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Volumn 9, Issue 5, 2005, Pages 355-365

AMP-forming acetyl-CoA synthetase from the extremely halophilic archaeon Haloarcula marismortui: Purification, identification and expression of the encoding gene, and phylogenetic affiliation

Author keywords

Acetate activation; ACS evolution; AMP forming acetyl CoA synthetase; Haloarcula marismortui; Halophilic archaea

Indexed keywords

ACETYL COENZYME A SYNTHETASE; ADENOSINE PHOSPHATE; POTASSIUM CHLORIDE; RECOMBINANT PROTEIN; SODIUM CHLORIDE;

EID: 26444522209     PISSN: 14310651     EISSN: 14334909     Source Type: Journal    
DOI: 10.1007/s00792-005-0449-0     Document Type: Article
Times cited : (17)

References (45)
  • 1
    • 0024297194 scopus 로고
    • Purification and characterization of acetate kinase from acetate-grown Methanosarcina thermophila. Evidence for regulation of synthesis
    • Aceti DJ, Ferry JG (1988) Purification and characterization of acetate kinase from acetate-grown Methanosarcina thermophila. Evidence for regulation of synthesis. J Biol Chem 263:15444-15448
    • (1988) J Biol Chem , vol.263 , pp. 15444-15448
    • Aceti, D.J.1    Ferry, J.G.2
  • 2
    • 0029994972 scopus 로고    scopus 로고
    • Glucose dehydrogenase from the halophilic Archaeon Haloferax mediterranei: Enzyme purification, characterisation and N-terminal sequence
    • Bonete MJ, Pire C, Llorca FI, Camacho ML (1996) Glucose dehydrogenase from the halophilic Archaeon Haloferax mediterranei: enzyme purification, characterisation and N-terminal sequence. FEBS Lett 383:227-229
    • (1996) FEBS Lett , vol.383 , pp. 227-229
    • Bonete, M.J.1    Pire, C.2    Llorca, F.I.3    Camacho, M.L.4
  • 3
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford MM (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72:248-254
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 4
    • 0034997498 scopus 로고    scopus 로고
    • Mechanisms of acetate formation and acetate activation in halophilic archaea
    • Erratum, 180:504, 2003
    • Bräsen C, Schönheit P (2001) Mechanisms of acetate formation and acetate activation in halophilic archaea. Arch Microbiol 175:360-368 (Erratum, 180:504, 2003)
    • (2001) Arch Microbiol , vol.175 , pp. 360-368
    • Bräsen, C.1    Schönheit, P.2
  • 5
    • 6344253194 scopus 로고    scopus 로고
    • Unusual ADP-forming acetyl-coenzyme A synthetases from the mesophilic halophilic euryarchaeon Haloarcula marismortui and from the hyperthermophilic crenarchaeon Pyrobaculum aerophilum
    • Bräsen C, Schönheit P (2004) Unusual ADP-forming acetyl-coenzyme A synthetases from the mesophilic halophilic euryarchaeon Haloarcula marismortui and from the hyperthermophilic crenarchaeon Pyrobaculum aerophilum. Arch Microbiol 182:277-287
    • (2004) Arch Microbiol , vol.182 , pp. 277-287
    • Bräsen, C.1    Schönheit, P.2
  • 6
    • 0033526898 scopus 로고    scopus 로고
    • Expression, reactivation, and purification of enzymes from Haloferax volcanii in Escherichia coli
    • Connaris H, Chaudhuri JB, Danson MJ, Hough DW (1999) Expression, reactivation, and purification of enzymes from Haloferax volcanii in Escherichia coli. Biotechnol Bioeng 64:38-45
    • (1999) Biotechnol Bioeng , vol.64 , pp. 38-45
    • Connaris, H.1    Chaudhuri, J.B.2    Danson, M.J.3    Hough, D.W.4
  • 7
    • 0030586251 scopus 로고    scopus 로고
    • NADP-glutamate dehydrogenase from the halophilic archaeon Haloferax mediterranei: Enzyme purification, N-terminal sequence and stability
    • Ferrer J, Perez-Pomares F, Bonete MJ (1996) NADP-glutamate dehydrogenase from the halophilic archaeon Haloferax mediterranei: enzyme purification, N-terminal sequence and stability. FEMS Microbiol Lett 141:59-63
    • (1996) FEMS Microbiol Lett , vol.141 , pp. 59-63
