메뉴 건너뛰기




Volumn 21, Issue , 2014, Pages 42-47

Protein engineering for development of new hydrolytic biocatalysts

Author keywords

[No Author keywords available]

Indexed keywords

EPOXIDE HYDROLASE; TRIACYLGLYCEROL LIPASE;

EID: 84899107214     PISSN: 13675931     EISSN: 18790402     Source Type: Journal    
DOI: 10.1016/j.cbpa.2014.03.015     Document Type: Review
Times cited : (42)

References (42)
  • 4
    • 84876732154 scopus 로고    scopus 로고
    • Strategies for the discovery and engineering of enzymes for biocatalysis
    • Davids T., Schmidt M., Böttcher D., Bornscheuer U.T. Strategies for the discovery and engineering of enzymes for biocatalysis. Curr Opin Chem Biol 2013, 17:215-220.
    • (2013) Curr Opin Chem Biol , vol.17 , pp. 215-220
    • Davids, T.1    Schmidt, M.2    Böttcher, D.3    Bornscheuer, U.T.4
  • 6
    • 84880513684 scopus 로고    scopus 로고
    • Inverting hydrolases and their use in enantioconvergent biotransformations
    • Schober M., Faber K. Inverting hydrolases and their use in enantioconvergent biotransformations. Trends Biotechnol 2013, 31:468-478.
    • (2013) Trends Biotechnol , vol.31 , pp. 468-478
    • Schober, M.1    Faber, K.2
  • 8
    • 0029132275 scopus 로고
    • Kinetics of acyl transfer reactions in organic media catalysed by Candida antarctica lipase B
    • Martinelle M., Hult K. Kinetics of acyl transfer reactions in organic media catalysed by Candida antarctica lipase B. Biochim Biophys Acta 1995, 1251:191-197.
    • (1995) Biochim Biophys Acta , vol.1251 , pp. 191-197
    • Martinelle, M.1    Hult, K.2
  • 9
    • 78650413957 scopus 로고    scopus 로고
    • Circular permutation: a different way to engineer enzyme structure and function
    • Yu Y., Lutz S. Circular permutation: a different way to engineer enzyme structure and function. Trends Biotechnol 2011, 29:18-25.
    • (2011) Trends Biotechnol , vol.29 , pp. 18-25
    • Yu, Y.1    Lutz, S.2
  • 10
    • 73949098126 scopus 로고    scopus 로고
    • Improved triglyceride transesterification by circular permuted Candida antarctica lipase B
    • Yu Y., Lutz S. Improved triglyceride transesterification by circular permuted Candida antarctica lipase B. Biotechnol Bioeng 2010, 105:44-50.
    • (2010) Biotechnol Bioeng , vol.105 , pp. 44-50
    • Yu, Y.1    Lutz, S.2
  • 11
    • 70349255505 scopus 로고    scopus 로고
    • Structural redesign of lipase B from Candida antarctica by circular permutation and incremental truncation
    • Qian Z., Horton J.R., Cheng X., Lutz S. Structural redesign of lipase B from Candida antarctica by circular permutation and incremental truncation. J Mol Biol 2009, 393:191-201.
    • (2009) J Mol Biol , vol.393 , pp. 191-201
    • Qian, Z.1    Horton, J.R.2    Cheng, X.3    Lutz, S.4
  • 12
    • 29844436474 scopus 로고    scopus 로고
    • Fast carbon carbon bond formation by a promiscuous lipase
    • Svedendahl M., Hult K., Berglund P. Fast carbon carbon bond formation by a promiscuous lipase. J Am Chem Soc 2005, 127:17988-17989.
    • (2005) J Am Chem Soc , vol.127 , pp. 17988-17989
    • Svedendahl, M.1    Hult, K.2    Berglund, P.3
  • 14
    • 84868572912 scopus 로고    scopus 로고
    • Bioinformatic analysis of alpha/beta-hydrolase fold enzymes reveals subfamily-specific positions responsible for discrimination of amidase and lipase activities
