메뉴 건너뛰기




Volumn 1, Issue 6, 2005, Pages 411-423

Oligomerization of Sulfolobus solfataricus signature amidase is promoted by acidic pH and high temperature

Author keywords

Amidase signature; Amide metabolism; Hyperthermophile

Indexed keywords

ARCHAEA; SULFOLOBUS SOLFATARICUS;

EID: 33244490042     PISSN: 14723646     EISSN: None     Source Type: Journal    
DOI: 10.1155/2005/543789     Document Type: Article
Times cited : (8)

References (44)
  • 1
    • 0033227463 scopus 로고    scopus 로고
    • Characterization of an inducible nitrilase from a thermophilic bacillus
    • Almatawah, A.A., R. Cramp and A. Cowan. 1999. Characterization of an inducible nitrilase from a thermophilic bacillus. Extremophiles 3:283-291.
    • (1999) Extremophiles , vol.3 , pp. 283-291
    • Almatawah, A.A.1    Cramp, R.2    Cowan, A.3
  • 3
    • 0014028960 scopus 로고
    • The reversibile acid dissociation and hybridization of lactic dehydrogenase
    • Anderson, S. and G. Weber. 1966. The reversibile acid dissociation and hybridization of lactic dehydrogenase. Arch. Biochem. Biophys. 116:207-223.
    • (1966) Arch. Biochem. Biophys. , vol.116 , pp. 207-223
    • Anderson, S.1    Weber, G.2
  • 4
    • 2242490907 scopus 로고    scopus 로고
    • Structural adaptation in a membrane enzyme that terminates endocannabinoid signaling
    • Bracey, M.H., M.A. Hanson, K.R. Masuda, R.C. Stevens and B.F. Cravatt. 2002. Structural adaptation in a membrane enzyme that terminates endocannabinoid signaling. Science 296: 1793-1796.
    • (2002) Science , vol.296 , pp. 1793-1796
    • Bracey, M.H.1    Hanson, M.A.2    Masuda, K.R.3    Stevens, R.C.4    Cravatt, B.F.5
  • 7
    • 0037093643 scopus 로고    scopus 로고
    • Docking unbound proteins using shape complementarity, desolvation and electrostatics
    • Chen, R. and Z. Weng. 2002. Docking unbound proteins using shape complementarity, desolvation and electrostatics. Proteins 47:281-294.
    • (2002) Proteins , vol.47 , pp. 281-294
    • Chen, R.1    Weng, Z.2
  • 8
    • 0029904838 scopus 로고    scopus 로고
    • Molecular characterization of an enzyme that degrades neuromodulatory fatty-acid amides
    • Cravatt, B.F., D.K. Giang, S.P. Mayfield, D.L. Boger, R.A. Lerner and N.B. Gilula. 1996. Molecular characterization of an enzyme that degrades neuromodulatory fatty-acid amides. Nature 384:83-87.
    • (1996) Nature , vol.384 , pp. 83-87
    • Cravatt, B.F.1    Giang, D.K.2    Mayfield, S.P.3    Boger, D.L.4    Lerner, R.A.5    Gilula, N.B.6
  • 10
    • 0016426743 scopus 로고
    • Extremely thermophilic acidophilic bacteria convergent with Sulfolobus acidocaldarius
    • De Rosa, M., A. Gambacorta and D. Bulock. 1975. Extremely thermophilic acidophilic bacteria convergent with Sulfolobus acidocaldarius. J. Gen. Microbiol. 86:154-164.
    • (1975) J. Gen. Microbiol. , vol.86 , pp. 154-164
    • De Rosa, M.1    Gambacorta, A.2    Bulock, D.3
  • 11
    • 0036122073 scopus 로고    scopus 로고
    • Prediction of protein-protein interaction sites in heterocomplexes with neural networks
    • Fariselli, P., F. Pazos, A. Valencia and R. Casadio. 2002. Prediction of protein-protein interaction sites in heterocomplexes with neural networks. Eur. J. Biochem. 269:1356-1361.
    • (2002) Eur. J. Biochem. , vol.269 , pp. 1356-1361
    • Fariselli, P.1    Pazos, F.2    Valencia, A.3    Casadio, R.4
  • 12
    • 0025180147 scopus 로고
    • Indolacetic acid operon of Pseudomonas syringae subsp. savastanoi: Transcription analysis and promoter identification
    • Gaffney, T.D., O. da Costa e Silva, T. Yamada and T. Kosuge. 1990. Indolacetic acid operon of Pseudomonas syringae subsp. savastanoi: transcription analysis and promoter identification. J. Bacteriol. 172:5593-5601.
