerck, N.1    Joyet, P.2    Trosset, J.-Y.3    Garnier, J.4    Gaillardin, C.5
  • 7
    • 0030826555 scopus 로고    scopus 로고
    • Cloning, sequencing, and expression of the gene encoding extracellular α-amylase from Pyrococcus furiosus and biochemical characterization of the recombinant enzyme
    • Dong G, Vieille C, Savchenko A, Zeikus JG (1997) Cloning, sequencing, and expression of the gene encoding extracellular α-amylase from Pyrococcus furiosus and biochemical characterization of the recombinant enzyme. Appl Environ Microbiol 63:3569-3576
    • (1997) Appl Environ Microbiol , vol.63 , pp. 3569-3576
    • Dong, G.1    Vieille, C.2    Savchenko, A.3    Zeikus, J.G.4
  • 8
    • 0026673888 scopus 로고
    • Purification, characterization, and nucleotide sequence of the thermolabile α-amylase from the antarctic psychotroph Alteromonas haloplanctis A23
    • Feller G, Lonhienne T, Deroanne C, Libioulle C, Van Beeumen J, Gerday C (1992) Purification, characterization, and nucleotide sequence of the thermolabile α-amylase from the antarctic psychotroph Alteromonas haloplanctis A23. J Biol Chem 267:5217-5221
    • (1992) J Biol Chem , vol.267 , pp. 5217-5221
    • Feller, G.1    Lonhienne, T.2    Deroanne, C.3    Libioulle, C.4    Van Beeumen, J.5    Gerday, C.6
  • 9
    • 0000461280 scopus 로고
    • Confidence limits on phylogenies: An approach using the bootstrap
    • Felsenstein J (1985) Confidence limits on phylogenies: an approach using the bootstrap. Evolution 39:783-791
    • (1985) Evolution , vol.39 , pp. 783-791
    • Felsenstein, J.1
  • 10
    • 0030724903 scopus 로고    scopus 로고
    • Molecular characterization of the α-amylase genes of Lactobacillus plantarum A6 and Lactobacillus amylovorus reveals an unusual 3′ end structure with direct tandem repeats and suggests a common evolutionary origin
    • Giraud E, Cuny G (1997) Molecular characterization of the α-amylase genes of Lactobacillus plantarum A6 and Lactobacillus amylovorus reveals an unusual 3′ end structure with direct tandem repeats and suggests a common evolutionary origin. Gene 198:149-157
    • (1997) Gene , vol.198 , pp. 149-157
    • Giraud, E.1    Cuny, G.2
  • 11
    • 0023852679 scopus 로고
    • Molecular cloning, characterization, and nucleotide sequence of an extracellular amylase gene from Aeromonas hydrophila
    • Gobius KS, Pemberton JM (1988) Molecular cloning, characterization, and nucleotide sequence of an extracellular amylase gene from Aeromonas hydrophila. J Bacteriol 170:1325-1332
    • (1988) J Bacteriol , vol.170 , pp. 1325-1332
    • Gobius, K.S.1    Pemberton, J.M.2
  • 12
    • 0029929874 scopus 로고    scopus 로고
    • Updating the sequence-based classification of glycosyl hydrolases
    • Henrissat B, Bairoch A (1996) Updating the sequence-based classification of glycosyl hydrolases. Biochem J 316:695-696
    • (1996) Biochem J , vol.316 , pp. 695-696
    • Henrissat, B.1    Bairoch, A.2
  • 13
    • 0024288689 scopus 로고
    • Cloning and expression in Escherichia coli of two additional amylase genes of a strictly anaerobic thermophile, Dictyoglomus thermophilum, and their nucleotide sequences with extremely low guanine-plus-cytosine contents
    • Horinouchi S, Fukusumi S, Ohshima T, Beppu T (1988) Cloning and expression in Escherichia coli of two additional amylase genes of a strictly anaerobic thermophile, Dictyoglomus thermophilum, and their nucleotide sequences with extremely low guanine-plus-cytosine contents. Eur J Biochem 176:243-253
    • (1988) Eur J Biochem , vol.176 , pp. 243-253
