메뉴 건너뛰기




Volumn 2008, Issue 3, 2008, Pages 9-19

Understanding structural features of microbial lipases - An overview

Author keywords

Active site; Bioinformatics; Candida rugosa lipase; Crystallization; Lipase structure; Structure prediction

Indexed keywords


EID: 41949112320     PISSN: None     EISSN: 11773901     Source Type: Journal    
DOI: None     Document Type: Review
Times cited : (42)

References (79)
  • 1
    • 0025723985 scopus 로고
    • Systematic use of the incomplete factorial approach in the design of protein crystallization experiments
    • Abergel, C., Moulard, M., Moreau, H. et al. 1991. Systematic use of the incomplete factorial approach in the design of protein crystallization experiments. J. Biol. Chem., 266:20131-8.
    • (1991) J. Biol. Chem , vol.266 , pp. 20131-20138
    • Abergel, C.1    Moulard, M.2    Moreau, H.3
  • 2
    • 7444229762 scopus 로고    scopus 로고
    • GSDL family of serine esterases/lipases
    • Akoh, C.C., Lee, G.C., Liaw, Y.C. et al. 2004. GSDL family of serine esterases/lipases. Prog. Lipid Res., 43:534-52.
    • (2004) Prog. Lipid Res , vol.43 , pp. 534-552
    • Akoh, C.C.1    Lee, G.C.2    Liaw, Y.C.3
  • 4
    • 24044478793 scopus 로고    scopus 로고
    • Importance of a repetitive nine residue sequence motif for intracellular stability and functional structure of a family 1.3 lipase
    • Angkawidjaja, C., Paul, A., Koga, Y. et al. 2005. Importance of a repetitive nine residue sequence motif for intracellular stability and functional structure of a family 1.3 lipase. FEBS Lett., 579:4707-12.
    • (2005) FEBS Lett , vol.579 , pp. 4707-4712
    • Angkawidjaja, C.1    Paul, A.2    Koga, Y.3
  • 5
    • 0034044103 scopus 로고    scopus 로고
    • PROF_PAT 1.3: Updated database of patterns used to detect local similarities
    • Bachinsky, A.G., Frolov, A.S., Naumochkin, A.N. et al. 2000. PROF_PAT 1.3: Updated database of patterns used to detect local similarities. Bioinf., 16:358-66.
    • (2000) Bioinf , vol.16 , pp. 358-366
    • Bachinsky, A.G.1    Frolov, A.S.2    Naumochkin, A.N.3
  • 6
    • 85047685160 scopus 로고    scopus 로고
    • Identification, purification and characterization of a thermally stable lipase from rice bran. A new member of the (phospho) lipase family
    • Bhardwaj, K., Raju, A. and Rajasekharan, R. 2001. Identification, purification and characterization of a thermally stable lipase from rice bran. A new member of the (phospho) lipase family. Plant Physiol., 127:1728-38.
    • (2001) Plant Physiol , vol.127 , pp. 1728-1738
    • Bhardwaj, K.1    Raju, A.2    Rajasekharan, R.3
  • 7
    • 33646192301 scopus 로고    scopus 로고
    • Structural bioinformatics prediction of membrane-binding proteins
    • Bhardwaj, N., Stahelin, R.V., Langlois, R.E. et al. 2006. Structural bioinformatics prediction of membrane-binding proteins. J. Mol. Biol., 359:486-95.
    • (2006) J. Mol. Biol , vol.359 , pp. 486-495
    • Bhardwaj, N.1    Stahelin, R.V.2    Langlois, R.E.3
  • 8
    • 23944483387 scopus 로고    scopus 로고
    • Purification and preliminary crystallographic analysis of a Pencillium expansum lipase
    • Bian, C., Yuan, C., Lin, L. et al. 2005. Purification and preliminary crystallographic analysis of a Pencillium expansum lipase. Biochim. Biophys. Acta., 1752:99-102.
    • (2005) Biochim. Biophys. Acta , vol.1752 , pp. 99-102
    • Bian, C.1    Yuan, C.2    Lin, L.3
  • 10
    • 0025057072 scopus 로고
    • A serine protease triad forms the catalytic centre of a triglyceride lipase
    • Brady, L., Brzozowski, A.M., Derewenda, Z.S. et al. 1990. A serine protease triad forms the catalytic centre of a triglyceride lipase. Nature, 343:767-70.
    • (1990) Nature , vol.343 , pp. 767-770
    • Brady, L.1    Brzozowski, A.M.2    Derewenda, Z.S.3
  • 11
    • 0026418174 scopus 로고
    • A model for interfacial activation in lipases from the structure of a fungal lipase-inhibitor complex
    • Brzozowski, A.M., Derewenda, U., Derewenda, Z.S. et al. 1991. A model for interfacial activation in lipases from the structure of a fungal lipase-inhibitor complex. Nature., 351:491-4.
