메뉴 건너뛰기




Volumn 77, Issue 3, 2009, Pages 710-717

Crystal structure and enhanced activity of a cutinase-like enzyme from Cryptococcus sp. strain S-2

Author keywords

CLE; Cutinase; Hydrolysis; Lipase; Protein engineering; Site directed mutagenesis; Structural biology; Substrate specificity

Indexed keywords

CUTINASE; CUTINASE LIKE ENZYME; FUNGAL ENZYME; HYDROLASE; UNCLASSIFIED DRUG;

EID: 70349304121     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1002/prot.22484     Document Type: Article
Times cited : (43)

References (49)
  • 3
    • 0029065498 scopus 로고
    • Cutinase from Fusarium solani pisi hydrolyzing triglyceride analogues. Effect of acyl chain length and position in the substrate molecule on activity and enantioselectivity
    • Mannesse ML, Cox RC, Koops BC, Verheij HM, de Haas GH, Egmond MR, van der Hijden HT, de Vlieg J. Cutinase from Fusarium solani pisi hydrolyzing triglyceride analogues. Effect of acyl chain length and position in the substrate molecule on activity and enantioselectivity. Biochemistry 1995;34:6400-6407.
    • (1995) Biochemistry , vol.34 , pp. 6400-6407
    • Mannesse, M.L.1    Cox, R.C.2    Koops, B.C.3    Verheij, H.M.4    De Haas, G.H.5    Egmond, M.R.6    Van Der Hijden, H.T.7    De Vlieg, J.8
  • 4
    • 0029056506 scopus 로고
    • Construction and heterologous expression of a synthetic copy of the cutinase cDNA from Fusarium solani pisi
    • van Gemeren IA, Musters W, van den Hondel CA, Verrips CT. Construction and heterologous expression of a synthetic copy of the cutinase cDNA from Fusarium solani pisi. J Biotechnol 1995;40: 155-162.
    • (1995) J Biotechnol , vol.40 , pp. 155-162
    • Van Gemeren, I.A.1    Musters, W.2    Van Den Hondel, C.A.3    Verrips, C.T.4
  • 7
    • 0031555003 scopus 로고    scopus 로고
    • Kinetic studies of fusarium solani pisi cutinase used in a gas/solid system: Transesterification and hydrolysis reactions
    • DOI 10.1002/(SICI)1097-0290(19971005)56:1<1::AID-BIT1>3.0.CO;2-O
    • Lamare S, Lortie R, Legoy MD. Kinetic studies of fusarium solani pisi cutinase used in a gas/solid system: transesterification and hydrolysis reactions. Biotechnol Bioeng 1997;56:1-8. (Pubitemid 27382481)
    • (1997) Biotechnology and Bioengineering , vol.56 , Issue.1 , pp. 1-8
    • Lamare, S.1    Lortie, R.2    Legoy, M.D.3
  • 9
    • 0032524506 scopus 로고    scopus 로고
    • Effects of amphipaths on the activity and stability of Fusarium solani pisi cutinase
    • DOI 10.1016/S0141-0229(98)00013-1, PII S0141022998000131
    • Pocalyko DJ, Tallman M. Effects of amphipaths on the activity and stability of Fusarium solani pisi cutinase. Enzyme Microb Technol 1998;22:647-651. (Pubitemid 28260582)
    • (1998) Enzyme and Microbial Technology , vol.22 , Issue.7 , pp. 647-651
    • Pocalyko, D.J.1    Tallman, M.2
  • 10
    • 0342459772 scopus 로고    scopus 로고
    • Stability studies of a recombinant cutinase immobilized to dextran and derivatized silica supports
    • DOI 10.1016/S0141-0229(98)00089-1, PII S0141022998000891
    • Gonçalves AM, Schacht E, Matthijs G, Aires-Barros MR, Cabral JM, Gil MH. Stability studies of a recombinant cutinase immobilized to dextran and derivatized silica supports. Enzyme Microb Technol 1999;24:60-66. (Pubitemid 28529470)
    • (1999) Enzyme and Microbial Technology , vol.24 , Issue.1-2 , pp. 60-66
    • Goncalves, A.M.1    Schacht, E.2    Matthijs, G.3    Aires Barros, M.R.4    Cabral, J.M.S.5    Gil, M.H.6
  • 13
    • 0030227450 scopus 로고    scopus 로고
    • Immobilization of a recombinant cutinase by entrapment and by covalent binding. Kinetic and stability studies
    • Gonçalves AP, Cabral JM, Aires-Barros MR. Immobilization of a recombinant cutinase by entrapment and by covalent binding. Kinetic and stability studies. Appl Biochem Biotechnol 1996;60: 217-228.
    • (1996) Appl Biochem Biotechnol , vol.60 , pp. 217-228
    • Gonçalves, A.P.1    Cabral, J.M.2    Aires-Barros, M.R.3
  • 14
