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Volumn 37, Issue 12, 2011, Pages 1053-1061

In silico approaches towards understanding CALB using molecular dynamics simulation and docking

Author keywords

CALB; Docking; Gyration; Molecular dynamics simulation; Mutation

Indexed keywords

ACTIVE SITE; CALB; CANDIDA ANTARCTICA LIPASE B; GYRATION; HYDROGEN BONDINGS; IN-SILICO; MOLECULAR DYNAMICS SIMULATION; MOLECULAR DYNAMICS SIMULATIONS; MUTATION; RADIUS OF GYRATION; SERINE PROTEASE;

EID: 81255186021     PISSN: 08927022     EISSN: 10290435     Source Type: Journal    
DOI: 10.1080/08927022.2011.589050     Document Type: Article
Times cited : (11)

References (31)
  • 1
    • 0013357463 scopus 로고
    • Enantioselectivity of some lipases: Control andprediction
    • K. Hult and T. Norin, Enantioselectivity of some lipases: Control andprediction, Pure Appl. Chem. 64 (1992), pp. 1129-1134.
    • (1992) Pure Appl. Chem. , vol.64 , pp. 1129-1134
    • Hult, K.1    Norin, T.2
  • 2
    • 0032167489 scopus 로고    scopus 로고
    • Microbial lipases form versatile tools for biotechnology
    • DOI 10.1016/S0167-7799(98)01195-0, PII S0167779998011950
    • K.E. Jaeger and M.T. Reetz, Microbial lipasesform versatile tools for biotechnology, Trends Biotechnol. 16 (1998), pp. 396-403. (Pubitemid 28410428)
    • (1998) Trends in Biotechnology , vol.16 , Issue.9 , pp. 396-403
    • Jaeger, K.-E.1    Reetz, M.T.2
  • 4
    • 38049012808 scopus 로고    scopus 로고
    • X-ray structure of Candida antarctica lipase A shows a novel lid structure and a likely mode of interfacial activation
    • D.J. Ericsson, A. Kasrayan, P. Johansson, T. Bergfors, A.G. Sandstrom, J.E. Backvall, and S.L. Mowbray, X-ray structure of Candida antarctica lipase A shows a novel lid structure and a likely mode of interfacial activation, J. Mol. Biol. 376 (2008), pp. 109-119.
    • (2008) J. Mol. Biol. , vol.376 , pp. 109-119
    • Ericsson, D.J.1    Kasrayan, A.2    Johansson, P.3    Bergfors, T.4    Sandstrom, A.G.5    Backvall, J.E.6    Mowbray, S.L.7
  • 5
    • 0026432669 scopus 로고
    • Ser-His-Glu triad forms the catalytic site of the lipase from Geotrichum candidum
    • J.D. Schrag, Y.G. Li, S. Wu, and M. Cygler, Ser-His-Glu triadforms the catalytic site of the lipase from Geotrichum candidum, Nature 351 (1991), pp. 761-764. (Pubitemid 21896686)
    • (1991) Nature , vol.351 , Issue.6329 , pp. 761-764
    • Schrag, J.D.1    Li, Y.2    Wu, S.3    Cygler, M.4
  • 6
    • 0025062291 scopus 로고
    • Structure of human pancreatic lipase
    • F.K. Winkler, A. D'Arcy, and W. Hunziker, Structure of human pancreatic lipase, Nature 343 (1990), pp. 771-774.
    • (1990) Nature , vol.343 , pp. 771-774
    • Winkler, F.K.1    D'Arcy, A.2    Hunziker, W.3
  • 10
    • 2542506051 scopus 로고    scopus 로고
    • The crystal structure of a triacylglycerol lipase from Pseudomonas cepacia reveals a highly open conformation in the absence of a bound inhibitor
    • K.K. Kim, H.K. Song, D.H. Shin, K.Y. Hwang, and S.W. Suh, The crystal structure of a triacyl glycerol lipasefrom Pseudomonas cepacia reveals a highly open conformation in the absence of a bound inhibitor, Structure 5 (1997), pp. 173-185. (Pubitemid 27158725)
    • (1997) Structure , vol.5 , Issue.2 , pp. 173-185
    • Kim, K.K.1    Song, H.K.2    Shin, D.H.3    Hwang, K.Y.4    Sun, S.W.5
  • 11
    • 0027336654 scopus 로고
    • 1.8 A refined structure of the lipase from Geotrichum candidum
    • DOI 10.1006/jmbi.1993.1171