    • (1991) Nature , vol.351 , pp. 491-494
    • Brzozowski, A.M.1    Derewenda, U.2    Derewenda, Z.S.3
  • 12
    • 0028078789 scopus 로고
    • Cloning of the classical guinea pig pancreatic lipase and comparison with the lipase related protein 2
    • Carriere, F., Thirstrup, K., Hjorth, S. et al. 1994. Cloning of the classical guinea pig pancreatic lipase and comparison with the lipase related protein 2. FEBS Lett., 388:63-8.
    • (1994) FEBS Lett , vol.388 , pp. 63-68
    • Carriere, F.1    Thirstrup, K.2    Hjorth, S.3
  • 13
    • 0032701223 scopus 로고    scopus 로고
    • Structure and conformational flexibility of Candida rugosa lipase
    • Cygler, M. and Schrag, J.D. 1999. Structure and conformational flexibility of Candida rugosa lipase. Biochim. Biophys. Acta., 1441:205-14.
    • (1999) Biochim. Biophys. Acta , vol.1441 , pp. 205-214
    • Cygler, M.1    Schrag, J.D.2
  • 15
    • 0035937542 scopus 로고    scopus 로고
    • Glycoprotein structure determination by Mass spectrometry
    • Dell, A. and Morris, H.R. 2001. Glycoprotein structure determination by Mass spectrometry. Science., 291:2351-6.
    • (2001) Science , vol.291 , pp. 2351-2356
    • Dell, A.1    Morris, H.R.2
  • 16
    • 0026550733 scopus 로고
    • Catalysis at the interface: The anatomy of a conformational change in a triglyceride lipase
    • Derewenda, U., Brzozowski, A.M., Lawson, D.M. et al. 1992. Catalysis at the interface: the anatomy of a conformational change in a triglyceride lipase. Biochem., 31:1532-41.
    • (1992) Biochem , vol.31 , pp. 1532-1541
    • Derewenda, U.1    Brzozowski, A.M.2    Lawson, D.M.3
  • 17
    • 0026786234 scopus 로고
    • The crystal and molecular structure of the Rhizomucor miehei triacylglyceride lipase at 1.9 Å resolution
    • Derewenda, Z.S., Derewenda, U. and Dodson, G.G. 1992. The crystal and molecular structure of the Rhizomucor miehei triacylglyceride lipase at 1.9 Å resolution. J. Mol. Biol., 227:818-39.
    • (1992) J. Mol. Biol , vol.227 , pp. 818-839
    • Derewenda, Z.S.1    Derewenda, U.2    Dodson, G.G.3
  • 18
    • 0025321633 scopus 로고
    • Studies of crystal growth mechanisms of proteins by electron microscopy
    • Durbin, S.D. and Feher, G. 1990. Studies of crystal growth mechanisms of proteins by electron microscopy. J. Mol. Biol., 212:763-74.
    • (1990) J. Mol. Biol , vol.212 , pp. 763-774
    • Durbin, S.D.1    Feher, G.2
  • 19
    • 0036071674 scopus 로고    scopus 로고
    • Biochemical properties and three-dimensional structures of two extracellular lipolytic enzymes from Bacillus subtilis
    • Eggert, T., van Pouderoyen, G., Pencreac'h, G. et al. 2002. Biochemical properties and three-dimensional structures of two extracellular lipolytic enzymes from Bacillus subtilis. Coll. Surf. B: Biointerf., 26:37-46.
    • (2002) Coll. Surf. B: Biointerf , vol.26 , pp. 37-46
    • Eggert, T.1    van Pouderoyen, G.2    Pencreac'h, G.3
  • 20
    • 0033653715 scopus 로고    scopus 로고
    • What distinguishes an esterase from a lipase: A novel structural approach
    • Fojan, P., Jonson, P.H., Peterson, M.T.N. et al. 2000. What distinguishes an esterase from a lipase: A novel structural approach. Biochimie., 82:1033-41.
    • (2000) Biochimie , vol.82 , pp. 1033-1041
    • Fojan, P.1    Jonson, P.H.2    Peterson, M.T.N.3
  • 21
    • 0032436341 scopus 로고    scopus 로고
    • DOMO: A new database of aligned protein domains
    • Gracy, J. and Argos, P. 1998. DOMO: a new database of aligned protein domains. TIBS, 23:495-7.
    • (1998) TIBS , vol.23 , pp. 495-497
    • Gracy, J.1    Argos, P.2
  • 22
    • 0027160452 scopus 로고
    • Insights into interfacial activation from an open structure of Candida rugosa lipase
    • Grochulski, P., Li, Y., Schrag, J.D. et al. 1993. Insights into interfacial activation from an open structure of Candida rugosa lipase. J. Biol. Chem., 268:12843-7.
