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Volumn 13, Issue 12, 2004, Pages 3092-3103

Specificity in lipases: A computational study of transesterification of sucrose

Author keywords

Computational methods; Lipases; Specificity; Sucrose; Transesterification

Indexed keywords

LAURIC ACID VINYL ESTER; SUCROSE; TRIACYLGLYCEROL LIPASE; UNCLASSIFIED DRUG; VINYL DERIVATIVE;

EID: 9344265171     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.04724504     Document Type: Article
Times cited : (22)

References (61)
  • 1
    • 0026642968 scopus 로고
    • Docking by least-squares fitting of molecular surface patterns
    • Bacon, D.J. and Moult, J. 1992. Docking by least-squares fitting of molecular surface patterns. J. Mol. Biol. 225: 849-858.
    • (1992) J. Mol. Biol. , vol.225 , pp. 849-858
    • Bacon, D.J.1    Moult, J.2
  • 2
    • 0034613172 scopus 로고    scopus 로고
    • Dynamically controlled protein tunneling paths in photosynthetic reaction centers
    • Baladin, I.A. and Onuchic, J. 2000. Dynamically controlled protein tunneling paths in photosynthetic reaction centers. Science 290: 114-117.
    • (2000) Science , vol.290 , pp. 114-117
    • Baladin, I.A.1    Onuchic, J.2
  • 3
    • 0141523254 scopus 로고    scopus 로고
    • Sequence of the lid affects activity and specificity of Candida rugosa lipase isoenzymes
    • Brocca, S., Secundo, F., Ossola, M., Alberghina, L., Carrea, G., and Lotti, M. 2003. Sequence of the lid affects activity and specificity of Candida rugosa lipase isoenzymes. Protein Sci. 12: 2312-2319.
    • (2003) Protein Sci. , vol.12 , pp. 2312-2319
    • Brocca, S.1    Secundo, F.2    Ossola, M.3    Alberghina, L.4    Carrea, G.5    Lotti, M.6
  • 6
  • 8
    • 0037418340 scopus 로고    scopus 로고
    • Atomic-level observation of macromolecular crowding effects: Escape of a protein from the GroEL cage
    • Elcock, A.M. 2003. Atomic-level observation of macromolecular crowding effects: Escape of a protein from the GroEL cage. Proc. Natl. Acad. Sci. 100: 2340-2344.
    • (2003) Proc. Natl. Acad. Sci. , vol.100 , pp. 2340-2344
    • Elcock, A.M.1
  • 9
    • 0025047629 scopus 로고
    • A mutant T4 lysozyme displays five different crystal conformations
    • Faber, H.R. and Matthews, B.W. 1990. A mutant T4 lysozyme displays five different crystal conformations. Nature 348: 263-266.
    • (1990) Nature , vol.348 , pp. 263-266
    • Faber, H.R.1    Matthews, B.W.2
  • 11
    • 0034625425 scopus 로고    scopus 로고
    • A simple procedure for the regioselective synthesis of fatty acid esters of maltose, leucrose, maltotriose and n-dodecyl maltosides
    • Ferrer, M., Cruces, M.A., Plou, F.J., Bernabé, M. and Ballesteros, A. 2000. A simple procedure for the regioselective synthesis of fatty acid esters of maltose, leucrose, maltotriose and n-dodecyl maltosides. Tetrahedron 56: 4053-4061.
    • (2000) Tetrahedron , vol.56 , pp. 4053-4061
    • Ferrer, M.1    Cruces, M.A.2    Plou, F.J.3    Bernabé, M.4    Ballesteros, A.5
  • 12
    • 0035940247 scopus 로고    scopus 로고
    • Dissecting the vibrational entropy change on protein/ligand binding: Burial of a water molecule in bovine pancreatic trypsin inhibitor
    • Fischer, S., Smith, J.C., and Verma, C.S. 2001. Dissecting the vibrational entropy change on protein/ligand binding: Burial of a water molecule in bovine pancreatic trypsin inhibitor. J. Phys. Chem. B 105: 8050-8055.
    • (2001) J. Phys. Chem. B , vol.105 , pp. 8050-8055
    • Fischer, S.1    Smith, J.C.2    Verma, C.S.3
  • 14
    • 0028304966 scopus 로고
    • X-ray crystal structure of cross-linked subtilisin Carlsberg in water vs. acetonitrile
    • Fitzpatrick, P.A., Ringe, D., and Klibanov, A.M. 1994. X-ray crystal structure of cross-linked subtilisin Carlsberg in water vs. acetonitrile. Biochem. Biophys. Res. Comm. 198: 675-681.