    • Ferrer, J.1    Perez-Pomares, F.2    Bonete, M.J.3
  • 8
    • 0035815751 scopus 로고    scopus 로고
    • Acetyl-CoA synthetase 2, a mitochondrial matrix enzyme involved in the oxidation of acetate
    • Fujino T, Kondo J, Ishikawa M, Morikawa K, Yamamoto TT (2001) Acetyl-CoA synthetase 2, a mitochondrial matrix enzyme involved in the oxidation of acetate. J Biol Chem 276:11420-11426
    • (2001) J Biol Chem , vol.276 , pp. 11420-11426
    • Fujino, T.1    Kondo, J.2    Ishikawa, M.3    Morikawa, K.4    Yamamoto, T.T.5
  • 10
    • 0037452897 scopus 로고    scopus 로고
    • The 1.75 Å crystal structure of acetyl-CoA synthetase bound to adenosine-5′-propylphosphate and coenzyme A
    • Gulick AM, Starai VJ, Horswill AR, Homick KM, Escalante-Semerena JC (2003) The 1.75 Å crystal structure of acetyl-CoA synthetase bound to adenosine-5′-propylphosphate and coenzyme A. Biochemistry 42:2866-2873
    • (2003) Biochemistry , vol.42 , pp. 2866-2873
    • Gulick, A.M.1    Starai, V.J.2    Horswill, A.R.3    Homick, K.M.4    Escalante-Semerena, J.C.5
  • 11
    • 0035823629 scopus 로고    scopus 로고
    • Transcriptional regulation of the murine acetyl-CoA synthetase 1 gene through multiple clustered binding sites for sterol regulatory element-binding proteins and a single neighboring site for Sp1
    • Ikeda Y, Yamamoto J, Okamura M, Fujino T, Takahashi S, Takeuchi K, Osborne TF, Yamamoto TT, Ito S, Sakai J (2001) Transcriptional regulation of the murine acetyl-CoA synthetase 1 gene through multiple clustered binding sites for sterol regulatory element-binding proteins and a single neighboring site for Sp1. J Biol Chem 276:34259-34269
    • (2001) J Biol Chem , vol.276 , pp. 34259-34269
    • Ikeda, Y.1    Yamamoto, J.2    Okamura, M.3    Fujino, T.4    Takahashi, S.5    Takeuchi, K.6    Osborne, T.F.7    Yamamoto, T.T.8    Ito, S.9    Sakai, J.10
  • 12
    • 0029199066 scopus 로고
    • Kinetic properties and structural characterization of highly purified acetyl-CoA synthetase from bovine heart and tissue distribution of the enzyme in rat tissues
    • Ishikawa M, Fujino T, Sakashita H, Morikawa K, Yamamoto T (1995) Kinetic properties and structural characterization of highly purified acetyl-CoA synthetase from bovine heart and tissue distribution of the enzyme in rat tissues. Tohoku J Exp Med 175:55-67
    • (1995) Tohoku J Exp Med , vol.175 , pp. 55-67
    • Ishikawa, M.1    Fujino, T.2    Sakashita, H.3    Morikawa, K.4    Yamamoto, T.5
  • 13
    • 0026780594 scopus 로고
    • Methanogenesis from acetate: A comparasion in Methanothrix soehngenii and Methanosarcina spp.
    • Jetten MSM, Stams AJM, Zehnder AJB (1992) Methanogenesis from acetate: a comparasion in Methanothrix soehngenii and Methanosarcina spp. FEMS Microbiol Rev 88:181-198
    • (1992) FEMS Microbiol Rev , vol.88 , pp. 181-198
    • Jetten, M.S.M.1    Stams, A.J.M.2    Zehnder, A.J.B.3
  • 14
    • 1042276711 scopus 로고    scopus 로고
    • Crystal structure of yeast acetyl-coenzyme A synthetase in complex with AMP
    • Jogl G, Tong L (2004) Crystal structure of yeast acetyl-coenzyme A synthetase in complex with AMP. Biochemistry 43:1425-1431
    • (2004) Biochemistry , vol.43 , pp. 1425-1431
    • Jogl, G.1    Tong, L.2
  • 15
    • 4444329994 scopus 로고    scopus 로고
    • Novel xylose dehydrogenase in the halophilic archaeon Haloarcula marismortui
    • Johnsen U, Schönheit P (2004) Novel xylose dehydrogenase in the halophilic archaeon Haloarcula marismortui. J Bacteriol 186:6198-6207
    • (2004) J Bacteriol , vol.186 , pp. 6198-6207
    • Johnsen, U.1    Schönheit, P.2
  • 16
    • 0035819933 scopus 로고    scopus 로고
    • Molecular evolution of the AMP-forming acetyl-CoA synthetase
    • Karan D, David JR, Capy P (2001) Molecular evolution of the AMP-forming acetyl-CoA synthetase. Gene 265:95-101
