메뉴 건너뛰기




Volumn 46, Issue 31, 2007, Pages 8969-8979

Structure of a novel enzyme that catalyzes acyl transfer to alcohols in aqueous conditions

Author keywords

[No Author keywords available]

Indexed keywords

ALCOHOLS; CATALYST ACTIVITY; CRYSTAL STRUCTURE; HYDROLYSIS; SOLUTIONS;

EID: 34547762614     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi7002444     Document Type: Article
Times cited : (94)

References (25)
  • 1
    • 34547782516 scopus 로고
    • Lipase and its action. The synthetic action of pancreatic lipase in the system: Oleic acid-glycerol-water-dissolved lipase
    • Sym, E. A. (1930) Lipase and its action. The synthetic action of pancreatic lipase in the system: oleic acid-glycerol-water-dissolved lipase, Biochem J. 24, 1265-1281.
    • (1930) Biochem J , vol.24 , pp. 1265-1281
    • Sym, E.A.1
  • 2
    • 0000321692 scopus 로고
    • Enzyme-catalyzed processes in organic solvents
    • Zaks, A., and Klibanov, A. M. (1985) Enzyme-catalyzed processes in organic solvents, Proc. Natl. Acad. Sci. U.S.A., 82, 3192-3196.
    • (1985) Proc. Natl. Acad. Sci. U.S.A , vol.82 , pp. 3192-3196
    • Zaks, A.1    Klibanov, A.M.2
  • 3
    • 0035843166 scopus 로고    scopus 로고
    • Improving enzymes by using them in organic solvents
    • Klibanov, A. M. (2001) Improving enzymes by using them in organic solvents, Nature 409, 241-246.
    • (2001) Nature , vol.409 , pp. 241-246
    • Klibanov, A.M.1
  • 4
    • 34547759020 scopus 로고    scopus 로고
    • Amin, N. S., Boston, M. G., Bott, R. R., Cervin, M. A., Concar, E. M., Gustwiller, M. E., Jones, B. E., Liebeton, K., Miracle, G., Oh, H., Poulose, A. J., Ramer, S. W., Scheibel, J. J., Weyler, W., and Whited, G. M. (2005) Perhydrolyase, WO2005056782.
    • Amin, N. S., Boston, M. G., Bott, R. R., Cervin, M. A., Concar, E. M., Gustwiller, M. E., Jones, B. E., Liebeton, K., Miracle, G., Oh, H., Poulose, A. J., Ramer, S. W., Scheibel, J. J., Weyler, W., and Whited, G. M. (2005) Perhydrolyase, WO2005056782.
  • 5
    • 0023151506 scopus 로고
    • p-Nitrophenyl and cholesteryl-N-alkyl carbamates as inhibitors of cholesterol esterase
    • Hosie, L., Sutton, L. D., and Quinn, D. M. (1987) p-Nitrophenyl and cholesteryl-N-alkyl carbamates as inhibitors of cholesterol esterase, J. Biol. Chem. 262, 260-264.
    • (1987) J. Biol. Chem , vol.262 , pp. 260-264
    • Hosie, L.1    Sutton, L.D.2    Quinn, D.M.3
  • 6
    • 34547767855 scopus 로고    scopus 로고
    • Pettrone, F, Whited, G, and Goodhue, C, 1992 Methods for preparing acetate esters of diols and polyols using Corynebacterium oxydans in substantially aqueous media, U.S. Patent No. 5,-114,850
    • Pettrone, F., Whited, G., and Goodhue, C. (1992) Methods for preparing acetate esters of diols and polyols using Corynebacterium oxydans in substantially aqueous media, U.S. Patent No. 5,-114,850.
  • 8
    • 0033212815 scopus 로고    scopus 로고
    • Integration of macromolecular diffraction data
    • Leslie, A. G. W. (1999) Integration of macromolecular diffraction data, Acta Crystallogr. D55, 1696-1702.
    • (1999) Acta Crystallogr , vol.D55 , pp. 1696-1702
    • Leslie, A.G.W.1
  • 9
    • 0028103275 scopus 로고    scopus 로고
    • Collaborative Computational Project, Number 4 (1994) The CCP4 suite: programs for protein crystallography, Acta Crystallogr. D50, 760-763.
    • Collaborative Computational Project, Number 4 (1994) The CCP4 suite: programs for protein crystallography, Acta Crystallogr. D50, 760-763.
  • 10
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski, Z., and Minor, W. (1997) Processing of X-ray diffraction data collected in oscillation mode, Methods Enzymol. 276, 307-326.
    • (1997) Methods Enzymol , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 11
    • 0033119895 scopus 로고    scopus 로고
    • Automated structure solution for MIR and MAD
    • Terwilliger, T. C., and Berendzen, J. (1999) Automated structure solution for MIR and MAD, Acta Crystallogr. D55, 849-861.
    • (1999) Acta Crystallogr , vol.D55 , pp. 849-861
    • Terwilliger, T.C.1    Berendzen, J.2
  • 12
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones, T. A., Zou, J. Y., Cowtan, S. W., and Kjeldgaard, M. (1991) Improved methods for building protein models in electron density maps and the location of errors in these models, Acta Crystallogr. A47, 110-119.
    • (1991) Acta Crystallogr , vol.A47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowtan, S.W.3    Kjeldgaard, M.4
  • 13
    • 0001513485 scopus 로고
    • PROCHECK: A program to check the stereochemical quality of protein structures