    • J.D. SchragandM. Cygler, 1.8 A Refined structure of the lipase from Geotrichum candidum, J. Mol. Biol. 230 (1993), pp. 575-591. (Pubitemid 23161364)
    • (1993) Journal of Molecular Biology , vol.230 , Issue.2 , pp. 575-591
    • Schrag, J.D.1    Cygler, M.2
  • 12
    • 0029148636 scopus 로고
    • On the interfacial activation of Candida antarctica lipase A and B as compared with Humicola lanuginosa lipase
    • M. Martinelle, M. Holmquist, and K. Hult, On the interfacial activation of Candida antarctica lipase A and B as compared with Humicola lanuginosa lipase, Biochim. Biophys. Acta 1258 (1995), pp. 272-276.
    • (1995) Biochim. Biophys. Acta , vol.1258 , pp. 272-276
    • Martinelle, M.1    Holmquist, M.2    Hult, K.3
  • 13
    • 0028773288 scopus 로고
    • The sequence crystal structure determination and refinement of two crystal forms of lipase B from Candida antarctica
    • J. Uppenberg, M.T. Hansen, S. Patkar, and TA. Jones, The sequence, crystal structure determination and refinement of two crystal forms of lipase B from Candida antarctica, Structure 2 (1994), pp. 293-308.
    • (1994) Structure , vol.2 , pp. 293-308
    • Uppenberg, J.1    Hansen, M.T.2    Patkar, S.3    Jones, T.A.4
  • 14
    • 0038814072 scopus 로고    scopus 로고
    • Mutations in distant residues moderately increase the enantioselectivity ofPseudomonas fluorescens esterase towards methyl 3bromo-2-methylpropanoate and ethyl 3phenylbutyrate
    • G.P. Horsman, A.M. Liu, E. Henke, U.T. Bornscheuer, and R.J. Kazlauskas, Mutations in distant residues moderately increase the enantioselectivity ofPseudomonas fluorescens esterase towards methyl 3bromo-2-methylpropanoate and ethyl 3phenylbutyrate, Chemistry 9 (2003), pp. 1933-1939.
    • (2003) Chemistry , vol.9 , pp. 1933-1939
    • Horsman, G.P.1    Liu, A.M.2    Henke, E.3    Bornscheuer, U.T.4    Kazlauskas, R.J.5
  • 15
    • 0042933795 scopus 로고    scopus 로고
    • Engineered enzymes for improved organic synthesis
    • DOI 10.1016/S0958-1669(03)00095-8
    • K. Hult and P. Berglund, Engineered enzymes for improved organic synthesis, Curr. Opin. Biotechnol. 14 (2003), pp. 395-400. (Pubitemid 37011319)
    • (2003) Current Opinion in Biotechnology , vol.14 , Issue.4 , pp. 395-400
    • Hult, K.1    Berglund, P.2
  • 17
    • 20444448921 scopus 로고    scopus 로고
    • Creating space for large secondary alcohols by rational redesign of Candida antarctica lipase B
    • DOI 10.1002/cbic.200400410
    • A.O. Magnusson, J.C. Rotticci-Mulder, A. Santagostino, and K. Hult, Creating space for large secondary alcohols by rational redesign of Candida antarctica lipase B, Chembiochem 6 (2005), pp. 1051-1056. (Pubitemid 40825346)
    • (2005) ChemBioChem , vol.6 , Issue.6 , pp. 1051-1056
    • Magnusson, A.O.1    Rotticci-Mulder, J.C.2    Santagostino, A.3    Hult, K.4
  • 18
    • 0034848412 scopus 로고    scopus 로고
    • Rational design of enantioselective enzymes requires considerations of entropy
    • DOI 10.1110/ps.13501
    • J. Ottosson, J.C. Rotticci-Mulder, D. Rotticci, and K. Hult, Rational design ofenantioselective enzymes requires considerations ofentropy, Protein Sci. 10 (2001), pp. 1769-1774. (Pubitemid 32848773)
    • (2001) Protein Science , vol.10 , Issue.9 , pp. 1769-1774
    • Ottosson, J.1    Rotticci-Mulder, J.C.2    Rotticci, D.3    Hult, K.4
  • 19
    • 0035496145 scopus 로고    scopus 로고
    • Improved enantioselectivity of a lipase by rational protein engineering
    • D. Rotticci, J.C. Rotticci-Mulder, S. Denman, T. Norin, and K. Hult, Improved enantioselectivity of a lipase by rational protein engineering, Chembiochem. 2 (2001), pp. 766-770. (Pubitemid 33722631)