    • (1993) J. Biol. Chem , vol.268 , pp. 12843-12847
    • Grochulski, P.1    Li, Y.2    Schrag, J.D.3
  • 23
    • 0032818805 scopus 로고    scopus 로고
    • FTIR. spectroscopic characterization of protein structure in aqueous and non-aqueous media
    • Haris, P.I. and Severcan, F. 1999. FTIR. spectroscopic characterization of protein structure in aqueous and non-aqueous media. J. Mol. Catal. B: Enz., 7:207-21.
    • (1999) J. Mol. Catal. B: Enz , vol.7 , pp. 207-221
    • Haris, P.I.1    Severcan, F.2
  • 24
    • 33747518326 scopus 로고    scopus 로고
    • Industrial applications of microbial lipases
    • Hasan, F., Shah, A.A. and Hameed, A. 2006. Industrial applications of microbial lipases. Enz. Microb. Technol., 39:235-51.
    • (2006) Enz. Microb. Technol , vol.39 , pp. 235-251
    • Hasan, F.1    Shah, A.A.2    Hameed, A.3
  • 25
    • 3242710304 scopus 로고    scopus 로고
    • Low microwave-amplitude ESR. spectroscopy: Measuring spin - relaxation interactions of moderately immobilized spin labels in proteins
    • Hedin, E.M.K., Hult, K., Mouritsen, O.G. et al. 2004. Low microwave-amplitude ESR. spectroscopy: Measuring spin - relaxation interactions of moderately immobilized spin labels in proteins. J. Biochem. Biophys. Methods, 60:117-38.
    • (2004) J. Biochem. Biophys. Methods , vol.60 , pp. 117-138
    • Hedin, E.M.K.1    Hult, K.2    Mouritsen, O.G.3
  • 26
    • 0030297503 scopus 로고    scopus 로고
    • Connecting protein family resources using the proweb network
    • Henikoff, S., Endow, S.A. and Greene, E.A. 1996. Connecting protein family resources using the proweb network. TIBS, 21:444-5.
    • (1996) TIBS , vol.21 , pp. 444-445
    • Henikoff, S.1    Endow, S.A.2    Greene, E.A.3
  • 27
    • 0342547002 scopus 로고    scopus 로고
    • Computer-aided modeling of stereoselective triglyceride hydrolysis catalysed by Rhizopus oryzae lipase
    • Holzwarth, H.C., Pleiss, J. and Schmid, R.D. 1997. Computer-aided modeling of stereoselective triglyceride hydrolysis catalysed by Rhizopus oryzae lipase. J. Mol. Catal. B., 3:73-82.
    • (1997) J. Mol. Catal. B , vol.3 , pp. 73-82
    • Holzwarth, H.C.1    Pleiss, J.2    Schmid, R.D.3
  • 28
    • 0027523292 scopus 로고
    • Primary structure determination of mono- and diacylglycerol lipase from Pencillium camembertii
    • Isobe, K. and Nokihara, K. 1993. Primary structure determination of mono- and diacylglycerol lipase from Pencillium camembertii. FEBS Lett., 320:101-6.
    • (1993) FEBS Lett , vol.320 , pp. 101-106
    • Isobe, K.1    Nokihara, K.2
  • 29
    • 0032549475 scopus 로고    scopus 로고
    • Nucleation and growth of microbial lipase crystals from clarified concentrated fermentation broths
    • Jacobsen, C., Garside, J. and Hoare, M. 1998. Nucleation and growth of microbial lipase crystals from clarified concentrated fermentation broths. Biotechnol. Bioeng., 57:666-75.
    • (1998) Biotechnol. Bioeng , vol.57 , pp. 666-675
    • Jacobsen, C.1    Garside, J.2    Hoare, M.3
  • 30
    • 0027359783 scopus 로고
    • Topological characterization and modeling of the 3D structure of lipase from Pseudomonas aeruginosa
    • Jaeger, K.E., Ransac, S., Koch, H.B. et al. 1993. Topological characterization and modeling of the 3D structure of lipase from Pseudomonas aeruginosa. FEBS Lett., 232:143-9.
    • (1993) FEBS Lett , vol.232 , pp. 143-149
    • Jaeger, K.E.1    Ransac, S.2    Koch, H.B.3
  • 31
    • 0037171119 scopus 로고    scopus 로고
    • High-resolution nuclear magnetic resonance studies of proteins
    • Jonas, J. 2002. High-resolution nuclear magnetic resonance studies of proteins. Biochim. Biophys. Acta., 1595:145-59.
    • (2002) Biochim. Biophys. Acta , vol.1595 , pp. 145-159
    • Jonas, J.1
  • 32
    • 5444266206 scopus 로고    scopus 로고
    • Fluorescence spectroscopic characterization of Humicola lanuginose lipase dissolved in its substrate
    • Jutila, A., Zhu, K., Tuominen, E.K.J. et al. 2004. Fluorescence spectroscopic characterization of Humicola lanuginose lipase dissolved in its substrate. Biochim. Biophys. Acta., 1702:181-9.