    • (1994) Biochem. Biophys. Res. Comm. , vol.198 , pp. 675-681
    • Fitzpatrick, P.A.1    Ringe, D.2    Klibanov, A.M.3
  • 15
    • 0032574827 scopus 로고    scopus 로고
    • Dynamics and function of proteins: The search for general concepts
    • Frauenfelder, H. and McMahon, B. 1998. Dynamics and function of proteins: The search for general concepts. Proc. Natl. Acad. Sci. 95: 4795-4797.
    • (1998) Proc. Natl. Acad. Sci. , vol.95 , pp. 4795-4797
    • Frauenfelder, H.1    McMahon, B.2
  • 16
    • 0035957014 scopus 로고    scopus 로고
    • The role of structure, energy landscape, dynamics, and allostery in the enzymatic function of myoglobin
    • Frauenfelder, H., McMahon, B.H., Austin, R.H., Chu, K., and Groves, J.T. 2001. The role of structure, energy landscape, dynamics, and allostery in the enzymatic function of myoglobin. Proc. Natl. Acad. Sci. 98: 2370-2374
    • (2001) Proc. Natl. Acad. Sci. , vol.98 , pp. 2370-2374
    • Frauenfelder, H.1    McMahon, B.H.2    Austin, R.H.3    Chu, K.4    Groves, J.T.5
  • 17
    • 12244312164 scopus 로고    scopus 로고
    • Computational studies of subtilisin-catalyzed transesterification of sucrose: Importance of entropic effects
    • Fuentes, G., Cruces, M.A., Plou, F.J., Ballesteros, A., and Verma, C.S. 2002. Computational studies of subtilisin-catalyzed transesterification of sucrose: Importance of entropic effects. ChemBioChem 3: 907-910.
    • (2002) ChemBioChem , vol.3 , pp. 907-910
    • Fuentes, G.1    Cruces, M.A.2    Plou, F.J.3    Ballesteros, A.4    Verma, C.S.5
  • 18
    • 0346726109 scopus 로고    scopus 로고
    • How enzymes work: Analysis by modern rate theory and computer simulations
    • Garcia-Viloca, M., Gao, J., Karplus, M., and Truhlar, D.G. 2004. How enzymes work: Analysis by modern rate theory and computer simulations. Science 303: 186-195.
    • (2004) Science , vol.303 , pp. 186-195
    • Garcia-Viloca, M.1    Gao, J.2    Karplus, M.3    Truhlar, D.G.4
  • 19
    • 0028335096 scopus 로고
    • Structural mechanisms for domain movements in proteins
    • Gerstein, M., Lesk, A., and Chotia, C. 1994. Structural mechanisms for domain movements in proteins. Biochemistry 33: 6739-6749.
    • (1994) Biochemistry , vol.33 , pp. 6739-6749
    • Gerstein, M.1    Lesk, A.2    Chotia, C.3
  • 20
    • 0025135112 scopus 로고
    • Automated docking to proteins by simulated annealing
    • Goodsell, D.S. and Olsen, A.J. 1990. Automated docking to proteins by simulated annealing. Proteins 8: 195-202.
    • (1990) Proteins , vol.8 , pp. 195-202
    • Goodsell, D.S.1    Olsen, A.J.2
  • 21
    • 4143085329 scopus 로고    scopus 로고
    • Modulating functional loop movements: The role of highly conserved residues in the correlated loop motions
    • Gunasekaran, K. and Nussinov, R. 2004. Modulating functional loop movements: The role of highly conserved residues in the correlated loop motions. ChemBioChem 5: 224-230.
    • (2004) ChemBioChem , vol.5 , pp. 224-230
    • Gunasekaran, K.1    Nussinov, R.2
  • 22
    • 0031887073 scopus 로고    scopus 로고
    • Molecular modeling of the enantioselectivity in lipase-catalyzed transesterification reactions
    • Haeffner, F., Norin, T., and Hult, K. 1998. Molecular modeling of the enantioselectivity in lipase-catalyzed transesterification reactions. Biophys. J. 74: 1251-1262.