    • Suplatov D.A., Besenmatter, Švedas V.K., Svendsen A. Bioinformatic analysis of alpha/beta-hydrolase fold enzymes reveals subfamily-specific positions responsible for discrimination of amidase and lipase activities. Protein Eng Des Sel 2012, 25:689-697.
    • (2012) Protein Eng Des Sel , vol.25 , pp. 689-697
    • Suplatov, D.A.1    Besenmatter, W.2    Švedas, V.K.3    Svendsen, A.4
  • 15
    • 80051810428 scopus 로고    scopus 로고
    • Amidases have a hydrogen bond that facilitates nitrogen inversion, but esterases have not
    • Syrén P.-O., Hult K. Amidases have a hydrogen bond that facilitates nitrogen inversion, but esterases have not. ChemCatChem 2011, 3:853-860.
    • (2011) ChemCatChem , vol.3 , pp. 853-860
    • Syrén, P.-O.1    Hult, K.2
  • 17
    • 78650092281 scopus 로고    scopus 로고
    • Mutated variant of Candida antarctica lipase B in (S)-selective dynamic kinetic resolution of secondary alcohols
    • Engström K., Vallin M., Syrén P.O., Hult K., Bäckvall J.E. Mutated variant of Candida antarctica lipase B in (S)-selective dynamic kinetic resolution of secondary alcohols. Org Biomol Chem 2011, 9:81-82.
    • (2011) Org Biomol Chem , vol.9 , pp. 81-82
    • Engström, K.1    Vallin, M.2    Syrén, P.O.3    Hult, K.4    Bäckvall, J.E.5
  • 18
    • 84867372778 scopus 로고    scopus 로고
    • Enantioselective route to ketones and lactones from exocyclic allylic alcohols via metal and enzyme catalysis
    • Warner M.C., Nagendiran A., Bogár K., Bäckvall J.E. Enantioselective route to ketones and lactones from exocyclic allylic alcohols via metal and enzyme catalysis. Org Lett 2012, 14:5094-5097.
    • (2012) Org Lett , vol.14 , pp. 5094-5097
    • Warner, M.C.1    Nagendiran, A.2    Bogár, K.3    Bäckvall, J.E.4
  • 19
    • 84873346530 scopus 로고    scopus 로고
    • Laboratory evolution of enantiocomplementary Candida antarctica lipase B mutants with broad substrate scope
    • Wu Q., Soni P., Reetz M.T. Laboratory evolution of enantiocomplementary Candida antarctica lipase B mutants with broad substrate scope. J Am Chem Soc 2013, 135:1872-1881.
    • (2013) J Am Chem Soc , vol.135 , pp. 1872-1881
    • Wu, Q.1    Soni, P.2    Reetz, M.T.3
  • 20
    • 79959407879 scopus 로고    scopus 로고
    • Rational redesign of Candida antarctica lipase B for the ring opening polymerization of d,d-lactide
    • Takwa M., Larsen M.W., Hult K., Martinelle M. Rational redesign of Candida antarctica lipase B for the ring opening polymerization of d,d-lactide. Chem Commun 2011, 47:7392-7394.
    • (2011) Chem Commun , vol.47 , pp. 7392-7394
    • Takwa, M.1    Larsen, M.W.2    Hult, K.3    Martinelle, M.4
  • 21
    • 84866397954 scopus 로고    scopus 로고
    • Rational engineering of Candida antarctica lipase B for selective monoacylation of diols
    • Hamberg A., Maurer S., Hult K. Rational engineering of Candida antarctica lipase B for selective monoacylation of diols. Chem Commun 2012, 48:10013-10015.
    • (2012) Chem Commun , vol.48 , pp. 10013-10015
    • Hamberg, A.1    Maurer, S.2    Hult, K.3
  • 22
    • 67651161911 scopus 로고    scopus 로고
    • Directed evolution of Candida antarctica lipase A using an episomaly replicating yeast plasmid
    • Sandström A.G., Engström K., Nyhlén J., Kasrayan A., Bäckvall J.E. Directed evolution of Candida antarctica lipase A using an episomaly replicating yeast plasmid. Protein Eng Des Sel 2009, 22:413-420.
    • (2009) Protein Eng Des Sel , vol.22 , pp. 413-420