    • 0029205576 scopus 로고
    • Triglyceride hydrolysis and stability of a recombinant cutinase from Fusarium solani in AOT-iso-octane reversed micelles
    • Melo EP, Aires-Barros MR, Cabral JM. Triglyceride hydrolysis and stability of a recombinant cutinase from Fusarium solani in AOT-iso-octane reversed micelles. Appl Biochem Biotechnol 1995; 50:45-56.
    • (1995) Appl Biochem Biotechnol , vol.50 , pp. 45-56
    • Melo, E.P.1    Aires-Barros, M.R.2    Cabral, J.M.3
  • 15
    • 0030596102 scopus 로고    scopus 로고
    • Action of cutinase at the triolein-water interface. Characterisation of interfacial effects during lipid hydrolysis using the oil-drop tensiometer as a tool to study lipase kinetics
    • Flipsen JA, van der Hijden HT, Egmond MR, Verheij HM. Action of cutinase at the triolein-water interface. Characterisation of interfacial effects during lipid hydrolysis using the oil-drop tensiometer as a tool to study lipase kinetics. Chem Phys Lipids 1996;84:105-115.
    • (1996) Chem Phys Lipids , vol.84 , pp. 105-115
    • Flipsen, J.A.1    Van Der Hijden, H.T.2    Egmond, M.R.3    Verheij, H.M.4
  • 16
    • 0033646650 scopus 로고    scopus 로고
    • Fusarium solani pisi cutinase
    • Egmond MR, de Vlieg J. Fusarium solani pisi cutinase. Biochimie 2000;82:1015-1021.
    • (2000) Biochimie , vol.82 , pp. 1015-1021
    • Egmond, M.R.1    De Vlieg, J.2
  • 17
    • 0016682066 scopus 로고
    • Hydrolysis of plant cuticle by plant pathogens. Purification, amino acid composition, and molecular weight of two isozymes of cutinase and a nonspecific esterase from Fusarium solani f. pisi
    • Purdy RE, Kolattukudy PE. Hydrolysis of plant cuticle by plant pathogens. Purification, amino acid composition, and molecular weight of two isozymes of cutinase and a nonspecific esterase from Fusarium solani f. pisi. Biochemistry 1975;14:2824-2831.
    • (1975) Biochemistry , vol.14 , pp. 2824-2831
    • Purdy, R.E.1    Kolattukudy, P.E.2
  • 18
    • 0033752932 scopus 로고    scopus 로고
    • Production, purification and characterization of an extracellular lipase from the yeast, Cryptococcus sp. S-2
    • DOI 10.1016/S0032-9592(00)00228-4, PII S0032959200002284
    • Kamini NR, Fujii T, Kurosu T, Iefuji H. Production, purification and characterization of an extracellular lipase from the yeast, Cryptococcus sp. S-2. Process Biochem 2000;36:317-324. (Pubitemid 30818283)
    • (2000) Process Biochemistry , vol.36 , Issue.4 , pp. 317-324
    • Kamini, N.R.1    Fujii, T.2    Kurosu, T.3    Iefuji, H.4
  • 19
    • 32044458811 scopus 로고    scopus 로고
    • Cutinase-like enzyme from the yeast Cryptococcus sp. strain S-2 hydrolyzes polylactic acid and other biodegradable plastics
    • DOI 10.1128/AEM.71.11.7548-7550.2005
    • Masaki K, Kamini NR, Ikeda H, Iefuji H. Cutinase-like enzyme from the yeast Cryptococcus sp. strain S-2 hydrolyzes polylactic acid and other biodegradable plastics. Appl Environ Microbiol 2005;71: 7548-7550. (Pubitemid 43194252)
    • (2005) Applied and Environmental Microbiology , vol.71 , Issue.11 , pp. 7548-7550
    • Masaki, K.1    Kamini, N.R.2    Ikeda, H.3    Iefuji, H.4
  • 20
    • 0035169233 scopus 로고    scopus 로고
    • Lipase catalyzed methanolysis of vegetable oils in aqueous medium by cryptococcus spp. S-2
    • DOI 10.1016/S0032-9592(01)00220-5, PII S0032959201002205
    • Kamini NR, Iefuji H. Lipase catalyzed methanolysis of vegetable oils in aqueous medium by Cryptococcus spp. S-2. Process Biochem 2001;37:405-410. (Pubitemid 33078097)
    • (2001) Process Biochemistry , vol.37 , Issue.4 , pp. 405-410
    • Kamini, N.R.1    Iefuji, H.2
  • 21
    • 44049097661 scopus 로고    scopus 로고
    • Comparing the effect of immobilization methods on the activity of lipase biocatalysts in ester hydrolysis
    • DOI 10.1007/s00449-007-0165-5
    • Costa L, Brissos V, Lemos F, Ribeiro FR, Cabral JM. Comparing the effect of immobilization methods on the activity of lipase biocatalysts in ester hydrolysis. Bioprocess Biosyst Eng 2008;31:323-327. (Pubitemid 351713120)