    • (1990) J. Bacteriol. , vol.172 , pp. 5593-5601
    • Gaffney, T.D.1    Da Costa E Silva, O.2    Yamada, T.3    Kosuge, T.4
  • 13
    • 0024448151 scopus 로고
    • Calculation of protein extinction coefficients from amino acid sequence data
    • Gill, S. and P.H. von Hippel. 1989. Calculation of protein extinction coefficients from amino acid sequence data. Anal. Biochem. 182:319-326.
    • (1989) Anal. Biochem. , vol.182 , pp. 319-326
    • Gill, S.1    Von Hippel, P.H.2
  • 14
    • 0025838318 scopus 로고
    • Cloning and molecular characterization of the acetamidase-encoding gene (amdS) from Aspergillus orizae
    • Gomi, K., K. Kitamoto and C. Kumagai. 1991. Cloning and molecular characterization of the acetamidase-encoding gene (amdS) from Aspergillus orizae. Gene 108:91-98.
    • (1991) Gene , vol.108 , pp. 91-98
    • Gomi, K.1    Kitamoto, K.2    Kumagai, C.3
  • 15
    • 0034673175 scopus 로고    scopus 로고
    • pH-dependent changes in the in vitro ligand-binding properties and structure of human clusterin
    • Hochgrebe, T., G.J. Pankhurst, J. Wilce and S.B. Easterbrook-Smith. 2000. pH-dependent changes in the in vitro ligand-binding properties and structure of human clusterin. Biochemistry 15:1411-1419.
    • (2000) Biochemistry , vol.15 , pp. 1411-1419
    • Hochgrebe, T.1    Pankhurst, G.J.2    Wilce, J.3    Easterbrook-Smith, S.B.4
  • 16
    • 0034682705 scopus 로고    scopus 로고
    • Flipping the switch: The structural basis for signaling through the CRIB motif
    • Hoffman, G.R. and R.A. Cerione. 2000. Flipping the switch: the structural basis for signaling through the CRIB motif. Cell 102:403-406.
    • (2000) Cell , vol.102 , pp. 403-406
    • Hoffman, G.R.1    Cerione, R.A.2
  • 17
    • 0037151005 scopus 로고    scopus 로고
    • Structural characterizations of fusion peptide analog of influenza virus hemagglutinin. Implication of the necessity of a helix-hinge-helix motif in fusion activity
    • Hsu, C.H., S.H. Wu, D.K. Chang and C. Chen. 2002. Structural characterizations of fusion peptide analog of influenza virus hemagglutinin. Implication of the necessity of a helix-hinge-helix motif in fusion activity. J. Biol. Chem. 277:22,725-22,733.
    • (2002) J. Biol. Chem. , vol.277
    • Hsu, C.H.1    Wu, S.H.2    Chang, D.K.3    Chen, C.4
  • 18
    • 0030966367 scopus 로고    scopus 로고
    • Reconstitution of mitogen-activated protein kinase phosphorylation cascades in bacteria. Efficient synthesis of active protein kinases
    • Khokhlatchev, A., S. Xu, J. English, P. Wu, E. Schaefer and M.H. Cobb. 1997. Reconstitution of mitogen-activated protein kinase phosphorylation cascades in bacteria. Efficient synthesis of active protein kinases. J. Biol. Chem. 272:11,057-11,062.
    • (1997) J. Biol. Chem. , vol.272
    • Khokhlatchev, A.1    Xu, S.2    English, J.3    Wu, P.4    Schaefer, E.5    Cobb, M.H.6
  • 19
    • 0029976451 scopus 로고    scopus 로고
    • Tetrameric triosephosphate isomerase from hyperthermophilic Archaea
    • Kohlhoff, M., A. Dahm and R. Hensel. 1996. Tetrameric triosephosphate isomerase from hyperthermophilic Archaea. FEBS Lett. 383:245-250.