    • (2004) Biochim. Biophys. Acta , vol.1702 , pp. 181-189
    • Jutila, A.1    Zhu, K.2    Tuominen, E.K.J.3
  • 33
    • 33646496383 scopus 로고    scopus 로고
    • Analysis of disulfide bond connectivity patterns in protein tertiary structure
    • Kartik, V.J., Lavanya, T. and Guruprasad, K. 2006. Analysis of disulfide bond connectivity patterns in protein tertiary structure. Int.J. Biol. Macromol., 38:174-9.
    • (2006) Int.J. Biol. Macromol , vol.38 , pp. 174-179
    • Kartik, V.J.1    Lavanya, T.2    Guruprasad, K.3
  • 34
    • 0033963834 scopus 로고    scopus 로고
    • Molecular modeling and biocatalysis: Explanations, predictions, limitations, and opportunities
    • Kazlauskas, R.J. 2000. Molecular modeling and biocatalysis: explanations, predictions, limitations, and opportunities. Curr. Opin. Chem. Biol., 4:81-8.
    • (2000) Curr. Opin. Chem. Biol , vol.4 , pp. 81-88
    • Kazlauskas, R.J.1
  • 35
    • 23444456924 scopus 로고    scopus 로고
    • How to study proteins by circular dichroism
    • Kelly, S.M., Jess, T.J. and Price, N.C. 2005. How to study proteins by circular dichroism. Biochim. Biophys. Acta., 1751:119-39.
    • (2005) Biochim. Biophys. Acta , vol.1751 , pp. 119-139
    • Kelly, S.M.1    Jess, T.J.2    Price, N.C.3
  • 36
    • 29144455258 scopus 로고    scopus 로고
    • Infrared spectroscopy used to evaluate glycosylation of proteins
    • Khajehpour, M., Dashnau J.L. and Vanderkooi, J.M., 2006. Infrared spectroscopy used to evaluate glycosylation of proteins. Anal. Biochem., 348:40-8.
    • (2006) Anal. Biochem , vol.348 , pp. 40-48
    • Khajehpour, M.1    Dashnau, J.L.2    Vanderkooi, J.M.3
  • 37
    • 0027450397 scopus 로고
    • Preliminary investigation of crystals of lipase I from Rhizopus niveus
    • Kohno, M., Kugimiya, W., Hashimoto, Y. et al. 1993. Preliminary investigation of crystals of lipase I from Rhizopus niveus. J. Mol. Biol., 229:785-6.
    • (1993) J. Mol. Biol , vol.229 , pp. 785-786
    • Kohno, M.1    Kugimiya, W.2    Hashimoto, Y.3
  • 38
    • 0036202210 scopus 로고    scopus 로고
    • Role of repetitive nine - residue sequence motifs in secretion, enzymatic activity and protein conformation of a family 1.3 lipase
    • Kwon, H.J., Haruki, M., Morikawa, M. et al. 2002. Role of repetitive nine - residue sequence motifs in secretion, enzymatic activity and protein conformation of a family 1.3 lipase. J. Biosc. Bioeng., 93:157-64.
    • (2002) J. Biosc. Bioeng , vol.93 , pp. 157-164
    • Kwon, H.J.1    Haruki, M.2    Morikawa, M.3
  • 39
    • 0030659457 scopus 로고    scopus 로고
    • PDBSum: A web based database of summaries and analysis of all PDB. structures
    • Laskowski, R.A., Hutchinson, E.G., Michie, A.D. et al. 1997. PDBSum: a web based database of summaries and analysis of all PDB. structures. TIBS, 22:488-90.
    • (1997) TIBS , vol.22 , pp. 488-490
    • Laskowski, R.A.1    Hutchinson, E.G.2    Michie, A.D.3
  • 40
    • 4644319196 scopus 로고    scopus 로고
    • CD tool - an integrated software package for circular dichroism spectroscopic data processing, analysis, and archiving
    • Lees, J.G., Smith, B.R., Wein, F. et al. 2004. CD tool - an integrated software package for circular dichroism spectroscopic data processing, analysis, and archiving. Anal. Biochem., 332:285-9.
    • (2004) Anal. Biochem , vol.332 , pp. 285-289
    • Lees, J.G.1    Smith, B.R.2    Wein, F.3
  • 41
    • 34547813677 scopus 로고    scopus 로고
    • Selection and characterization of lipase abzyme from phage displayed antibody libraries
    • Leong, M.K., Chen, C., Shar, K.C. et al. 2007. Selection and characterization of lipase abzyme from phage displayed antibody libraries. Biochem. Biaphys. Res. Commun., 361:567-73.