    • Sandström, A.G.1    Engström, K.2    Nyhlén, J.3    Kasrayan, A.4    Bäckvall, J.E.5
  • 23
    • 77952562463 scopus 로고    scopus 로고
    • Directed evolution of an enantioselective lipase with broad substrate scope for hydrolysis of alpha-substituted esters
    • Engström K., Nyhlén J., Sandström A.G., Bäckvall J.E. Directed evolution of an enantioselective lipase with broad substrate scope for hydrolysis of alpha-substituted esters. J Am Chem Soc 2010, 132:7038-7042.
    • (2010) J Am Chem Soc , vol.132 , pp. 7038-7042
    • Engström, K.1    Nyhlén, J.2    Sandström, A.G.3    Bäckvall, J.E.4
  • 24
    • 84856021987 scopus 로고    scopus 로고
    • Combinatorial reshaping of the Candida antarctica lipase A substrate pocket for enantioselectivity using an extremely condensed library
    • Sandström A.G., Wikmark Y., Engström K., Nyhlén J., Bäckvall J.E. Combinatorial reshaping of the Candida antarctica lipase A substrate pocket for enantioselectivity using an extremely condensed library. Proc Natl Acad Sci U S A 2012, 109:78-83.
    • (2012) Proc Natl Acad Sci U S A , vol.109 , pp. 78-83
    • Sandström, A.G.1    Wikmark, Y.2    Engström, K.3    Nyhlén, J.4    Bäckvall, J.E.5
  • 25
    • 84855916144 scopus 로고    scopus 로고
    • Towards quantitative computer-aided studies of enzymatic enantioselectivity: the case of Candida antarctica lipase A
    • Frushicheva M.P., Warshel A. Towards quantitative computer-aided studies of enzymatic enantioselectivity: the case of Candida antarctica lipase A. ChemBioChem 2012, 13:215-223.
    • (2012) ChemBioChem , vol.13 , pp. 215-223
    • Frushicheva, M.P.1    Warshel, A.2
  • 26
    • 79959252484 scopus 로고    scopus 로고
    • Enantioselectivity of Candida rugosa lipases (Lip1 Lip3, and Lip4) towards 2-bromo phenylacetic acid octyl esters controlled by a single amino acid
    • Piamtongkam R., Duquesne S., Bordes F., Barbe S., André I., Marty A., Chulalaksananukul W. Enantioselectivity of Candida rugosa lipases (Lip1 Lip3, and Lip4) towards 2-bromo phenylacetic acid octyl esters controlled by a single amino acid. Biotechnol Bioeng 2011, 108:1749-1756.
    • (2011) Biotechnol Bioeng , vol.108 , pp. 1749-1756
    • Piamtongkam, R.1    Duquesne, S.2    Bordes, F.3    Barbe, S.4    André, I.5    Marty, A.6    Chulalaksananukul, W.7
  • 27
    • 0035710814 scopus 로고    scopus 로고
    • Microbial epoxide hydrolases for preparative biotransformations
    • Steinreiber A., Faber K. Microbial epoxide hydrolases for preparative biotransformations. Curr Opin Biotechnol 2001, 6:552-558.
    • (2001) Curr Opin Biotechnol , vol.6 , pp. 552-558
    • Steinreiber, A.1    Faber, K.2
  • 28
    • 40949160217 scopus 로고    scopus 로고
    • Enzymatic synthesis of optically active tertiary alcohols: expanding the biocatalysis toolbox
    • Kourist R., Dominguez de Maria P., Bornscheuer U.T. Enzymatic synthesis of optically active tertiary alcohols: expanding the biocatalysis toolbox. ChemBioChem 2008, 9:491-498.
    • (2008) ChemBioChem , vol.9 , pp. 491-498
    • Kourist, R.1    Dominguez de Maria, P.2    Bornscheuer, U.T.3
  • 29
    • 68749119358 scopus 로고    scopus 로고
    • Biotechnological production of enantiopure epoxides by enzymatic kinetic resolution
    • Choi W.J. Biotechnological production of enantiopure epoxides by enzymatic kinetic resolution. Appl Microbiol Biotechnol 2009, 84:239-247.