    • (2001) Gene , vol.265 , pp. 95-101
    • Karan, D.1    David, J.R.2    Capy, P.3
  • 17
    • 0029009026 scopus 로고
    • Cloning, characterization, and functional expression of acs, the gene which encodes acetyl coenzyme A synthetase in Escherichia coli
    • Kumari S, Tishel R, Eisenbach M, Wolfe AJ (1995) Cloning, characterization, and functional expression of acs, the gene which encodes acetyl coenzyme A synthetase in Escherichia coli. J Bacteriol 177:2878-2886
    • (1995) J Bacteriol , vol.177 , pp. 2878-2886
    • Kumari, S.1    Tishel, R.2    Eisenbach, M.3    Wolfe, A.J.4
  • 18
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli UK (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 19
    • 0034714382 scopus 로고    scopus 로고
    • Molecular characterization of human acetyl-CoA synthetase, an enzyme regulated by sterol regulatory element-binding proteins
    • Luong A, Hannah VC, Brown MS, Goldstein JL (2000) Molecular characterization of human acetyl-CoA synthetase, an enzyme regulated by sterol regulatory element-binding proteins. J Biol Chem 275:26458-26466
    • (2000) J Biol Chem , vol.275 , pp. 26458-26466
    • Luong, A.1    Hannah, V.C.2    Brown, M.S.3    Goldstein, J.L.4
  • 21
    • 0026768020 scopus 로고
    • Isolation and characterization of the acetyl-CoA synthetase from Penicillium chrysogenum. Involvement of this enzyme in the biosynthesis of penicillins
    • Martinez-Blanco H, Reglero A, Fernandez-Valverde M, Ferrero MA, Moreno MA, Penalva MA, Luengo JM (1992) Isolation and characterization of the acetyl-CoA synthetase from Penicillium chrysogenum. Involvement of this enzyme in the biosynthesis of penicillins. J Biol Chem 267:5474-5481
    • (1992) J Biol Chem , vol.267 , pp. 5474-5481
    • Martinez-Blanco, H.1    Reglero, A.2    Fernandez-Valverde, M.3    Ferrero, M.A.4    Moreno, M.A.5    Penalva, M.A.6    Luengo, J.M.7
  • 22
    • 0029900104 scopus 로고    scopus 로고
    • Purification and partial sequencing of high-affinity progesterone-binding site(s) from porcine liver membranes
    • Meyer C, Schmid R, Scriba PC, Wehling M (1996) Purification and partial sequencing of high-affinity progesterone-binding site(s) from porcine liver membranes. Eur J Biochem 239:726-731
    • (1996) Eur J Biochem , vol.239 , pp. 726-731
    • Meyer, C.1    Schmid, R.2    Scriba, P.C.3    Wehling, M.4
  • 23
    • 0019254365 scopus 로고
    • Acetate thiokinase and the assimilation of acetate in Methanobacterium thermoautotrophicum
    • Oberlies G, Fuchs G, Thauer RK (1980) Acetate thiokinase and the assimilation of acetate in Methanobacterium thermoautotrophicum. Arch Microbiol 128:248-252
    • (1980) Arch Microbiol , vol.128 , pp. 248-252
    • Oberlies, G.1    Fuchs, G.2    Thauer, R.K.3
  • 24
    • 0028973075 scopus 로고
    • Uptake and turnover of acetate in hypersaline environments
    • Oren A (1995) Uptake and turnover of acetate in hypersaline environments. FEMS Microbiol Ecol 18:75-85
    • (1995) FEMS Microbiol Ecol , vol.18 , pp. 75-85
    • Oren, A.1
  • 25
    • 0025276332 scopus 로고
    • Haloarcula marismortui (Volcani) sp. nov., nom. rev., an extremely halophilic bacterium from the Dead Sea
    • Oren A, Ginzburg M, Ginzburg BZ, Hochstein LI, Volcani BE (1990) Haloarcula marismortui (Volcani) sp. nov., nom. rev., an extremely halophilic bacterium from the Dead Sea. Int J Syst Bacteriol 40:209-210
    • (1990) Int J Syst Bacteriol , vol.40 , pp. 209-210
    • Oren, A.1    Ginzburg, M.2    Ginzburg, B.Z.3    Hochstein, L.I.4    Volcani, B.E.5
  • 26
    • 0017176712 scopus 로고
    • Characterization of the acetyl-CoA synthetase of Acetobacter aceti
    • O'Sullivan J, Ettlinger L (1976) Characterization of the acetyl-CoA synthetase of Acetobacter aceti. Biochim Biophys Acta 450:410-417