    • Horinouchi, S.1    Fukusumi, S.2    Ohshima, T.3    Beppu, T.4
  • 14
    • 0029740660 scopus 로고    scopus 로고
    • Raw-starch-digesting and thermostable α-amylase from the yeast Cryptococcus sp. S-2: Purification, characterization, cloning, and sequencing
    • Iefuji H, Chino M, Kato M, Iimura Y (1996) Raw-starch-digesting and thermostable α-amylase from the yeast Cryptococcus sp. S-2: purification, characterization, cloning, and sequencing. Biochem J 318:989-996
    • (1996) Biochem J , vol.318 , pp. 989-996
    • Iefuji, H.1    Chino, M.2    Kato, M.3    Iimura, Y.4
  • 15
    • 0028021627 scopus 로고
    • Sequence similarities and evolutionary relationships of microbial, plant and animal α-amylases
    • Janeček Š (1994) Sequence similarities and evolutionary relationships of microbial, plant and animal α-amylases. Eur J Biochem 224: 519-524
    • (1994) Eur J Biochem , vol.224 , pp. 519-524
    • Janeček, Š.1
  • 16
    • 0000300807 scopus 로고
    • Tracing the evolutionary lineages among α-amylases and cyclodextrin glycosyltransferases: The question of so-called "intermediary" enzymes
    • Janeček Š (1995) Tracing the evolutionary lineages among α-amylases and cyclodextrin glycosyltransferases: the question of so-called "intermediary" enzymes. Biologia 50:515-522
    • (1995) Biologia , vol.50 , pp. 515-522
    • Janeček, Š.1
  • 17
    • 0030778420 scopus 로고    scopus 로고
    • α-Amylase family: Molecular biology and evolution
    • Janeček Š (1997) α-Amylase family: Molecular biology and evolution. Prog Biophys Mol Biol 67:67-97
    • (1997) Prog Biophys Mol Biol , vol.67 , pp. 67-97
    • Janeček, Š.1
  • 18
    • 0031604393 scopus 로고    scopus 로고
    • Sequence of archaeal Methanococcus jannaschii α-amylase contains features of families 13 and 57 of glycosyl hydrolases: A trace of their common ancestor?
    • Janeček Š (1998) Sequence of archaeal Methanococcus jannaschii α-amylase contains features of families 13 and 57 of glycosyl hydrolases: a trace of their common ancestor? Folia Microbiol 43: 123-128
    • (1998) Folia Microbiol , vol.43 , pp. 123-128
    • Janeček, Š.1
  • 19
  • 22
    • 0030910823 scopus 로고    scopus 로고
    • Cloning, sequencing, characterization, and expression of an extracellular α-amylase from the hyperthermophilic archaeon Pyrococcus furiosus in Escherichia coli and Bacillus subtilis
    • Jørgensen S, Vorgias CE, Antranikian G (1997) Cloning, sequencing, characterization, and expression of an extracellular α-amylase from the hyperthermophilic archaeon Pyrococcus furiosus in Escherichia coli and Bacillus subtilis. J Biol Chem 272:16335-16342
    • (1997) J Biol Chem , vol.272 , pp. 16335-16342
    • Jørgensen, S.1    Vorgias, C.E.2    Antranikian, G.3
  • 23
    • 0032562777 scopus 로고    scopus 로고
    • Molecular structure of a barley α-amylase-inhibitor complex: Implications for starch binding and catalysis
    • Kadziola A, Søgaard M, Svensson B, Haser R (1998) Molecular structure of a barley α-amylase-inhibitor complex: implications for starch binding and catalysis. J Mol Biol 278:205-217
    • (1998) J Mol Biol , vol.278 , pp. 205-217
    • Kadziola, A.1    Søgaard, M.2    Svensson, B.3    Haser, R.4
  • 24
    • 0000157880 scopus 로고    scopus 로고
    • Cloning, nucleotide sequence, and hyperexpression of α-amylase gene from an archaeon, Thermococcus profundus
    • Lee JT, Kanai H, Kobayashi T, Akiba T, Kudo T (1996) Cloning, nucleotide sequence, and hyperexpression of α-amylase gene from an archaeon, Thermococcus profundus. J Ferment Bioeng 82:432-438
    • (1996) J Ferment Bioeng , vol.82 , pp. 432-438