    • (1998) Biophys. J. , vol.74 , pp. 1251-1262
    • Haeffner, F.1    Norin, T.2    Hult, K.3
  • 23
    • 0026076090 scopus 로고
    • Collective motions in proteins: A covariance analysis of atomic fluctuations in molecular dynamics and normal mode simulations
    • Ichiye, T. and Karplus, M. 1991. Collective motions in proteins: A covariance analysis of atomic fluctuations in molecular dynamics and normal mode simulations. Proteins 11: 205-217.
    • (1991) Proteins , vol.11 , pp. 205-217
    • Ichiye, T.1    Karplus, M.2
  • 24
    • 0038851964 scopus 로고    scopus 로고
    • Identifying key electrostatic interactions in Rhizomucor miehei lipase: The influence of solvent dielectric
    • Jääskeläinen, S., Verma, C.S., Hubbard, R.E., and Caves, L.S.D. 1998a. Identifying key electrostatic interactions in Rhizomucor miehei lipase: The influence of solvent dielectric. Theor. Chem. Acc. 101: 175-179.
    • (1998) Theor. Chem. Acc. , vol.101 , pp. 175-179
    • Jääskeläinen, S.1    Verma, C.S.2    Hubbard, R.E.3    Caves, L.S.D.4
  • 27
    • 0030028728 scopus 로고    scopus 로고
    • Principles of protein-protein interactions derived from structural studies
    • Jones, S. and Thornton, J.M. 1996. Principles of protein-protein interactions derived from structural studies. Proc. Natl. Acad. Sci. 93: 13-20.
    • (1996) Proc. Natl. Acad. Sci. , vol.93 , pp. 13-20
    • Jones, S.1    Thornton, J.M.2
  • 29
    • 0035929129 scopus 로고    scopus 로고
    • Modeling-A tool for experimentalists
    • Kazlauskas, R.J. 2001. Modeling-A tool for experimentalists. Science 293: 2277-2279.
    • (2001) Science , vol.293 , pp. 2277-2279
    • Kazlauskas, R.J.1
  • 30
    • 0001858251 scopus 로고
    • Application of a theory of enzyme specificity to protein synthesis
    • Koshland, D.E. 1958. Application of a theory of enzyme specificity to protein synthesis. Proc. Natl. Acad. Sci. 44: 98-104.
    • (1958) Proc. Natl. Acad. Sci. , vol.44 , pp. 98-104
    • Koshland, D.E.1
  • 31
    • 0031687653 scopus 로고    scopus 로고
    • Anatomy of protein pockets and cavities: Measurements of binding site geometry and implications for ligand design
    • Liang, J., Edelsbrunner, H., and Woodward, C. 1998. Anatomy of protein pockets and cavities: Measurements of binding site geometry and implications for ligand design. Protein Sci. 7: 1884-1897.
    • (1998) Protein Sci. , vol.7 , pp. 1884-1897
    • Liang, J.1    Edelsbrunner, H.2    Woodward, C.3
  • 32
    • 0032501383 scopus 로고    scopus 로고
    • Dynamic flexibility of protein-inhibitor complexes: A study of the HIV-1 protease/KNI-272 complex
    • Luo, X., Kato, R., and Collins, J.R. 1998. Dynamic flexibility of protein-inhibitor complexes: A study of the HIV-1 protease/KNI-272 complex. J. Amer. Chem. Soc. 120: 12410-12418.
    • (1998) J. Amer. Chem. Soc. , vol.120 , pp. 12410-12418
    • Luo, X.1    Kato, R.2    Collins, J.R.3
  • 33
    • 0029148636 scopus 로고
    • On the interfacial activation of Candida antarctica lipase A and B as compared with Humicola lanuginosa lipase
    • Martinelle, M., Holmquist, M., and Hult, K. 1995. On the interfacial activation of Candida antarctica lipase A and B as compared with Humicola lanuginosa lipase. Biochim. Biophys. Acta 1258: 272-276.
    • (1995) Biochim. Biophys. Acta , vol.1258 , pp. 272-276
    • Martinelle, M.1    Holmquist, M.2    Hult, K.3
  • 35
    • 0037077656 scopus 로고    scopus 로고
    • Molecular dynamics at the root of expansion of function in the M69L inhibitor-resistant TEM -lactamase from Escherichia coli
    • Meroueh, S.O., Roblin, P., Golemi, D., Maveyraud, L., Vakulenko, S.B., Zhang, Y., Samama, J.-P., and Mobashery, S. 2002. Molecular dynamics at the root of expansion of function in the M69L inhibitor-resistant TEM -lactamase from Escherichia coli. J. Am. Chem. Soc. 124: 9422-9430.