    • (2008) Bioprocess and Biosystems Engineering , vol.31 , Issue.4 , pp. 323-327
    • Costa, L.1    Brissos, V.2    Lemos, F.3    Ribeiro, F.R.4    Cabral, J.M.S.5
  • 22
    • 0031574909 scopus 로고    scopus 로고
    • Atomic resolution (1.0 A) crystal structure of Fusarium solani cutinase: Stereochemical analysis
    • DOI 10.1006/jmbi.1997.1000
    • Longhi S, Czjzek M, Lamzin V, Nicolas A, Cambillau C. Atomic resolution (1.0 A) crystal structure of Fusarium solani cutinase: stereochemical analysis. J Mol Biol 1997;268:779-799. (Pubitemid 27214437)
    • (1997) Journal of Molecular Biology , vol.268 , Issue.4 , pp. 779-799
    • Longhi, S.1    Czjzek, M.2    Lamzin, V.3    Nicolas, A.4    Cambillau, C.5
  • 24
    • 0033609115 scopus 로고    scopus 로고
    • Backbone dynamics of Fusarium solani pisi cutinase probed by nuclear magnetic resonance: The lack of interfacial activation revisited
    • Prompers JJ, Groenewegen A, Hilbers CW, Pepermans HA. Backbone dynamics of Fusarium solani pisi cutinase probed by nuclear magnetic resonance: the lack of interfacial activation revisited. Biochemistry 1999;38:5315-5327. (Pubitemid 129514837)
    • (1999) Biochemistry , vol.38 , Issue.17 , pp. 5315-5327
    • Prompers, J.J.1    Groenewegen, A.2    Hilbers, C.W.3    Pepermans, H.A.M.4
  • 26
    • 0001844392 scopus 로고    scopus 로고
    • Strategies and design of mutations in lipases
    • Malcata FX, editor. Dordrecht: Kluwer Academic
    • Egmond MR, de Vlieg J, Verhey HM, de Haas GH. Strategies and design of mutations in lipases. In: Malcata FX, editor. Engineering of/with lipases. Dordrecht: Kluwer Academic; 1996. pp 193-202.
    • (1996) Engineering Of/with Lipases , pp. 193-202
    • Egmond, M.R.1    De Vlieg, J.2    Verhey, H.M.3    De Haas, G.H.4
  • 27
    • 0037165610 scopus 로고    scopus 로고
    • Enhancement of transglutaminase activity by NMR identification of its flexible residues affecting the active site
    • DOI 10.1016/S0014-5793(02)02616-9, PII S0014579302026169
    • Shimba N, Shinohara M, Yokoyama K, Kashiwagi T, Ishikawa K, Ejima D, Suzuki E. Enhancement of transglutaminase activity by NMR identification of its flexible residues affecting the active site. FEBS Lett 2002;517:175-179. (Pubitemid 34327654)
    • (2002) FEBS Letters , vol.517 , Issue.1-3 , pp. 175-179
    • Shimba, N.1    Shinohara, M.2    Yokoyama, K.-I.3    Kashiwagi, T.4    Ishikawa, K.5    Ejima, D.6    Suzuki, E.-I.7
  • 28
    • 85004662218 scopus 로고
    • Crystallization and characterization of lipase from Penicillium cyclopium
    • Isobe K, Akiba T, Yamaguchi S. Crystallization and characterization of lipase from Penicillium cyclopium. Agric Biol Chem 1988;52:41-47.
    • (1988) Agric Biol Chem , vol.52 , pp. 41-47
    • Isobe, K.1    Akiba, T.2    Yamaguchi, S.3
  • 29
    • 0026030413 scopus 로고
    • Vectors for constitutive and inducible gene expression in yeast
    • Schena M, Picard D, Yamamoto KR. Vectors for constitutive and inducible gene expression in yeast.Methods Enzymol 1991;194:389-398.
    • (1991) Methods Enzymol , vol.194 , pp. 389-398
    • Schena, M.1    Picard, D.2    Yamamoto, K.R.3
  • 30
    • 0025272639 scopus 로고
    • Current approaches to macromolecular crystallization
    • McPherson A. Current approaches to macromolecular crystallization. Eur J Biochem 1990;189:1-23.
    • (1990) Eur J Biochem , vol.189 , pp. 1-23
    • McPherson, A.1
  • 31
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • DOI 10.1016/S0076-6879(97)76066-X
    • Otwinowski Z, Minor W. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol 1997;276:307-326. (Pubitemid 27085611)
    • (1997) Methods in Enzymology , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 32
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Collaborative Computational Project, Number 4.