    • Lee, J.T.1    Kanai, H.2    Kobayashi, T.3    Akiba, T.4    Kudo, T.5
  • 26
    • 0031028407 scopus 로고    scopus 로고
    • Properties and gene structure of the Thermotoga maritima α-amyiase AmyA, a putative lipoprotein of a hyperthermophilic bacterium
    • Liebl W, Stemplinger I, Ruile P (1997) Properties and gene structure of the Thermotoga maritima α-amyiase AmyA, a putative lipoprotein of a hyperthermophilic bacterium. J Bacteriol 179:941-948
    • (1997) J Bacteriol , vol.179 , pp. 941-948
    • Liebl, W.1    Stemplinger, I.2    Ruile, P.3
  • 27
    • 0023477190 scopus 로고
    • α-Amylase gene of Streptomyces limosus: Nucleotide sequence, expression motifs, and amino acid sequence homology to mammalian and invertebrate α-amylases
    • Long CM, Virolle M-J, Chang S-Y, Chang S, Bibb MJ (1987) α-Amylase gene of Streptomyces limosus: nucleotide sequence, expression motifs, and amino acid sequence homology to mammalian and invertebrate α-amylases. J Bacteriol 169:5745-5754
    • (1987) J Bacteriol , vol.169 , pp. 5745-5754
    • Long, C.M.1    Virolle, M.-J.2    Chang, S.-Y.3    Chang, S.4    Bibb, M.J.5
  • 28
    • 0028933531 scopus 로고
    • Crystal structure of calcium-depleted Bacillus lichenifarmis α-amylase at 2.2 Å resolution
    • Machius M, Wiegand G, Huber R (1995) Crystal structure of calcium-depleted Bacillus lichenifarmis α-amylase at 2.2 Å resolution. J Mol Biol 246:545-559
    • (1995) J Mol Biol , vol.246 , pp. 545-559
    • Machius, M.1    Wiegand, G.2    Huber, R.3
  • 29
    • 0030850422 scopus 로고    scopus 로고
    • The evolution of the Calvin cycle from prokaryotic to eukaryotic chromosomes: A case study of functional redundancy in ancient pathways through endosymbiosis
    • Martin W, Schnarrenberger C (1997) The evolution of the Calvin cycle from prokaryotic to eukaryotic chromosomes: a case study of functional redundancy in ancient pathways through endosymbiosis. Curr Genet 32:1-18
    • (1997) Curr Genet , vol.32 , pp. 1-18
    • Martin, W.1    Schnarrenberger, C.2
  • 30
    • 0022670999 scopus 로고
    • Comparison of amino acid sequences of eleven different α-amylases
    • Nakajima R, Imanaka T, Aiba S (1986) Comparison of amino acid sequences of eleven different α-amylases. Appl Microbiol Biotechnol 23:355-360
    • (1986) Appl Microbiol Biotechnol , vol.23 , pp. 355-360
    • Nakajima, R.1    Imanaka, T.2    Aiba, S.3
  • 35
    • 0024384836 scopus 로고
    • Hydrophobic cluster analysis of the primary sequences of αv-amylases
    • Raimbaud E, Buleon A, Perez S, Henrissat B (1989) Hydrophobic cluster analysis of the primary sequences of αv-amylases. Int J Biol Macromol 11:217-225
    • (1989) Int J Biol Macromol , vol.11 , pp. 217-225
    • Raimbaud, E.1    Buleon, A.2    Perez, S.3    Henrissat, B.4
  • 36
    • 0022431982 scopus 로고
    • Two barley α-amylase gene families are regulated differently in aleurone cells
    • Rogers JC (1985) Two barley α-amylase gene families are regulated differently in aleurone cells. J Biol Chem 260:3731-3738
    • (1985) J Biol Chem , vol.260 , pp. 3731-3738
    • Rogers, J.C.1
  • 37
    • 0021099734 scopus 로고
    • Isolation and sequence analysis of a barley α-amylase cDNA clone
    • Rogers JC, Milliman C (1983) Isolation and sequence analysis of a barley α-amylase cDNA clone. J Biol Chem 258:8169-8174
    • (1983) J Biol Chem , vol.258 , pp. 8169-8174
    • Rogers, J.C.1    Milliman, C.2
  • 38
    • 0031886567 scopus 로고    scopus 로고
    • Molecular characterization of the α-glucosidase gene (malA) from the hyperthermophilic archaeon Sulfolobus solfataricus