    • (1996) FEBS Lett. , vol.383 , pp. 245-250
    • Kohlhoff, M.1    Dahm, A.2    Hensel, R.3
  • 21
  • 22
    • 0025173890 scopus 로고
    • Use of nonlinear regression to analyze enzyme kinetic data: Application to situations of substrate contamination and background subtraction
    • Leatherbarrow, R.J. 1990. Use of nonlinear regression to analyze enzyme kinetic data: application to situations of substrate contamination and background subtraction. Anal. Biochem. 184:274-278.
    • (1990) Anal. Biochem. , vol.184 , pp. 274-278
    • Leatherbarrow, R.J.1
  • 23
    • 0041317291 scopus 로고    scopus 로고
    • The effect of interactions involving ionizable residues flanking membrane-inserted hydrophobic helices upon helix-helix interactions
    • Lew, S., G. A. Caputo and E. London. 2003. The effect of interactions involving ionizable residues flanking membrane-inserted hydrophobic helices upon helix-helix interactions. Biochemistry 42:10833-10842.
    • (2003) Biochemistry , vol.42 , pp. 10833-10842
    • Lew, S.1    Caputo, G.A.2    London, E.3
  • 24
    • 0034620517 scopus 로고    scopus 로고
    • Insights into the molecular relationship between malate and lactate dehydrogenases:structural and biochemical properties of monomeric and dimeric intermediates of a mutant of tetrameric L-(LDH-like) malate dehydrogenase from the halophilic archaeon Haloarcula marismortui
    • Madern, D., C. Ebel, M. Mevarech, S.B. Richard, C. Pfister and G. Zaccai. 2000. Insights into the molecular relationship between malate and lactate dehydrogenases:structural and biochemical properties of monomeric and dimeric intermediates of a mutant of tetrameric L-(LDH-like) malate dehydrogenase from the halophilic archaeon Haloarcula marismortui. Biochemistry 39:1001-1010.
    • (2000) Biochemistry , vol.39 , pp. 1001-1010
    • Madern, D.1    Ebel, C.2    Mevarech, M.3    Richard, S.B.4    Pfister, C.5    Zaccai, G.6
  • 25
    • 0035964362 scopus 로고    scopus 로고
    • Differences in the oligomeric states of the LDH-like MalDH from the hyperthermophilic archaea Methanococcus jannaschii and Archaeoglobus fulgidus
    • Madern, D., C. Ebel, H.A. Dale, T. Lien, I.H. Steen, N.K. Birkeland and G. Zaccai. 2001. Differences in the oligomeric states of the LDH-like MalDH from the hyperthermophilic archaea Methanococcus jannaschii and Archaeoglobus fulgidus. Biochemistry 40:10310-10316.
    • (2001) Biochemistry , vol.40 , pp. 10310-10316
    • Madern, D.1    Ebel, C.2    Dale, H.A.3    Lien, T.4    Steen, I.H.5    Birkeland, N.K.6    Zaccai, G.7
  • 26
    • 0025747960 scopus 로고
    • Purification, cloning, and primary structure of new enantiomer-selective amidase from Rhodococcus strain: Structural evidence for a conserved genetic coupling with nitrile hydratase
    • Mayaux, J.F., E. Cerebelaud, F. Soubrier, P. Yeh, F. Blanche and D. Petre. 1991. Purification, cloning, and primary structure of new enantiomer-selective amidase from Rhodococcus strain: structural evidence for a conserved genetic coupling with nitrile hydratase. J. Bacteriol. 173:6694-6704.
    • (1991) J. Bacteriol. , vol.173 , pp. 6694-6704
    • Mayaux, J.F.1    Cerebelaud, E.2    Soubrier, F.3    Yeh, P.4    Blanche, F.5    Petre, D.6
  • 27
    • 0000720562 scopus 로고
    • + cycling across the plasma membrane of the thermoacidophilic archaebacterium Sulfolobus acidocaldarius
    • + cycling across the plasma membrane of the thermoacidophilic archaebacterium Sulfolobus acidocaldarius. FEBS Lett. 32:359-363.