    • (2001) ChemBioChem , vol.2 , Issue.10 , pp. 766-770
    • Rotticci, D.1    Rotticci-Mulder, J.C.2    Denman, S.3    Norin, T.4    Hult, K.5
  • 20
    • 54349122272 scopus 로고    scopus 로고
    • Influence of ?̀-functional groups on the enantior-ecognition of secondary alcohols by Candida antarctica lipase B
    • J. Nyhlen, B. Martin-Matute, A.G. Sandstrom, M. Bocola, and J.E. Backvall, Influence of ?̀-functional groups on the enantior-ecognition of secondary alcohols by Candida antarctica lipase B, Chembiochem. 9 (2008), pp. 1968-1974.
    • (2008) Chembiochem. , vol.9 , pp. 1968-1974
    • Nyhlen, J.1    Martin-Matute, B.2    Sandstrom, A.G.3    Bocola, M.4    Backvall, J.E.5
  • 21
    • 25844525807 scopus 로고    scopus 로고
    • Improving the catalytic activity of Candida antarctica lipase B by circular permutation
    • DOI 10.1021/ja053932h
    • Z. Qian and S. Lutz, Improving the catalytic activity ofCandida antarctica lipase B by circularpermutation, J. Am. Chem. Soc. 127 (2005), pp. 13466-13467. (Pubitemid 41401178)
    • (2005) Journal of the American Chemical Society , vol.127 , Issue.39 , pp. 13466-13467
    • Qian, Z.1    Lutz, S.2
  • 22
    • 37549058473 scopus 로고    scopus 로고
    • Investigating the structural and functional consequences of circular permutation on lipase B from Candida antarctica
    • Z. Qian, C.J. Fields, and S. Lutz, Investigating the structural and functional consequences of circular permutation on lipase B from Candida antarctica, Chembiochem 8 (2007), pp. 1989-1996.
    • (2007) Chembiochem , vol.8 , pp. 1989-1996
    • Qian, Z.1    Fields, C.J.2    Lutz, S.3
  • 23
    • 40449100818 scopus 로고    scopus 로고
    • Modeling structure and flexibility of Candida antarctica lipase B in organic solvents
    • Available at
    • P. Trodler and J. Pleiss, Modeling structure and flexibility of Candida antarctica lipase B in organic solvents, BMC. Struct. Biol. 8 (2008), pp. 1-10. Available at http://www.biomedcentral.com/ 1472-6807/8/9.
    • (2008) BMC. Struct. Biol. , vol.8 , pp. 1-10
    • Trodler, P.1    Pleiss, J.2
  • 24
    • 0035101120 scopus 로고    scopus 로고
    • Enantioselectivity in Candida antarctica lipase B: A molecular dynamics study
    • DOI 10.1110/ps.33901
    • S. Raza, L. Fransson, and K. Hult, Enantioselectivity in Candida antarctica lipase B: A molecular dynamics study, Protein Sci. 10 (2001), pp. 329-338. (Pubitemid 32225653)
    • (2001) Protein Science , vol.10 , Issue.2 , pp. 329-338
    • Raza, S.1    Fransson, L.2    Hult, K.3
  • 25
    • 60849113126 scopus 로고    scopus 로고
    • Structure-based substrate screening for an enzyme
    • Available at
    • T. Xu, L. Zhang, X. Wang, D. Wei, and T. Li, Structure-based substrate screening for an enzyme, BMC Bioinform. 10 (2009), pp. 1-7. Available at http://www.biomedcentral.com/1471-2105/ 10/257.
    • (2009) BMC Bioinform. , vol.10 , pp. 1-7
    • Xu, T.1    Zhang, L.2    Wang, X.3    Wei, D.4    Li, T.5
  • 31
    • 0043102513 scopus 로고    scopus 로고
    • A helix initiation signal in T4 lysozyme identified by polyalanine mutagenesis
    • DOI 10.1016/S0301-4622(02)00193-X, PII S030146220200193X
    • X.J. Zhang, WA. Baase, and B.W. Matthews, A helix initiation signal in T4 lysozyme identified by polyalanine mutagenesis, Biophys. Chem. 101-102 (2002), pp. 43-56. (Pubitemid 35462035)
    • (2002) Biophysical Chemistry , vol.101-102 , pp. 43-56
    • Zhang, X.-J.1    Baase, W.A.2    Matthews, B.W.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.