    • (2007) Biochem. Biaphys. Res. Commun , vol.361 , pp. 567-573
    • Leong, M.K.1    Chen, C.2    Shar, K.C.3
  • 42
    • 20444408450 scopus 로고    scopus 로고
    • Characterization of thermostable lipase from thermophilic Geobacillus sp. TW1
    • Li, H. and Zhang, X. 2005. Characterization of thermostable lipase from thermophilic Geobacillus sp. TW1. Protein Expr. Purif., 42:153-9.
    • (2005) Protein Expr. Purif , vol.42 , pp. 153-159
    • Li, H.1    Zhang, X.2
  • 43
    • 0035150139 scopus 로고    scopus 로고
    • Disulphide bond in Pseudomonas aeruginosa lipase stabilizes the structure but is not required for interaction with its foldase
    • Liebeton, K., Zacharias, A. and Jaeger, K.E. 2001. Disulphide bond in Pseudomonas aeruginosa lipase stabilizes the structure but is not required for interaction with its foldase. J. Bacteriol., 183:597-603.
    • (2001) J. Bacteriol , vol.183 , pp. 597-603
    • Liebeton, K.1    Zacharias, A.2    Jaeger, K.E.3
  • 44
    • 85016229161 scopus 로고    scopus 로고
    • Large-scale protein identification using mass spectrometry
    • Lin, D., Tabb, D.L. and Yates III, J.R. 2003. Large-scale protein identification using mass spectrometry. Biochim. Biophys. Acta., 1646:1-10.
    • (2003) Biochim. Biophys. Acta , vol.1646 , pp. 1-10
    • Lin, D.1    Tabb, D.L.2    Yates III, J.R.3
  • 45
    • 0042386531 scopus 로고    scopus 로고
    • Structural insights into the lipase/esterase behavior in the Candida rugosa lipases family: Crystal structure of the lipase2 isoenzyme at 1.97 Å resolution
    • Mancheno, J.M., Pernas, M.A., Martinez, M.J. et al. 2003. Structural insights into the lipase/esterase behavior in the Candida rugosa lipases family: Crystal structure of the lipase2 isoenzyme at 1.97 Å resolution. J. Mol. Biol., 332:1059-69.
    • (2003) J. Mol. Biol , vol.332 , pp. 1059-1069
    • Mancheno, J.M.1    Pernas, M.A.2    Martinez, M.J.3
  • 46
    • 0035663046 scopus 로고    scopus 로고
    • Structural study of lipase modified with fatty acids
    • Maruyama, T., Nakajima, M., Ichikawa, S. et al. 2001. Structural study of lipase modified with fatty acids. Biochem. Eng. J., 9:185-91.
    • (2001) Biochem. Eng. J , vol.9 , pp. 185-191
    • Maruyama, T.1    Nakajima, M.2    Ichikawa, S.3
  • 47
    • 23344444462 scopus 로고    scopus 로고
    • Improved estimation of the secondary structures of proteins by vacuum-ultraviolet circular dichroism spectroscopy
    • Matsuo, K., Yonehara, R. and Gekko, K. 2005. Improved estimation of the secondary structures of proteins by vacuum-ultraviolet circular dichroism spectroscopy. J. Biochem., 138:79-88.
    • (2005) J. Biochem , vol.138 , pp. 79-88
    • Matsuo, K.1    Yonehara, R.2    Gekko, K.3
  • 48
    • 0025272639 scopus 로고
    • Current approaches to macromolecular crystallization
    • McPherson,A. 1990. Current approaches to macromolecular crystallization. Eur. J. Biochem., 189:1-23.
    • (1990) Eur. J. Biochem , vol.189 , pp. 1-23
    • McPherson, A.1
  • 49
    • 0034735624 scopus 로고    scopus 로고
    • A spectroscopic analysis of thermal stability of the Chromobacterium viscosum lipase
    • Melo, E.P., Taipa, M.A., Castellar, M.R. et al. 2000. A spectroscopic analysis of thermal stability of the Chromobacterium viscosum lipase. Biophys. Chem., 87:111-20.
    • (2000) Biophys. Chem , vol.87 , pp. 111-120
    • Melo, E.P.1    Taipa, M.A.2    Castellar, M.R.3
  • 50
    • 17444386712 scopus 로고    scopus 로고
    • Data analysis methods for detection of differential protein expression in two-dimensional gel electrophoresis
    • Meunier, B., Bouley, J., Piec, I. et al. 2005. Data analysis methods for detection of differential protein expression in two-dimensional gel electrophoresis. Anal. Biochem., 340:226-30.
    • (2005) Anal. Biochem , vol.340 , pp. 226-230
    • Meunier, B.1    Bouley, J.2    Piec, I.3
  • 51
    • 14644405513 scopus 로고    scopus 로고
    • Discrimination between closed and open forms of lipases using electrophoretic techniques
    • Miled, N., Riviere, M., Cavalier, J.F. et al. 2005. Discrimination between closed and open forms of lipases using electrophoretic techniques. Anal. Biochem., 338:171-8.
