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Volumn 71, Issue 1, 2008, Pages 476-484

Structural basis for the cold adaptation of psychrophilic M37 lipase from Photobacterium lipolyticum

Author keywords

Cavity; Cold adaptation; M37 lipase; Oxyanion hole; Rhizomucor miehei lipase (RML)

Indexed keywords

TRIACYLGLYCEROL LIPASE;

EID: 40549102244     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1002/prot.21884     Document Type: Article
Times cited : (38)

References (29)
  • 2
    • 0032717591 scopus 로고    scopus 로고
    • Bacterial biochatalysts: Molecular biology, three dimensional structures, and biotechnological applications of lipases
    • Jaeger KE, Dijkstra BW, Reetz MT. Bacterial biochatalysts: molecular biology, three dimensional structures, and biotechnological applications of lipases. Annu Rev Microbiol 1999;53:315-351.
    • (1999) Annu Rev Microbiol , vol.53 , pp. 315-351
    • Jaeger, K.E.1    Dijkstra, B.W.2    Reetz, M.T.3
  • 3
    • 3142773489 scopus 로고    scopus 로고
    • Bacterial lipases: An overview of production, purification and biochemical properties
    • Gupta R, Gupta N, Rathi P. Bacterial lipases: an overview of production, purification and biochemical properties. Appl Microbiol Biotechnol 2004;64:763-781.
    • (2004) Appl Microbiol Biotechnol , vol.64 , pp. 763-781
    • Gupta, R.1    Gupta, N.2    Rathi, P.3
  • 7
    • 13244251295 scopus 로고    scopus 로고
    • Photobacterium lipolyticum sp. nov., a bacterium with lipolytic activity isolated from the Yellow Sea in Korea
    • Yoon JH, Lee JK, Kim YO, Oh TK. Photobacterium lipolyticum sp. nov., a bacterium with lipolytic activity isolated from the Yellow Sea in Korea. Int J Syst Evol Microbiol 2005;55:335-339.
    • (2005) Int J Syst Evol Microbiol , vol.55 , pp. 335-339
    • Yoon, J.H.1    Lee, J.K.2    Kim, Y.O.3    Oh, T.K.4
  • 8
    • 33644750581 scopus 로고    scopus 로고
    • New cold-adapted lipase from Photobacterium lipolyticum sp. nov. that is closely related to filamentous fungal lipases
    • Ryu HS, Kim HK, Choi WC, Kim MH, Park SY, Han NS, Oh TK, Lee JK. New cold-adapted lipase from Photobacterium lipolyticum sp. nov. that is closely related to filamentous fungal lipases. Appl Microbiol Biotechnol 2006;70:321-326.
    • (2006) Appl Microbiol Biotechnol , vol.70 , pp. 321-326
    • Ryu, H.S.1    Kim, H.K.2    Choi, W.C.3    Kim, M.H.4    Park, S.Y.5    Han, N.S.6    Oh, T.K.7    Lee, J.K.8
  • 9
    • 0031889267 scopus 로고    scopus 로고
    • A cold-adapted lipase of an Alaskan psychrotroph, Pseudomonas sp. strain B11-1: Gene cloning and enzyme purification and characterization
    • Choo DW, Kurihara T, Susuki T, Soda K, Esaki N. A cold-adapted lipase of an Alaskan psychrotroph, Pseudomonas sp. strain B11-1: gene cloning and enzyme purification and characterization. Appl Env Microbiol 1998;64:486-491.
    • (1998) Appl Env Microbiol , vol.64 , pp. 486-491
    • Choo, D.W.1    Kurihara, T.2    Susuki, T.3    Soda, K.4    Esaki, N.5
  • 11
    • 0034170458 scopus 로고    scopus 로고
    • Toward a molecular understanding of cold activity of enzymes from psychrophiles
    • Russell NJ. Toward a molecular understanding of cold activity of enzymes from psychrophiles. Extremophiles 2000;4:83-90.
    • (2000) Extremophiles , vol.4 , pp. 83-90
    • Russell, N.J.1
  • 12
    • 0032784276 scopus 로고    scopus 로고
    • α/β hydrolase fold enzymes: The family keeps growing
    • Nardini M, Dijkstra BW. α/β hydrolase fold enzymes: the family keeps growing. Curr Opin Struct Biol 1999;9:732-737.
    • (1999) Curr Opin Struct Biol , vol.9 , pp. 732-737
    • Nardini, M.1    Dijkstra, B.W.2
  • 13
    • 0033212815 scopus 로고    scopus 로고
    • Integration of macromolecular diffraction data