    • (1988) FEBS Lett. , vol.32 , pp. 359-363
    • Moll, R.1    Shafer, G.2
  • 28
    • 0023131203 scopus 로고
    • Proteolytic dimers of porcine muscle lactate dehydrogenase characterization, folding and reconstitution of the truncated and nicked polypeptide chain
    • Opitz, U., R. Rudolph, R. Jaenicke, L. Ericsson and H. Neurath. 1987. Proteolytic dimers of porcine muscle lactate dehydrogenase characterization, folding and reconstitution of the truncated and nicked polypeptide chain. Biochemistry 26:1399-1406
    • (1987) Biochemistry , vol.26 , pp. 1399-1406
    • Opitz, U.1    Rudolph, R.2    Jaenicke, R.3    Ericsson, L.4    Neurath, H.5
  • 29
    • 0034705440 scopus 로고    scopus 로고
    • Clarifying the catalytic roles of conserved residues in the amidase signature family
    • Patricelli, M.P. and B.F. Cravatt. 2000. Clarifying the catalytic roles of conserved residues in the amidase signature family. J. Biol. Chem. 275:19177-19184.
    • (2000) J. Biol. Chem. , vol.275 , pp. 19177-19184
    • Patricelli, M.P.1    Cravatt, B.F.2
  • 31
  • 32
    • 0025819086 scopus 로고
    • Temperature and pH dependence of the self-association of human spectrin
    • Ralston, G.B. 1991. Temperature and pH dependence of the self-association of human spectrin. Biochemistry 30:4179-4186.
    • (1991) Biochemistry , vol.30 , pp. 4179-4186
    • Ralston, G.B.1
  • 33
    • 0016828854 scopus 로고
    • Essential arginyl residues in aspartate aminotransferases
    • Riordan, J. and R. Scandurra. 1972. Essential arginyl residues in aspartate aminotransferases. Bioch. Biophys. Res. Comm. 66:417-424.
    • (1972) Bioch. Biophys. Res. Comm. , vol.66 , pp. 417-424
    • Riordan, J.1    Scandurra, R.2
  • 34
    • 0027136282 scopus 로고
    • Comparative protein modelling by satisfaction of spatial restraints
    • Sali, A. and T. L. Blundell. 1993. Comparative protein modelling by satisfaction of spatial restraints. J. Mol. Biol. 234:779-815.
    • (1993) J. Mol. Biol. , vol.234 , pp. 779-815
    • Sali, A.1    Blundell, T.L.2
  • 35
    • 0024285823 scopus 로고    scopus 로고
    • Protein biosynthesis in organelles requires misaminoacylation of tRNA
    • Schon, A., C.G. Kannangara, S. Gough and D. Soll. 1998. Protein biosynthesis in organelles requires misaminoacylation of tRNA. Nature 331:187-190.
    • (1998) Nature , vol.331 , pp. 187-190
    • Schon, A.1    Kannangara, C.G.2    Gough, S.3    Soll, D.4
  • 36
    • 0034668130 scopus 로고    scopus 로고
    • Determination of the sedimentation coefficient distribution by least-squares boundary modeling
    • Schuck, P. and P. Rossmanith. 2000. Determination of the sedimentation coefficient distribution by least-squares boundary modeling. Biopolymers 54:328-341.
    • (2000) Biopolymers , vol.54 , pp. 328-341
    • Schuck, P.1    Rossmanith, P.2
  • 37
    • 0035379978 scopus 로고    scopus 로고
    • Molecular and biochemical characterization of the recombinant amidase from hyperthermophilic archaeon Sulfolobus solfataricus
    • Scotto d'Abusco, A., S. Ammendola, R. Scandurra and L. Politi. 2001. Molecular and biochemical characterization of the recombinant amidase from hyperthermophilic archaeon Sulfolobus solfataricus. Extremophiles 5:183-192.
    • (2001) Extremophiles , vol.5 , pp. 183-192
    • Scotto D'Abusco, A.1    Ammendola, S.2    Scandurra, R.3    Politi, L.4
  • 38
    • 0033769510 scopus 로고    scopus 로고
    • A mutation affecting the association equilibrium of formyltransferase from the hyperthermophilic Methanopyrus kandleri and its influence on the enzyme's activity and thermostability
    • Shima, S., R.K. Thauer, U. Ermler, H. Durchschlag, C. Tziatzios and D. Shubert. 2000. A mutation affecting the association equilibrium of formyltransferase from the hyperthermophilic Methanopyrus kandleri and its influence on the enzyme's activity and thermostability. Eur. J. Biochem. 267:6619-6623.