    • (2005) Anal. Biochem , vol.338 , pp. 171-178
    • Miled, N.1    Riviere, M.2    Cavalier, J.F.3
  • 52
    • 0034002145 scopus 로고    scopus 로고
    • A strategy for the identification of site-specific glycosylation in glycoproteins using MALDI TOF MS
    • Mills, K., Johnson, A.W., Diettrich, O. et al. 2000. A strategy for the identification of site-specific glycosylation in glycoproteins using MALDI TOF MS. Tet. Asymm., 11:75-93.
    • (2000) Tet. Asymm , vol.11 , pp. 75-93
    • Mills, K.1    Johnson, A.W.2    Diettrich, O.3
  • 53
    • 0034713846 scopus 로고    scopus 로고
    • Involvement of electrostatic interactions in the mechanism of peptide folding induced by sodium dodecyl sulfate binding
    • Montserret, R., McLeish, M.J., Bockmann, A. et al. 2000. Involvement of electrostatic interactions in the mechanism of peptide folding induced by sodium dodecyl sulfate binding. Biochem., 39:8362-73.
    • (2000) Biochem , vol.39 , pp. 8362-8373
    • Montserret, R.1    McLeish, M.J.2    Bockmann, A.3
  • 54
    • 0028961335 scopus 로고
    • Scop: A structural classification of proteins database for the investigation of sequences and structures
    • Murzin, A.G., Brenner, S.E., Hubbard, T. et al. 1995. Scop: a structural classification of proteins database for the investigation of sequences and structures. J. Mol. Biol., 247:536-40.
    • (1995) J. Mol. Biol , vol.247 , pp. 536-540
    • Murzin, A.G.1    Brenner, S.E.2    Hubbard, T.3
  • 55
    • 33747029276 scopus 로고    scopus 로고
    • Foodprocessing enzymes from recombinant microorganisms-a review
    • Olempska-Beer, Z.S., Merker, R.I., Ditto, M.D. et al. 2006. Foodprocessing enzymes from recombinant microorganisms-a review. Reg. Toxicol. Pharmacol., 45:144-58.
    • (2006) Reg. Toxicol. Pharmacol , vol.45 , pp. 144-158
    • Olempska-Beer, Z.S.1    Merker, R.I.2    Ditto, M.D.3
  • 56
    • 0026540411 scopus 로고
    • The alpha/beta hydrolase fold
    • Ollis, D.L., Cheah, E., Cygler, M. et al. 1992. The alpha/beta hydrolase fold. Protein Eng., 5:197-221.
    • (1992) Protein Eng , vol.5 , pp. 197-221
    • Ollis, D.L.1    Cheah, E.2    Cygler, M.3
  • 57
    • 0030777303 scopus 로고    scopus 로고
    • CATH - a hierarchic classification of protein domain structures
    • Orengo, C.A., Michie, A.D., Jones, D.T. et al. 1997. CATH - a hierarchic classification of protein domain structures. Structure, 5:1093-108.
    • (1997) Structure , vol.5 , pp. 1093-1108
    • Orengo, C.A.1    Michie, A.D.2    Jones, D.T.3
  • 58
    • 0035852885 scopus 로고    scopus 로고
    • How do lipases and esterases work: The electrostatic contribution
    • Peterson, M.T.N., Fojan, P. and Peterson, S.B. 2001. How do lipases and esterases work: the electrostatic contribution. J. Biotechnol., 85:115-47.
    • (2001) J. Biotechnol , vol.85 , pp. 115-147
    • Peterson, M.T.N.1    Fojan, P.2    Peterson, S.B.3
  • 59
    • 0034597427 scopus 로고    scopus 로고
    • Lipase engineering database: Understanding and exploiting sequence - structure - function relationships
    • Pleiss, J., Fischer, M., Peiker, M. et al. 2000. Lipase engineering database: Understanding and exploiting sequence - structure - function relationships. J. Mol. Cat. B: Enz., 10:491-508.
    • (2000) J. Mol. Cat. B: Enz , vol.10 , pp. 491-508
    • Pleiss, J.1    Fischer, M.2    Peiker, M.3
  • 60
    • 19444381947 scopus 로고    scopus 로고
    • High-yield purification of an organic solvent-tolerant lipase from Pseudomonas sp. strain S5
    • Rahman, R.N.Z.R.A., Baharum, S.N., Basri, M. et al. 2005. High-yield purification of an organic solvent-tolerant lipase from Pseudomonas sp. strain S5. Anal. Biochem., 341:267-74.