    • (1976) Biochim Biophys Acta , vol.450 , pp. 410-417
    • O'Sullivan, J.1    Ettlinger, L.2
  • 27
    • 0039765216 scopus 로고    scopus 로고
    • Acetyl-CoA synthetase from the amitochondriate eukaryote Giardia lamblia belongs to the newly recognized superfamily of acyl-CoA synthetases (nucleoside diphosphate-forming)
    • Sanchez LB, Galperin MY, Müller M (2000) Acetyl-CoA synthetase from the amitochondriate eukaryote Giardia lamblia belongs to the newly recognized superfamily of acyl-CoA synthetases (nucleoside diphosphate-forming). J Biol Chem 275:5794-5803
    • (2000) J Biol Chem , vol.275 , pp. 5794-5803
    • Sanchez, L.B.1    Galperin, M.Y.2    Müller, M.3
  • 28
    • 0023472472 scopus 로고
    • Tricine-sodium-dodecylsulfate-polyacrylamide gel electrophoresis for the separations of proteins in the range from 1-100 kDa
    • Schaegger H, von Jagow G (1987) Tricine-sodium-dodecylsulfate- polyacrylamide gel electrophoresis for the separations of proteins in the range from 1-100 kDa. Anal Biochem 166:368-379
    • (1987) Anal Biochem , vol.166 , pp. 368-379
    • Schaegger, H.1    Von Jagow, G.2
  • 29
    • 0036205377 scopus 로고    scopus 로고
    • TREE-PUZZLE: Maximum likelihood phylogenetic analysis using quartets and parallel computing
    • Schmidt HA, Strimmer K, Vingron M, von Haeseler A (2002) TREE-PUZZLE: maximum likelihood phylogenetic analysis using quartets and parallel computing. Bioinformatics 18:502-504
    • (2002) Bioinformatics , vol.18 , pp. 502-504
    • Schmidt, H.A.1    Strimmer, K.2    Vingron, M.3    Von Haeseler, A.4
  • 30
    • 0035975189 scopus 로고    scopus 로고
    • Sequencing, phylogenetic and transcriptional analysis of the glyoxylate bypass operon (ace) in the halophilic archaeon Haloferax volcanii
    • Serrano JA, Bonete MJ (2001) Sequencing, phylogenetic and transcriptional analysis of the glyoxylate bypass operon (ace) in the halophilic archaeon Haloferax volcanii. Biochim Biophys Acta 1520:154-162
    • (2001) Biochim Biophys Acta , vol.1520 , pp. 154-162
    • Serrano, J.A.1    Bonete, M.J.2
  • 31
    • 0031688651 scopus 로고    scopus 로고
    • Operation of glyoxylate cycle in halophilic archaea: Presence of malate synthase and isocitrate lyase in Haloferax volcanii
    • Serrano JA, Camacho M, Bonete MJ (1998) Operation of glyoxylate cycle in halophilic archaea: presence of malate synthase and isocitrate lyase in Haloferax volcanii. FEBS Lett 434:13-16
    • (1998) FEBS Lett , vol.434 , pp. 13-16
    • Serrano, J.A.1    Camacho, M.2    Bonete, M.J.3
  • 32
    • 12944283150 scopus 로고    scopus 로고
    • +-dependent protein deacetylase activity in the Sir2 protein family
    • USA
    • +-dependent protein deacetylase activity in the Sir2 protein family. Proc Natl Acad Sci USA 97:6658-6663
    • (2000) Proc Natl Acad Sci , vol.97 , pp. 6658-6663
    • Smith, J.S.1
  • 33
    • 0001647511 scopus 로고
    • The citrate condensing enzyme of pigeon breast muscle and moth flight muscle
    • Srere PA, Brazil H, Gonen L (1963) The citrate condensing enzyme of pigeon breast muscle and moth flight muscle. Acta Chem Scand 17:129-134
    • (1963) Acta Chem Scand , vol.17 , pp. 129-134
    • Srere, P.A.1    Brazil, H.2    Gonen, L.3
  • 35
    • 3242788065 scopus 로고    scopus 로고
    • Identification of the protein acetyltransferase (Pat) enzyme that acetylates acetyl-CoA synthetase in Salmonella enterica
    • Starai VJ, Escalante-Semerena JC (2004b) Identification of the protein acetyltransferase (Pat) enzyme that acetylates acetyl-CoA synthetase in Salmonella enterica. J Mol Biol 340:1005-1012
    • (2004) J Mol Biol , vol.340 , pp. 1005-1012
    • Starai, V.J.1    Escalante-Semerena, J.C.2
  • 36
    • 0347457075 scopus 로고    scopus 로고