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 9422-9430
    • Meroueh, S.O.1    Roblin, P.2    Golemi, D.3    Maveyraud, L.4    Vakulenko, S.B.5    Zhang, Y.6    Samama, J.-P.7    Mobashery, S.8
  • 36
    • 0033548074 scopus 로고    scopus 로고
    • Enzyme specificity under dynamic control: A normal mode analysis of α-lytic protease
    • Miller, D.W. and Agard, D.A. 1999. Enzyme specificity under dynamic control: A normal mode analysis of α-lytic protease. J. Mol. Biol. 286: 267-278.
    • (1999) J. Mol. Biol. , vol.286 , pp. 267-278
    • Miller, D.W.1    Agard, D.A.2
  • 38
    • 0029048413 scopus 로고
    • Structure of bam-hi endonuclease bound to DNA-partial folding and unfolding on DNA-binding
    • Newman, M., Strzelecka, T., Dorner, L.F., Schildkraut, I., and Aggarwal, A.K. 1995. Structure of bam-hi endonuclease bound to DNA-partial folding and unfolding on DNA-binding. Science 269: 656-663.
    • (1995) Science , vol.269 , pp. 656-663
    • Newman, M.1    Strzelecka, T.2    Dorner, L.F.3    Schildkraut, I.4    Aggarwal, A.K.5
  • 39
    • 0027960085 scopus 로고
    • Computer modeling of substrate-binding to lipases from Rhizomucor miehei, Humicola lanuginosa and Candida rugosa
    • Norin, M., Haeffner, F., Achour, A., Norin, T., and Hult, K. 1994. Computer modeling of substrate-binding to lipases from Rhizomucor miehei, Humicola lanuginosa and Candida rugosa. Protein Sci. 3: 1493-1503.
    • (1994) Protein Sci. , vol.3 , pp. 1493-1503
    • Norin, M.1    Haeffner, F.2    Achour, A.3    Norin, T.4    Hult, K.5
  • 40
    • 0035122917 scopus 로고    scopus 로고
    • Predicting the emergence of antibiotic resistance by directed evolution and structural analysis
    • Orencia, M.C., Yoon, S.S., Ness, J.E., Stemmer, W.P.C., and Stevens, R.C. 2001. Predicting the emergence of antibiotic resistance by directed evolution and structural analysis. Nat. Struct. Biol. 8: 238-242.
    • (2001) Nat. Struct. Biol. , vol.8 , pp. 238-242
    • Orencia, M.C.1    Yoon, S.S.2    Ness, J.E.3    Stemmer, W.P.C.4    Stevens, R.C.5
  • 41
    • 0034681499 scopus 로고    scopus 로고
    • Substrate specificity of lipase B from Candida antarctica in the synthesis of arylaliphatic glycolipids
    • Otto, R.T., Scheib, H., Bornscheuer, U.T., Pleiss, J., Syldatk, C., and Schmid, R.D. 2000. Substrate specificity of lipase B from Candida antarctica in the synthesis of arylaliphatic glycolipids. J. Mol. Catal. B: Enzym. 8: 201-211.
    • (2000) J. Mol. Catal. B: Enzym. , vol.8 , pp. 201-211
    • Otto, R.T.1    Scheib, H.2    Bornscheuer, U.T.3    Pleiss, J.4    Syldatk, C.5    Schmid, R.D.6
  • 42
    • 0036102164 scopus 로고    scopus 로고
    • Substrate entropy in enzyme enantioselectivity: An experimental and molecular modeling study of a lipase
    • Ottosson, J., Fransson, L., and Hult, K. 2002. Substrate entropy in enzyme enantioselectivity: An experimental and molecular modeling study of a lipase. Protein Sci. 11: 1462-1471.
    • (2002) Protein Sci. , vol.11 , pp. 1462-1471
    • Ottosson, J.1    Fransson, L.2    Hult, K.3
  • 44
    • 0000421878 scopus 로고
    • Nature of the forces between large molecules of biological interest
    • Pauling, L. 1948. Nature of the forces between large molecules of biological interest. Nature 161: 707-709.