    • (2005) Anal. Biochem , vol.341 , pp. 267-274
    • Rahman, R.N.Z.R.A.1    Baharum, S.N.2    Basri, M.3
  • 61
    • 0029039712 scopus 로고
    • Crystallization and preliminary X-ray analysis of a lipase from Staphylococcus hyicus
    • Ransac, S., Blaauw, M., Dijkstra, B.W. et al. 1995. Crystallization and preliminary X-ray analysis of a lipase from Staphylococcus hyicus. J. Struct. Biol., 114:153-5.
    • (1995) J. Struct. Biol , vol.114 , pp. 153-155
    • Ransac, S.1    Blaauw, M.2    Dijkstra, B.W.3
  • 62
    • 0037208467 scopus 로고    scopus 로고
    • Purification strategies for microbial lipases
    • Saxena, R.K., Sheoran, A., Giri, B. et al. 2003. Purification strategies for microbial lipases. J. Microbiol. Methods, 52:1-18.
    • (2003) J. Microbiol. Methods , vol.52 , pp. 1-18
    • Saxena, R.K.1    Sheoran, A.2    Giri, B.3
  • 63
    • 0010237021 scopus 로고    scopus 로고
    • The open conformation of a Pseudomonas lipase
    • Schrag, J.D., Li, Y., Cygler, M. et al. 1997. The open conformation of a Pseudomonas lipase. Structure, 5:187-202.
    • (1997) Structure , vol.5 , pp. 187-202
    • Schrag, J.D.1    Li, Y.2    Cygler, M.3
  • 64
    • 33646002943 scopus 로고    scopus 로고
    • The lid is a structural and functional determinant of lipase activity and selectivity
    • Secundo, F., Carrea, G., Tarabiono, C. et al. 2006. The lid is a structural and functional determinant of lipase activity and selectivity. J. Mol. Cat. B: Enz., 39:166-70.
    • (2006) J. Mol. Cat. B: Enz , vol.39 , pp. 166-170
    • Secundo, F.1    Carrea, G.2    Tarabiono, C.3
  • 65
    • 8444246271 scopus 로고    scopus 로고
    • Using artificially generated spectral data to improve protein secondary structure prediction from Fourier transform infrared spectra of proteins
    • Severcan, M., Haris, P.I. and Severcan, F. 2004. Using artificially generated spectral data to improve protein secondary structure prediction from Fourier transform infrared spectra of proteins. Anal. Biochem., 332:238-44.
    • (2004) Anal. Biochem , vol.332 , pp. 238-244
    • Severcan, M.1    Haris, P.I.2    Severcan, F.3
  • 66
    • 33645385129 scopus 로고    scopus 로고
    • Homology modeling of milk enzymes using on-line resources : Insights to structure - function and evolutionary relationships
    • Sheehan, D. and Sullivan, S.O. 2006. Homology modeling of milk enzymes using on-line resources : Insights to structure - function and evolutionary relationships. Int. Diary J., 16:701-6.
    • (2006) Int. Diary J , vol.16 , pp. 701-706
    • Sheehan, D.1    Sullivan, S.O.2
  • 67
    • 2442508067 scopus 로고    scopus 로고
    • Molecular engineering of Rhizopus oryzae lipase using a combinatonal protein library constructed on the yeast cell surface
    • Shibamoto, H., Matsumoto, T., Fukuda, H. et al. 2004. Molecular engineering of Rhizopus oryzae lipase using a combinatonal protein library constructed on the yeast cell surface. J. Mol. Catal. B: Enz., 28:235-9.
    • (2004) J. Mol. Catal. B: Enz , vol.28 , pp. 235-239
    • Shibamoto, H.1    Matsumoto, T.2    Fukuda, H.3
  • 68
    • 0034810493 scopus 로고    scopus 로고
    • Structural modeling and characterization of a thermostable lipase from Bacillus stearothermophilus P1
    • Sinchaikul, S., Sookkheo, B., Phutrakal, S. et al. 2001. Structural modeling and characterization of a thermostable lipase from Bacillus stearothermophilus P1. Biochem. Biophys. Res. Commun., 283:868-75.
    • (2001) Biochem. Biophys. Res. Commun , vol.283 , pp. 868-875
    • Sinchaikul, S.1    Sookkheo, B.2    Phutrakal, S.3
  • 69
    • 0036006785 scopus 로고    scopus 로고
    • Expression, purification, crystallization and preliminary crystallographic analysis of a thermostable lipase from Bacillus stearothermophilus P1
    • Sinchaikul, S., Tyndall, J.D.A., Fothergill-Gilmore, L.A. et al. 2002. Expression, purification, crystallization and preliminary crystallographic analysis of a thermostable lipase from Bacillus stearothermophilus P1. Acta. Cryst., D58:182-5.
    • (2002) Acta. Cryst , vol.D58 , pp. 182-185
    • Sinchaikul, S.1    Tyndall, J.D.A.2    Fothergill-Gilmore, L.A.3
  • 70
    • 0034731605 scopus 로고    scopus 로고
    • Lipase protein engineering
    • Svendsen, A. 2000. Lipase protein engineering. Biochim. Biophys, Acta., 1543:233-8.