    • Sir2-dependent activation of acetyl-CoA synthetase by deacetylation of active lysine
    • Starai VJ, Celic I, Cole RN, Boeke JD, Escalante-Semerena JC (2002) Sir2-dependent activation of acetyl-CoA synthetase by deacetylation of active lysine. Science 298:2390-2392
    • (2002) Science , vol.298 , pp. 2390-2392
    • Starai, V.J.1    Celic, I.2    Cole, R.N.3    Boeke, J.D.4    Escalante-Semerena, J.C.5
  • 37
    • 0037297590 scopus 로고    scopus 로고
    • Short-Chain fatty acid activation by acyl-coenzyme A synthetases requires SIR2 protein function in Salmonella enterica and Saccharomyces cerevisiae
    • Starai VJ, Takahashi H, Boeke JD, Escalante-Semerena JC (2003) Short-Chain fatty acid activation by acyl-coenzyme A synthetases requires SIR2 protein function in Salmonella enterica and Saccharomyces cerevisiae. Genetics 163:545-555
    • (2003) Genetics , vol.163 , pp. 545-555
    • Starai, V.J.1    Takahashi, H.2    Boeke, J.D.3    Escalante-Semerena, J.C.4
  • 38
    • 0034051227 scopus 로고    scopus 로고
    • Acetylation of histones and transcription-related factors
    • Sterner DE, Berger SL (2000) Acetylation of histones and transcription-related factors. Microbiol Mol Biol Rev 64:435-459
    • (2000) Microbiol Mol Biol Rev , vol.64 , pp. 435-459
    • Sterner, D.E.1    Berger, S.L.2
  • 39
    • 0023726308 scopus 로고
    • Citric-acid cycle, 50 years on. Modifications and an alternative pathway in anaerobic bacteria
    • Thauer RK (1988) Citric-acid cycle, 50 years on. Modifications and an alternative pathway in anaerobic bacteria. Eur J Biochem 176:497-508
    • (1988) Eur J Biochem , vol.176 , pp. 497-508
    • Thauer, R.K.1
  • 40
    • 0024418766 scopus 로고
    • Biochemistry of acetate catabolism in anaerobic chemotrophic bacteria
    • Thauer RK, Möller-Zinkhan D, Spormann AM (1989) Biochemistry of acetate catabolism in anaerobic chemotrophic bacteria. Annu Rev Microbiol 43:43-67
    • (1989) Annu Rev Microbiol , vol.43 , pp. 43-67
    • Thauer, R.K.1    Möller-Zinkhan, D.2    Spormann, A.M.3
  • 41
    • 0031574072 scopus 로고    scopus 로고
    • The CLUSTAL_X windows interface: Flexible strategies for multiple sequence alignment aided by quality analysis tools
    • Thompson JD, Gibson TJ, Plewniak F, Jeanmougin F, Higgins DG (1997) The CLUSTAL_X windows interface: flexible strategies for multiple sequence alignment aided by quality analysis tools. Nucleic Acids Res 25:4876-4882
    • (1997) Nucleic Acids Res , vol.25 , pp. 4876-4882
    • Thompson, J.D.1    Gibson, T.J.2    Plewniak, F.3    Jeanmougin, F.4    Higgins, D.G.5
  • 42
    • 0037181133 scopus 로고    scopus 로고
    • Evidence for an operative glyoxylate cycle in the thermoacidophilic crenarchaeon Sulfolobus acidocaldarius
    • Uhrigshardt H, Walden M, John H, Petersen A, Anemüller S (2002) Evidence for an operative glyoxylate cycle in the thermoacidophilic crenarchaeon Sulfolobus acidocaldarius. FEBS Lett 513:223-229
    • (2002) FEBS Lett , vol.513 , pp. 223-229
    • Uhrigshardt, H.1    Walden, M.2    John, H.3    Petersen, A.4    Anemüller, S.5
  • 44
    • 0001610911 scopus 로고
    • Spinach leaf acetyl-coenzyme A syntehtase: Purification and characterization
    • Zeiher CA, Randall DD (1991) Spinach leaf acetyl-coenzyme A syntehtase: Purification and characterization. Plant Physiol 96:382-389
    • (1991) Plant Physiol , vol.96 , pp. 382-389
    • Zeiher, C.A.1    Randall, D.D.2
  • 45
    • 26444613802 scopus 로고    scopus 로고
    • Personal communication. NSF grant reference (MCB-0135595)
    • Zhang P, Ng WV, DasSarma S (2003) Personal communication. http://zdna2.umbi.umd.edu, NSF grant reference (MCB-0135595)
    • (2003)
    • Zhang, P.1    Ng, W.V.2    DasSarma, S.3


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