    • Collaborative Computational Project, Number 4. The CCP4 suite: programs for protein crystallography. Acta Crystallogr D Biol Crystallogr 1994;50:760-763.
    • (1994) Acta Crystallogr D Biol Crystallogr , vol.50 , pp. 760-763
  • 33
    • 0026095584 scopus 로고
    • Determination of macromolecular structures from anomalous diffraction of synchrotron radiation
    • Hendrickson WA. Determination of macromolecular structures from anomalous diffraction of synchrotron radiation. Science 1991; 254:51-58.
    • (1991) Science , vol.254 , pp. 51-58
    • Hendrickson, W.A.1
  • 37
    • 0030809260 scopus 로고    scopus 로고
    • WARP: Improvement and extension of crystallographic phases by weighted averaging of multiple-refined dummy atomic models
    • DOI 10.1107/S0907444997005696
    • Perrakis A, Sixma TK, Wilson KS, Lamzin VS. wARP: improvement and extension of crystallographic phases by weighted averaging of multiple-refined dummy atomic models. Acta Crystallogr D Biol Crystallogr 1997;53:448-455. (Pubitemid 27340643)
    • (1997) Acta Crystallographica Section D: Biological Crystallography , vol.53 , Issue.4 , pp. 448-455
    • Perrakis, A.1    Sixma, T.K.2    Wilson, K.S.3    Lamzin, V.S.4
  • 38
    • 0032790081 scopus 로고    scopus 로고
    • XtalView/Xfit-A versatile program for manipulating atomic coordinates and electron density
    • McRee DE. XtalView/Xfit-A versatile program for manipulating atomic coordinates and electron density. J Struct Biol 1999;125: 156-165.
    • (1999) J Struct Biol , vol.125 , pp. 156-165
    • McRee, D.E.1
  • 41
    • 0026597444 scopus 로고
    • Free R value: A novel statistical quantity for assessing the accuracy of crystal structures
    • Brünger AT. Free R value: a novel statistical quantity for assessing the accuracy of crystal structures. Nature 1992;355:472-475.
    • (1992) Nature , vol.355 , pp. 472-475
    • Brünger, A.T.1
  • 42
    • 0014432781 scopus 로고
    • Solvent content of protein crystals
    • Matthews BW. Solvent content of protein crystals. J Mol Biol 1968;33:491-497.
    • (1968) J Mol Biol , vol.33 , pp. 491-497
    • Matthews, B.W.1
  • 45
    • 0034308164 scopus 로고    scopus 로고
    • Protein structure comparison using the Markov transition model of evolution
    • DOI 10.1002/1097-0134(20001001)41:1<108::AID-PROT130>3.0.CO;2-S
    • Kawabata T, Nishikawa K. Protein structure comparison using the markov transition model of evolution. Proteins 2000;41:108-122. (Pubitemid 30666917)
    • (2000) Proteins: Structure, Function and Genetics , vol.41 , Issue.1 , pp. 108-122
    • Kawabata, T.1    Nishikawa, K.2
  • 46
    • 0041620359 scopus 로고    scopus 로고
    • MATRAS: A program for protein 3D structure comparison
    • DOI 10.1093/nar/gkg581
    • Kawabata T. MATRAS: a program for protein 3D structure comparison. Nucleic Acids Res 2003;31:3367-3369. (Pubitemid 37442161)
    • (2003) Nucleic Acids Research , vol.31 , Issue.13 , pp. 3367-3369
    • Kawabata, T.1
  • 48
    • 0030041250 scopus 로고    scopus 로고
    • Contribution of cutinase serine 42 side chain to the stabilization of the oxyanion transition state
    • DOI 10.1021/bi9515578
    • Nicolas A, Egmond M, Verrips CT, de Vlieg J, Longhi S, Cambillau C, Martinez C. Contribution of cutinase serine 42 side chain to the stabilization of the oxyanion transition state. Biochemistry 1996;35: 398-410. (Pubitemid 26033912)
    • (1996) Biochemistry , vol.35 , Issue.2 , pp. 398-410
    • Nicolas, A.1    Egmond, M.2    Verrips, C.T.3    De Vlieg, J.4    Longhi, S.5    Cambillau, C.6    Martinez, C.7
  • 49
    • 0026069154 scopus 로고
    • Development of hydrophobicity parameters to analyze proteins which bear post- Or cotranslational modifications
    • Black SD, Mould DR. Development of hydrophobicity parameters to analyze proteins which bear post- or cotranslational modifications. Anal Biochem 1991;193:72-82.
    • (1991) Anal Biochem , vol.193 , pp. 72-82
    • Black, S.D.1    Mould, D.R.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.