    • Rolfsmeier M, Haseltine C, Bini E, Clark A, Blum P (1998) Molecular characterization of the α-glucosidase gene (malA) from the hyperthermophilic archaeon Sulfolobus solfataricus. J Bacteriol 180: 1287-1295
    • (1998) J Bacteriol , vol.180 , pp. 1287-1295
    • Rolfsmeier, M.1    Haseltine, C.2    Bini, E.3    Clark, A.4    Blum, P.5
  • 39
    • 0023375195 scopus 로고
    • The neighbor-joining method: A new method for reconstructing phylogenetic trees
    • Saitou N, Nei M (1987) The neighbor-joining method: a new method for reconstructing phylogenetic trees. Mol Biol Evol 4:406-425
    • (1987) Mol Biol Evol , vol.4 , pp. 406-425
    • Saitou, N.1    Nei, M.2
  • 40
    • 0029859281 scopus 로고    scopus 로고
    • Cloning and expression of the α-amylase gene from the hyperthermophilic archaeon Pyrococcus sp. KOD1, and characterization of the enzyme
    • Tachibana Y, Mendez Leclere M, Fujiwara S, Takagi M, Imanaka T (1996) Cloning and expression of the α-amylase gene from the hyperthermophilic archaeon Pyrococcus sp. KOD1, and characterization of the enzyme. J Ferment Bioeng 82:224-232
    • (1996) J Ferment Bioeng , vol.82 , pp. 224-232
    • Tachibana, Y.1    Mendez Leclere, M.2    Fujiwara, S.3    Takagi, M.4    Imanaka, T.5
  • 41
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, positions specific gap penalties and weight matrix choice
    • Thompson JD, Higgins DG, Gibson TJ (1994) CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, positions specific gap penalties and weight matrix choice. Nucleic Acids Res 22:4673-4680
    • (1994) Nucleic Acids Res , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 42
    • 84989131370 scopus 로고
    • The complete amino acid sequence of Taka-amylase A
    • Toda H, Kondo K, Narita K (1982) The complete amino acid sequence of Taka-amylase A. Proc Japan Acad B58:208-212
    • (1982) Proc Japan Acad , vol.B58 , pp. 208-212
    • Toda, H.1    Kondo, K.2    Narita, K.3
  • 43
    • 0029889844 scopus 로고    scopus 로고
    • Cloning and sequencing analysis of three amylase cDNAs in the shrimp Penaeus vannamei (Crustacea decapoda): Evolutionary aspects
    • Van Wormhoudt A, Sellos D (1996) Cloning and sequencing analysis of three amylase cDNAs in the shrimp Penaeus vannamei (Crustacea decapoda): evolutionary aspects. J Mol Evol 42:543-551
    • (1996) J Mol Evol , vol.42 , pp. 543-551
    • Van Wormhoudt, A.1    Sellos, D.2
  • 44
    • 0021111544 scopus 로고
    • Nucleotide sequence of the amylase gens from Bacillus subtilis
    • Yang M, Galizzi A, Henner D (1983) Nucleotide sequence of the amylase gens from Bacillus subtilis. Nucleic Acids Res 11:237-249
    • (1983) Nucleic Acids Res , vol.11 , pp. 237-249
    • Yang, M.1    Galizzi, A.2    Henner, D.3
  • 45
    • 0022369683 scopus 로고
    • Complete nucleotide sequence of a gene coding for heat- and pH-stable α-amylase of Bacillus licheniformis: Comparison of the amino acid sequences of three bacterial liquefying α-amylases deduced from the DNA sequences
    • Yuuki T, Nomura T, Tezuka H, Tsuboi A, Yamagata H, Tsukagoshi N, Udaka S (1985) Complete nucleotide sequence of a gene coding for heat- and pH-stable α-amylase of Bacillus licheniformis: comparison of the amino acid sequences of three bacterial liquefying α-amylases deduced from the DNA sequences. J Biochem 98: 1147-1156
    • (1985) J Biochem , vol.98 , pp. 1147-1156
    • Yuuki, T.1    Nomura, T.2    Tezuka, H.3    Tsuboi, A.4    Yamagata, H.5    Tsukagoshi, N.6    Udaka, S.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.