    • (2000) Biochim. Biophys, Acta , vol.1543 , pp. 233-238
    • Svendsen, A.1
  • 71
    • 0035264178 scopus 로고    scopus 로고
    • Recombinant expression and characterization of the Candida rugosa lip4 lipase in Pichia pastoris: Comparison of glycosylation, activity, and stability
    • Tang, S.J., Shaw, J.F., Sun, K.H. et al. 2001. Recombinant expression and characterization of the Candida rugosa lip4 lipase in Pichia pastoris: Comparison of glycosylation, activity, and stability. Arch. Biochem. Biophys., 387:93-8.
    • (2001) Arch. Biochem. Biophys , vol.387 , pp. 93-98
    • Tang, S.J.1    Shaw, J.F.2    Sun, K.H.3
  • 72
    • 1642362476 scopus 로고    scopus 로고
    • Cloning, sequencing and structural features of a novel Streptococcus lipase
    • Tripathi, M.K., Roy, U. and Jinwal, U.K. 2004. Cloning, sequencing and structural features of a novel Streptococcus lipase. Enz. Microb. Technol., 34:437-45.
    • (2004) Enz. Microb. Technol , vol.34 , pp. 437-445
    • Tripathi, M.K.1    Roy, U.2    Jinwal, U.K.3
  • 73
    • 0036431593 scopus 로고    scopus 로고
    • Crystal structure of a thermostable-lipase from Bacillus stearothermophilus P1
    • Tyndall, J., Sinchaikul, S., Gilmore, L., Taylor, P. and Walkinshaw, M. 2002. Crystal structure of a thermostable-lipase from Bacillus stearothermophilus P1. J. Mol. Biol., 323:859-69.
    • (2002) J. Mol. Biol , vol.323 , pp. 859-869
    • Tyndall, J.1    Sinchaikul, S.2    Gilmore, L.3    Taylor, P.4    Walkinshaw, M.5
  • 74
    • 0000233752 scopus 로고    scopus 로고
    • Lipase specificities: Potential application in lipid bioconversions
    • Villeneuve, P. and Foglia, T.A. 1997. Lipase specificities: Potential application in lipid bioconversions. Inform., 8:640-50.
    • (1997) Inform , vol.8 , pp. 640-650
    • Villeneuve, P.1    Foglia, T.A.2
  • 75
    • 33750328436 scopus 로고    scopus 로고
    • Lipidic sponge phase crystallization of membrane proteins
    • Wadsten, P., Wohri, A.B., Snijder, A. et al. 2006. Lipidic sponge phase crystallization of membrane proteins. J. Mol. Biol., 364:44-53.
    • (2006) J. Mol. Biol , vol.364 , pp. 44-53
    • Wadsten, P.1    Wohri, A.B.2    Snijder, A.3
  • 76
    • 0024279235 scopus 로고
    • Analysis and prediction of the different types of β-turn in proteins
    • Wilmot, C.M. and Thornton, J.M. 1988. Analysis and prediction of the different types of β-turn in proteins. J. Mol. Biol., 203:221-32.
    • (1988) J. Mol. Biol , vol.203 , pp. 221-232
    • Wilmot, C.M.1    Thornton, J.M.2
  • 77
    • 33748053337 scopus 로고    scopus 로고
    • Conformation biases of amino acids based on tripeptide microenvironment from PDB. database
    • Yang, J., Dong, X.C. and Leng, Y. 2006. Conformation biases of amino acids based on tripeptide microenvironment from PDB. database. J. Theoret. Biol., 240:374-84.
    • (2006) J. Theoret. Biol , vol.240 , pp. 374-384
    • Yang, J.1    Dong, X.C.2    Leng, Y.3
  • 78
    • 0035844688 scopus 로고    scopus 로고
    • Impact of the tryptophan residues of Humicola lanuginosa lipase on its thermal stability
    • Zhu, K., Jutila, A., Tuominen, E.K.J. et al. 2001. Impact of the tryptophan residues of Humicola lanuginosa lipase on its thermal stability. Biochim. Biophys. Acta., 1547:329-38.
    • (2001) Biochim. Biophys. Acta , vol.1547 , pp. 329-338
    • Zhu, K.1    Jutila, A.2    Tuominen, E.K.J.3
  • 79
    • 0023660653 scopus 로고
    • Prediction of protein secondary structure and active sites using the alignment of homologous sequences
    • Zvelebil, M.J., Barton, G.J., Taylor, W.R. et al. 1987. Prediction of protein secondary structure and active sites using the alignment of homologous sequences. J. Mol. Biol., 195:957-61.
    • (1987) J. Mol. Biol , vol.195 , pp. 957-961
    • Zvelebil, M.J.1    Barton, G.J.2    Taylor, W.R.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.