    • Leslie AG. Integration of macromolecular diffraction data. Acta Crystallogr D 1999;55:1696-1702.
    • (1999) Acta Crystallogr D , vol.55 , pp. 1696-1702
    • Leslie, A.G.1
  • 14
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography. Acta Crystallogr D
    • 4
    • CCP4. The CCP4 suite: programs for protein crystallography. Acta Crystallogr D 1994;50:760-763.
    • (1994) , vol.50 , pp. 760-763
    • CCP1
  • 16
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones TA, Zou J-Y, Cowan SW, Kjeldgaard M. Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr A 1991;47:110-119.
    • (1991) Acta Crystallogr A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.-Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 18
    • 0027995683 scopus 로고
    • Detection, delineation, measurement and display of cavities in macromolecular structures
    • Kleywegt GJ, Jones TA. Detection, delineation, measurement and display of cavities in macromolecular structures. Acta Crystallogr D 1994;50:178-185.
    • (1994) Acta Crystallogr D , vol.50 , pp. 178-185
    • Kleywegt, G.J.1    Jones, T.A.2
  • 20
    • 0030815133 scopus 로고    scopus 로고
    • Raster3D: Photorealistic molecular graphics
    • Meritt EA, Bacon DJ. Raster3D: photorealistic molecular graphics. Methods Enzymol 1997;277:505-524.
    • (1997) Methods Enzymol , vol.277 , pp. 505-524
    • Meritt, E.A.1    Bacon, D.J.2
  • 21
    • 0027412196 scopus 로고
    • ALSCRIPT: A tool to format multiple sequence alignments
    • Baton GJ. ALSCRIPT: a tool to format multiple sequence alignments. Protein Eng 1993;6:37-40.
    • (1993) Protein Eng , vol.6 , pp. 37-40
    • Baton, G.J.1
  • 22
    • 0030729838 scopus 로고    scopus 로고
    • An extensively modified version of MolScript that includes greatly enhanced coloring capabilities
    • Esnouf RM. An extensively modified version of MolScript that includes greatly enhanced coloring capabilities. J Mol Graph Model 1997;15:112-134.
    • (1997) J Mol Graph Model , vol.15 , pp. 112-134
    • Esnouf, R.M.1
  • 23
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis P. MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J Appl Crystallogr 1991;24:946-950.
    • (1991) J Appl Crystallogr , vol.24 , pp. 946-950
    • Kraulis, P.1
  • 24
  • 25
    • 0027440362 scopus 로고
    • Protein structure comparison by alignment of distance matrices
    • Holm L, Sander C. Protein structure comparison by alignment of distance matrices. J Mol Biol 1993;233:123-138.
    • (1993) J Mol Biol , vol.233 , pp. 123-138
    • Holm, L.1    Sander, C.2
  • 26
    • 0026786234 scopus 로고
    • The crystal and molecular structure of the Rhizomucor miehei triacylglyceride lipase at 1.9 Å resolution
    • Derewenda ZS, Derewenda U. The crystal and molecular structure of the Rhizomucor miehei triacylglyceride lipase at 1.9 Å resolution. J Mol Biol 1992;227:818-839.
    • (1992) J Mol Biol , vol.227 , pp. 818-839
    • Derewenda, Z.S.1    Derewenda, U.2
  • 28
    • 0026550733 scopus 로고
    • Catalysis at the interface: The anatomy of a conformational change in a triglyceride lipase
    • Derewenda U, Brzozowski AM, Lawson DM, Drewenda ZS. Catalysis at the interface: the anatomy of a conformational change in a triglyceride lipase. Biochemistry 1992;31:1532-1541.
    • (1992) Biochemistry , vol.31 , pp. 1532-1541
    • Derewenda, U.1    Brzozowski, A.M.2    Lawson, D.M.3    Drewenda, Z.S.4
  • 29
    • 0029124153 scopus 로고
    • Acid and thermal denaturation of Barnase investigated by molecular dynamics simulations
    • Caflisch A, Kaplus M. Acid and thermal denaturation of Barnase investigated by molecular dynamics simulations. J Mol Biol 1995;252:672-708.
    • (1995) J Mol Biol , vol.252 , pp. 672-708
    • Caflisch, A.1    Kaplus, M.2


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