    • (2000) Eur. J. Biochem. , vol.267 , pp. 6619-6623
    • Shima, S.1    Thauer, R.K.2    Ermler, U.3    Durchschlag, H.4    Tziatzios, C.5    Shubert, D.6
  • 39
    • 0043092112 scopus 로고    scopus 로고
    • Characterization of a novel Ser-cisSer-Lys catalytic triad in comparison with the classical Ser-His-Asp triad
    • Shin, S., Y.S. Yun, H.M. Koo, Y.S. Kim, K.Y. Choi and B.H. Oh. 2003. Characterization of a novel Ser-cisSer-Lys catalytic triad in comparison with the classical Ser-His-Asp triad. J. Biol. Chem. 278:24937-24943.
    • (2003) J. Biol. Chem. , vol.278 , pp. 24937-24943
    • Shin, S.1    Yun, Y.S.2    Koo, H.M.3    Kim, Y.S.4    Choi, K.Y.5    Oh, B.H.6
  • 40
    • 0032539795 scopus 로고    scopus 로고
    • The crystal structure of Pyrococcus furiosus ornithine carbamoyltransferase reveals a key role for oligomerization in enzyme stability at extremely high temperatures
    • USA
    • Villeret, V., B. Clantin, C. Tricot, C. Legrain, M. Roovers, V. Stalon, N. Glansdorff and J. Van Beeumen. 1998. The crystal structure of Pyrococcus furiosus ornithine carbamoyltransferase reveals a key role for oligomerization in enzyme stability at extremely high temperatures. Proc. Natl. Acad. Sci. USA 95:2801-2806.
    • (1998) Proc. Natl. Acad. Sci. , vol.95 , pp. 2801-2806
    • Villeret, V.1    Clantin, B.2    Tricot, C.3    Legrain, C.4    Roovers, M.5    Stalon, V.6    Glansdorff, N.7    Van Beeumen, J.8
  • 41
    • 0035919731 scopus 로고    scopus 로고
    • Crystal structure of native an Cd/Cd-substituted Dioclea guaianensis seed lectin. A novel manganese-binding site and structural basis of dimer-tetramer association
    • Wah, D.A., A. Romero, F. Gallego del Sol, B.S. Cavad, M.V. Ramos, T.B. Grangeirp, A.H. Sampaio and J.J. Calvete. 2001. Crystal structure of native an Cd/Cd-substituted Dioclea guaianensis seed lectin. A novel manganese-binding site and structural basis of dimer-tetramer association. J. Mol. Biol. 310:885-894.
    • (2001) J. Mol. Biol. , vol.310 , pp. 885-894
    • Wah, D.A.1    Romero, A.2    Gallego Del Sol, F.3    Cavad, B.S.4    Ramos, M.V.5    Grangeirp, T.B.6    Sampaio, A.H.7    Calvete, J.J.8
  • 42
    • 0345589295 scopus 로고
    • Proteins in essential nonaqueous environments
    • Ed. R.B. Gregory. Marcel Dekker, New York
    • Williams, D.L Jr., I. Rapanovich and A. Russel. 1995. Proteins in essential nonaqueous environments. In Protein-Solvent Interactions. Ed. R.B. Gregory. Marcel Dekker, New York, pp 327-341.
    • (1995) Protein-Solvent Interactions , pp. 327-341
    • Williams Jr., D.L.1    Rapanovich, I.2    Russel, A.3
  • 43
    • 0038678628 scopus 로고    scopus 로고
    • Membrane fusion activity of vesicular stomatitis virus glycoprotein G is induced by low pH but not by heat or denaturant
    • Yao, Y., K. Ghosh, R.F. Epand, R.M. Epand and H.P. Ghosh. 2003. Membrane fusion activity of vesicular stomatitis virus glycoprotein G is induced by low pH but not by heat or denaturant. Virology 310:319-332.
    • (2003) Virology , vol.310 , pp. 319-332
    • Yao, Y.1    Ghosh, K.2    Epand, R.F.3    Epand, R.M.4    Ghosh, H.P.5
  • 44
    • 0030769231 scopus 로고    scopus 로고
    • Oligomerization properties of GCN4 leucine zipper e and g position mutants
    • Zeng, X., H. Zhu, H.A. Lashuel, J.C. Hu. 1997. Oligomerization properties of GCN4 leucine zipper e and g position mutants. Protein Sci. 6:2218-2226.
    • (1997) Protein Sci. , vol.6 , pp. 2218-2226
    • Zeng, X.1    Zhu, H.2    Lashuel, H.A.3    Hu, J.C.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.