    • (1948) Nature , vol.161 , pp. 707-709
    • Pauling, L.1
  • 45
    • 0036873130 scopus 로고    scopus 로고
    • Essential motions in a fungal lipase with bound substrate, covalemly attached inhibitor and product
    • Peters, G.H. and Bywater, R.P. 2002. Essential motions in a fungal lipase with bound substrate, covalemly attached inhibitor and product. J. Mol. Recognit. 15: 393-404.
    • (2002) J. Mol. Recognit. , vol.15 , pp. 393-404
    • Peters, G.H.1    Bywater, R.P.2
  • 46
    • 0032103791 scopus 로고    scopus 로고
    • Anatomy of lipase binding sites: The scissile fatty acid binding site
    • Pleiss, J., Fischer, M., and Schmid, R.D. 1998. Anatomy of lipase binding sites: The scissile fatty acid binding site. Chem. Phys. Lipids 93: 67-80.
    • (1998) Chem. Phys. Lipids , vol.93 , pp. 67-80
    • Pleiss, J.1    Fischer, M.2    Schmid, R.D.3
  • 47
    • 0034597427 scopus 로고    scopus 로고
    • Lipase engineering database: Understanding and exploiting sequence-structure-function relationships
    • Pleiss, J., Fischer, M., Peiker, M., Thiele, C., and Schmid, R.D. 2000. Lipase engineering database: Understanding and exploiting sequence-structure- function relationships. J. Mol. Catal. B: Enzym. 10: 491-508.
    • (2000) J. Mol. Catal. B: Enzym. , vol.10 , pp. 491-508
    • Pleiss, J.1    Fischer, M.2    Peiker, M.3    Thiele, C.4    Schmid, R.D.5
  • 48
    • 0033955055 scopus 로고    scopus 로고
    • Protein dynamics in enzymatic catalysis: Exploration of dihydrofolate reductase
    • Radkiewicz, J.L. and Brooks, C.L. 2000. Protein dynamics in enzymatic catalysis: Exploration of dihydrofolate reductase. J. Amer. Chem. Soc. 122: 225-231.
    • (2000) J. Amer. Chem. Soc. , vol.122 , pp. 225-231
    • Radkiewicz, J.L.1    Brooks, C.L.2
  • 49
    • 0028175417 scopus 로고
    • Refinement of γ-δ-resolvase reveals a strikingly flexible molecule
    • Rice, P.A. and Steitz, T.A. 1994. Refinement of γ-δ-resolvase reveals a strikingly flexible molecule. Structure 2: 371-384.
    • (1994) Structure , vol.2 , pp. 371-384
    • Rice, P.A.1    Steitz, T.A.2
  • 50
    • 0032479388 scopus 로고    scopus 로고
    • Lipases: Interfacial enzymes with attractive applications
    • Schmid, R.D. and Verger, R. 1998. Lipases: Interfacial enzymes with attractive applications. Angew. Chem. Int. Ed. Eng. 37: 1609-1633.
    • (1998) Angew. Chem. Int. Ed. Eng. , vol.37 , pp. 1609-1633
    • Schmid, R.D.1    Verger, R.2
  • 51
    • 9344258876 scopus 로고
    • Protein motions: Structural and functional aspects
    • (eds. R. Diamond et al.). Oxford University Press, Oxford, UK
    • Sneddon, S.F. and Brooks, C.L. 1991. Protein motions: Structural and functional aspects. In Molecular structures in biology (eds. R. Diamond et al.), pp. 113-160. Oxford University Press, Oxford, UK.
    • (1991) Molecular Structures in Biology , pp. 113-160
    • Sneddon, S.F.1    Brooks, C.L.2
  • 52
    • 0037219686 scopus 로고    scopus 로고
    • Evolutionarily conserved networks of residues mediate allosteric communication in proteins
    • Süel, G.M., Lockless, S.W., Wall, M.A., and Ranganathan, R. 2003. Evolutionarily conserved networks of residues mediate allosteric communication in proteins. Nat. Struc. Biol. 10: 59-69.