    • Laskowski, R., MacArthur, M., Moss, D., and Thornton, J. (1993) PROCHECK: a program to check the stereochemical quality of protein structures, J. Appl. Crystallogr. 26, 91-97.
    • (1993) J. Appl. Crystallogr , vol.26 , pp. 91-97
    • Laskowski, R.1    MacArthur, M.2    Moss, D.3    Thornton, J.4
  • 14
  • 16
    • 0028871926 scopus 로고
    • A network tool for protein structure comparisons
    • Holm, L., and Sander, C. D. (1995) A network tool for protein structure comparisons, Trends Biochem. Sci. 29, 478-480.
    • (1995) Trends Biochem. Sci , vol.29 , pp. 478-480
    • Holm, L.1    Sander, C.D.2
  • 17
    • 0038723702 scopus 로고    scopus 로고
    • Crystal structure of Escherichia coli thioesterase I/protease I/lysophospholipase L1: Consensus sequence blocks constitute the catalytic center of SGNH hydrolases through a conserved hydrogen bond network
    • Lo, Y. C., Lin, S. C., Shaw, J. F., and Liaw, Y. C. (2003) Crystal structure of Escherichia coli thioesterase I/protease I/lysophospholipase L1: Consensus sequence blocks constitute the catalytic center of SGNH hydrolases through a conserved hydrogen bond network, J. Mol. Biol. 330, 539-551.
    • (2003) J. Mol. Biol , vol.330 , pp. 539-551
    • Lo, Y.C.1    Lin, S.C.2    Shaw, J.F.3    Liaw, Y.C.4
  • 18
    • 0034655985 scopus 로고    scopus 로고
    • Rhamnogalacturonan acetylesterase elucidates the structure and function of a new family of hydrolases
    • Molgaard, A., Kauppinen, S., and Larsen, S. (2000) Rhamnogalacturonan acetylesterase elucidates the structure and function of a new family of hydrolases, Structure 8, 373-383.
    • (2000) Structure , vol.8 , pp. 373-383
    • Molgaard, A.1    Kauppinen, S.2    Larsen, S.3
  • 19
    • 0030864850 scopus 로고    scopus 로고
    • Three Neocallimastix patriciarum esterase associated with the degradation of complex polysaccharides are members of a new family of hydrolases
    • Dalrymple, B. P., Cybinski, D. H., Layton, I., McSweeney, C. S., Xue, G. P., Swadling, Y. J., and Lowry, J. B. (1997) Three Neocallimastix patriciarum esterase associated with the degradation of complex polysaccharides are members of a new family of hydrolases, Microbiology 143, 2605-2614.
    • (1997) Microbiology , vol.143 , pp. 2605-2614
    • Dalrymple, B.P.1    Cybinski, D.H.2    Layton, I.3    McSweeney, C.S.4    Xue, G.P.5    Swadling, Y.J.6    Lowry, J.B.7
  • 20
    • 0031906549 scopus 로고    scopus 로고
    • A novel arylesterase active toward 7-aminocephalosporanic acid from Agrobacterium radiobacter IFO 12607: Purification and characterization
    • Sakai, Y., Ayukawa, K., Yurimoto, H., Yamamoto, K., and Kato, N. (1998) A novel arylesterase active toward 7-aminocephalosporanic acid from Agrobacterium radiobacter IFO 12607: Purification and characterization, J. Ferment. Bioeng. 85, 58-62.
    • (1998) J. Ferment. Bioeng , vol.85 , pp. 58-62
    • Sakai, Y.1    Ayukawa, K.2    Yurimoto, H.3    Yamamoto, K.4    Kato, N.5
  • 21
    • 0031957627 scopus 로고    scopus 로고
    • A novel arylesterase active toward 7-aminocephalosporanic acid from Agrobacterium radiobacter IFO 12607: Nucleotide sequence, gene expression in Escherichia coli, and site-directed mutagenesis
    • Sakai, Y., Ayukawa, K., Yurimoto, H., Yamamoto, K, and Kato, N. (1998) A novel arylesterase active toward 7-aminocephalosporanic acid from Agrobacterium radiobacter IFO 12607: Nucleotide sequence, gene expression in Escherichia coli, and site-directed mutagenesis, J. Ferment. Bioeng. 85, 1389-143.
    • (1998) J. Ferment. Bioeng , vol.85 , pp. 1389-1143
    • Sakai, Y.1    Ayukawa, K.2    Yurimoto, H.3    Yamamoto, K.4    Kato, N.5
  • 23
    • 0032784276 scopus 로고    scopus 로고
    • α/β hydrolase fold enzymes: The family keeps growing
    • Nardini, M., and Dijkstra, B. W. (1999) α/β hydrolase fold enzymes: the family keeps growing, Curr. Opin. Struct. Biol. 9, 732-737.
    • (1999) Curr. Opin. Struct. Biol , vol.9 , pp. 732-737
    • Nardini, M.1    Dijkstra, B.W.2
  • 24
    • 0030874881 scopus 로고    scopus 로고
    • Lipases and α/β hydrolase fold
    • Schrag, J. D., and Cygler, M. (1997) Lipases and α/β hydrolase fold, Methods Enzymol. 284, 85-107.
    • (1997) Methods Enzymol , vol.284 , pp. 85-107
    • Schrag, J.D.1    Cygler, M.2
  • 25
    • 34547790539 scopus 로고    scopus 로고
    • DeLano Scientific LLC, Palo Alto, CA
    • DeLano, W. L. (2006) The PyMOL molecular graphics system, DeLano Scientific LLC, Palo Alto, CA (http://www.pymol.sourceforge.net/).
    • (2006)
    • DeLano, W.L.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.