메뉴 건너뛰기




Volumn 579, Issue 2, 2005, Pages 477-482

A novel octameric AMP-forming acetyl-CoA synthetase from the hyperthermophilic crenarchaeon Pyrobaculum aerophilum

Author keywords

AMP forming acetyl CoA synthetase; Hyperthermophilic archaea; Pyrobaculum aerophilum; Thermoadaptation

Indexed keywords

ACETIC ACID; ACETYL COENZYME A SYNTHETASE; ADENOSINE PHOSPHATE; AMINO ACID DERIVATIVE; ARGININE; ASPARAGINE; CARBOXYLIC ACID; CYSTEINE; GENE PRODUCT; GLUTAMIC ACID; GLUTAMINE; LYSINE; RECOMBINANT PROTEIN;

EID: 11844296747     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.febslet.2004.12.016     Document Type: Article
Times cited : (31)

References (26)
  • 1
    • 0026631359 scopus 로고
    • Ancestry of the 4-chlorobenzoate dehalogenase: Analysis of amino acid sequence identities among families of acyl:adenyl ligases, enoyl-CoA hydratases/isomerases, and acyl-CoA thioesterases
    • P.C. Babbitt, G.L. Kenyon, B.M. Martin, H. Charest, M. Slyvestre, J.D. Scholten, K.H. Chang, P.H. Liang, and D. Dunaway-Mariano Ancestry of the 4-chlorobenzoate dehalogenase: analysis of amino acid sequence identities among families of acyl:adenyl ligases, enoyl-CoA hydratases/isomerases, and acyl-CoA thioesterases Biochemistry 31 1992 5594 5604
    • (1992) Biochemistry , vol.31 , pp. 5594-5604
    • Babbitt, P.C.1    Kenyon, G.L.2    Martin, B.M.3    Charest, H.4    Slyvestre, M.5    Scholten, J.D.6    Chang, K.H.7    Liang, P.H.8    Dunaway-Mariano, D.9
  • 2
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • M.M. Bradford A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding Anal. Biochem. 72 1976 248 254
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 3
    • 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
    • C. Bräsen, and P. Schönheit Unusual ADP-forming acetyl-coenzyme A synthetases from the mesophilic halophilic euryarchaeon Haloarcula marismortui and from the hyperthermophilic crenarchaeon Pyrobaculum aerophilum Arch. Microbiol. 182 2004 277 287
    • (2004) Arch. Microbiol. , vol.182 , pp. 277-287
    • Bräsen, C.1    Schönheit, P.2
  • 4
    • 0034693042 scopus 로고    scopus 로고
    • Structural and genomic correlates of hyperthermostability
    • C. Cambillau, and J.M. Claverie Structural and genomic correlates of hyperthermostability J. Biol. Chem. 275 2000 32383 32386
    • (2000) J. Biol. Chem. , vol.275 , pp. 32383-32386
    • Cambillau, C.1    Claverie, J.M.2
  • 6
    • 0017350841 scopus 로고
    • Purification and properties of acetyl-coenzyme a synthetase from bakers' yeast
    • E.P. Frenkel, and R.L. Kitchens Purification and properties of acetyl-coenzyme A synthetase from bakers' yeast J. Biol. Chem. 252 1977 504 507
    • (1977) J. Biol. Chem. , vol.252 , pp. 504-507
    • Frenkel, E.P.1    Kitchens, R.L.2
  • 7
    • 0037452897 scopus 로고    scopus 로고
    • The 1.75 a crystal structure of acetyl-CoA synthetase bound to adenosine-5′-propylphosphate and coenzyme a
    • A.M. Gulick, V.J. Starai, A.R. Horswill, K.M. Homick, and J.C. Escalante-Semerena The 1.75 A crystal structure of acetyl-CoA synthetase bound to adenosine-5′-propylphosphate and coenzyme A Biochemistry 42 2003 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
  • 8
    • 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
    • M. Ishikawa, T. Fujino, H. Sakashita, K. Morikawa, and T. Yamamoto 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 1995 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
  • 9
    • 0024423884 scopus 로고
    • Isolation and characterization of acetyl-coenzyme a synthetase from Methanothrix soehngenii
    • M.S. Jetten, A.J. Stams, and A.J. Zehnder Isolation and characterization of acetyl-coenzyme A synthetase from Methanothrix soehngenii J. Bacteriol. 171 1989 5430 5435
    • (1989) J. Bacteriol. , vol.171 , pp. 5430-5435
    • Jetten, M.S.1    Stams, A.J.2    Zehnder, A.J.3
  • 10
    • 1042276711 scopus 로고    scopus 로고
    • Crystal structure of yeast acetyl-coenzyme a synthetase in complex with AMP
    • G. Jogl, and L. Tong Crystal structure of yeast acetyl-coenzyme A synthetase in complex with AMP Biochemistry 43 2004 1425 1431
    • (2004) Biochemistry , vol.43 , pp. 1425-1431
    • Jogl, G.1    Tong, L.2
  • 11
    • 3042995635 scopus 로고    scopus 로고
    • Properties of acetyl-CoA synthetase from Pseudomonas fluorescens
    • Y.S. Kim, J.H. An, B.H. Yang, and K.W. Kim Properties of acetyl-CoA synthetase from Pseudomonas fluorescens J. Biochem. Mol. Biol. 29 1996 277 285