    • (2003) Nat. Struc. Biol. , vol.10 , pp. 59-69
    • Süel, G.M.1    Lockless, S.W.2    Wall, M.A.3    Ranganathan, R.4
  • 53
    • 0029417196 scopus 로고
    • Crystallographic and molecular-modeling studies of lipase B from Candida antartica reveal a stereospecificity pocket for secondary alcohols
    • Uppenberg, J., Ohrner, N., Norin, M., Hult, K., Kleywegt, G.J., Patkar, S., Waagen, V., Anthonsen, T., and Jones, T.A. 1995. Crystallographic and molecular-modeling studies of lipase B from Candida antartica reveal a stereospecificity pocket for secondary alcohols. Biochemistry 34: 16838-16851.
    • (1995) Biochemistry , vol.34 , pp. 16838-16851
    • Uppenberg, J.1    Ohrner, N.2    Norin, M.3    Hult, K.4    Kleywegt, G.J.5    Patkar, S.6    Waagen, V.7    Anthonsen, T.8    Jones, T.A.9
  • 55
    • 0031557394 scopus 로고    scopus 로고
    • Domain motions in dihydrofolate reductase: A molecular dynamics study
    • Verma, C.S., Caves, L.S.D., Hubbard, R.E., and Roberts, G.G.K. 1997. Domain motions in dihydrofolate reductase: A molecular dynamics study. J. Mol. Biol. 226: 776-796.
    • (1997) J. Mol. Biol. , vol.226 , pp. 776-796
    • Verma, C.S.1    Caves, L.S.D.2    Hubbard, R.E.3    Roberts, G.G.K.4
  • 56
    • 0041876227 scopus 로고    scopus 로고
    • Computer simulations of enzyme catalysis: Methods, progress, and insights
    • Warshel, A. 2003. Computer simulations of enzyme catalysis: Methods, progress, and insights. Annu. Rev. Biophys. Biomol. Struct. 32: 425-443.
    • (2003) Annu. Rev. Biophys. Biomol. Struct. , vol.32 , pp. 425-443
    • Warshel, A.1
  • 58
    • 0026447731 scopus 로고
    • X-ray structure of the DNAse I-D(GGTATACC)(2) complex at 2.3-Å resolution
    • Weston, S.A., Lahm, A., and Suck, D. 1992. X-ray structure of the DNAse I-D(GGTATACC)(2) complex at 2.3-Å resolution. J. Mol. Biol. 226: 1237-1256.
    • (1992) J. Mol. Biol. , vol.226 , pp. 1237-1256
    • Weston, S.A.1    Lahm, A.2    Suck, D.3
  • 59
    • 0030569896 scopus 로고    scopus 로고
    • Regioselective acylation of disaccharides in tert-butyl alcohol catalyzed by C. antarctica lipase
    • Woudenberg, M., Van Rantwijk, F., and Sheldon, R.A. 1996. Regioselective acylation of disaccharides in tert-butyl alcohol catalyzed by C. antarctica lipase. Biotechnol. Bioeng. 49: 328-333.
    • (1996) Biotechnol. Bioeng. , vol.49 , pp. 328-333
    • Woudenberg, M.1    Van Rantwijk, F.2    Sheldon, R.A.3
  • 60
    • 0035815288 scopus 로고    scopus 로고
    • Dynamic coupling between the SH2 and SH3 domains of c-Src and Hck underlies their inactivation by C-terminal tyrosine phosphorylation
    • Young, M.A., Gonfloni, S., Superti-Furga, G., Roux, B., and Kuriyan, J. 2001. Dynamic coupling between the SH2 and SH3 domains of c-Src and Hck underlies their inactivation by C-terminal tyrosine phosphorylation. Cell 105: 115-126.
    • (2001) Cell , vol.105 , pp. 115-126
    • Young, M.A.1    Gonfloni, S.2    Superti-Furga, G.3    Roux, B.4    Kuriyan, J.5
  • 61
    • 0029036005 scopus 로고
    • Inversion of lipase stereospecificity for fluorogenic alkyldiacyl glycerols. Effect of substrate solubilization
    • Zandonella, G., Haalck, L., Spener, F., Faber, K., Paltauf, F., and Hermetter, A. 1995. Inversion of lipase stereospecificity for fluorogenic alkyldiacyl glycerols. Effect of substrate solubilization. Eur. J. Biochem. 231: 50-55.
    • (1995) Eur. J. Biochem. , vol.231 , pp. 50-55
    • Zandonella, G.1    Haalck, L.2    Spener, F.3    Faber, K.4    Paltauf, F.5    Hermetter, A.6


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