    • (1996) J. Biochem. Mol. Biol. , vol.29 , pp. 277-285
    • Kim, Y.S.1    An, J.H.2    Yang, B.H.3    Kim, K.W.4
  • 12
    • 0029009026 scopus 로고
    • Cloning, characterization, and functional expression of acs, the gene which encodes acetyl-coenzyme a synthetase in Escherichia coli
    • S. Kumari, R. Tishel, M. Eisenbach, and A.J. Wolfe Cloning, characterization, and functional expression of acs, the gene which encodes acetyl-coenzyme 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
  • 13
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • U.K. Laemmli Cleavage of structural proteins during the assembly of the head of bacteriophage T4 Nature 227 1970 680 685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 14
    • 0141483333 scopus 로고    scopus 로고
    • Metabolic pathway promiscuity in the archaeon Sulfolobus solfataricus revealed by studies on glucose dehydrogenase and 2-keto-3-deoxygluconate aldolase
    • H.J. Lamble, N.I. Heyer, S.D. Bull, D.W. Hough, and M.J. Danson Metabolic pathway promiscuity in the archaeon Sulfolobus solfataricus revealed by studies on glucose dehydrogenase and 2-keto-3-deoxygluconate aldolase J. Biol. Chem. 278 2003 34066 34072
    • (2003) J. Biol. Chem. , vol.278 , pp. 34066-34072
    • Lamble, H.J.1    Heyer, N.I.2    Bull, S.D.3    Hough, D.W.4    Danson, M.J.5
  • 15
    • 0026768020 scopus 로고
    • Isolation and characterization of the acetyl-CoA synthetase from Penicillium chrysogenum. Involvement of this enzyme in the biosynthesis of penicillins
    • H. Martinez-Blanco, A. Reglero, M. Fernandez-Valverde, M.A. Ferrero, M.A. Moreno, M.A. Penalva, and J.M. Luengo Isolation and characterization of the acetyl-CoA synthetase from Penicillium chrysogenum. Involvement of this enzyme in the biosynthesis of penicillins J. Biol. Chem. 267 1992 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
  • 16
    • 0017176712 scopus 로고
    • Characterization of the acetyl-CoA synthetase of Acetobacter aceti
    • J. O'Sullivan, and L. Ettlinger Characterization of the acetyl-CoA synthetase of Acetobacter aceti Biochim. Biophys. Acta 450 1976 410 417
    • (1976) Biochim. Biophys. Acta , vol.450 , pp. 410-417
    • O'Sullivan, J.1    Ettlinger, L.2
  • 17
    • 0019254365 scopus 로고
    • Acetate thiokinase and the assimilation of acetate in Methanobacterium thermoautotrophicum
    • G. Oberlies, G. Fuchs, and R.K. Thauer Acetate thiokinase and the assimilation of acetate in Methanobacterium thermoautotrophicum Arch. Microbiol. 128 1980 248 252
    • (1980) Arch. Microbiol. , vol.128 , pp. 248-252
    • Oberlies, G.1    Fuchs, G.2    Thauer, R.K.3
  • 18
    • 0025347097 scopus 로고
    • Purification and properties of acetyl-CoA synthetase from Bradyrhizobium japonicum bacteroids
    • G.G. Preston, J.D. Wall, and D.W. Emerich 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
  • 19
    • 0001647511 scopus 로고
    • The citrate condensing enzyme of pigeon breast muscle and moth flight muscle
    • P.A. Srere, H. Brazil, and L. Gonen The citrate condensing enzyme of pigeon breast muscle and moth flight muscle Acta Chem. Scand. 17 1963 129 134
    • (1963) Acta Chem. Scand. , vol.17 , pp. 129-134
    • Srere, P.A.1    Brazil, H.2    Gonen, L.3
  • 20
    • 0347457075 scopus 로고    scopus 로고
    • Sir2-dependent activation of acetyl-CoA synthetase by deacetylation of active lysine
    • V.J. Starai, I. Celic, R.N. Cole, J.D. Boeke, and J.C. Escalante-Semerena Sir2-dependent activation of acetyl-CoA synthetase by deacetylation of active lysine Science 298 2002 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
  • 23
    • 0035098779 scopus 로고    scopus 로고
    • Hyperthermophilic enzymes: Sources, uses, and molecular mechanisms for thermostability
    • C. Vieille, and G.J. Zeikus Hyperthermophilic enzymes: sources, uses, and molecular mechanisms for thermostability Microbiol. Mol. Biol. Rev. 65 2001 1 43
    • (2001) Microbiol. Mol. Biol. Rev. , vol.65 , pp. 1-43
    • Vieille, C.1    Zeikus, G.J.2
  • 26
    • 0001610911 scopus 로고
    • Spinach leaf acetyl-coenzyme a synthetase: Purification and characterization
    • C.A. Zeiher, and D.D. Randall Spinach leaf acetyl-coenzyme A synthetase: purification and characterization Plant Physiol. 96 1991 382 389
    • (1991) Plant Physiol. , vol.96 , pp. 382-389
    • Zeiher, C.A.1    Randall, D.D.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.