    • (2009) Appl Microbiol Biotechnol , vol.84 , pp. 239-247
    • Choi, W.J.1
  • 30
    • 76749138467 scopus 로고    scopus 로고
    • Structure-function relationships of epoxide hydrolases and their potential use in biocatalysis
    • Widersten M., Gurell A., Lindberg D. Structure-function relationships of epoxide hydrolases and their potential use in biocatalysis. Biochim Biophys Acta 2010, 1800:316-326.
    • (2010) Biochim Biophys Acta , vol.1800 , pp. 316-326
    • Widersten, M.1    Gurell, A.2    Lindberg, D.3
  • 32
    • 77049095558 scopus 로고    scopus 로고
    • Mutations in salt-bridging residues at the interface of the core and lid domains of epoxide hydrolase StEH1 affect regioselectivity, protein stability and hysteresis
    • Lindberg D., Ahmad S., Widersten M. Mutations in salt-bridging residues at the interface of the core and lid domains of epoxide hydrolase StEH1 affect regioselectivity, protein stability and hysteresis. Arch Biochem Biophys 2010, 495:165-173.
    • (2010) Arch Biochem Biophys , vol.495 , pp. 165-173
    • Lindberg, D.1    Ahmad, S.2    Widersten, M.3
  • 33
    • 78349235092 scopus 로고    scopus 로고
    • Deep eutectic solvents (DESs) are viable cosolvents for enzyme-catalyzed epoxide hydrolysis
    • Lindberg D., de la Fuente Revenga M., Widersten M. Deep eutectic solvents (DESs) are viable cosolvents for enzyme-catalyzed epoxide hydrolysis. J Biotechnol 2010, 147:169-171.
    • (2010) J Biotechnol , vol.147 , pp. 169-171
    • Lindberg, D.1    de la Fuente Revenga, M.2    Widersten, M.3
  • 34
    • 77949392428 scopus 로고    scopus 로고
    • Temperature and pH dependence of enzyme catalyzed hydrolysis of trans-methylstyrene oxide: a unifying kinetic model for observed hysteresis, cooperativity and regioselectivity
    • Lindberg D., de la Fuente Revenga M., Widersten M. Temperature and pH dependence of enzyme catalyzed hydrolysis of trans-methylstyrene oxide: a unifying kinetic model for observed hysteresis, cooperativity and regioselectivity. Biochemistry 2010, 49:2297-2304.
    • (2010) Biochemistry , vol.49 , pp. 2297-2304
    • Lindberg, D.1    de la Fuente Revenga, M.2    Widersten, M.3
  • 35
    • 77954358041 scopus 로고    scopus 로고
    • Modification of substrate specificity resulted in an epoxide hydrolase with shifted enantiopreference for (2,3-epoxypropyl)benzene
    • Gurell A., Widersten M. Modification of substrate specificity resulted in an epoxide hydrolase with shifted enantiopreference for (2,3-epoxypropyl)benzene. ChemBioChem 2010, 11:1422-1429.
    • (2010) ChemBioChem , vol.11 , pp. 1422-1429
    • Gurell, A.1    Widersten, M.2
  • 36
    • 84866723266 scopus 로고    scopus 로고
    • Obtaining optical purity for product diols in enzyme-catalyzed epoxide hydrolysis: contributions from changes in both enantio- and regioselectivity
    • Janfalk Carlsson Å., Bauer P., Ma H., Widersten M. Obtaining optical purity for product diols in enzyme-catalyzed epoxide hydrolysis: contributions from changes in both enantio- and regioselectivity. Biochemistry 2012, 51:7627-7637.
    • (2012) Biochemistry , vol.51 , pp. 7627-7637
    • Janfalk Carlsson, Å.1    Bauer, P.2    Ma, H.3    Widersten, M.4
  • 37
    • 80052884406 scopus 로고    scopus 로고
    • Laboratory evolution of an epoxide hydrolase - towards an enantioconvergent biocatalyst
    • Kotik M., Archelas A., Faměrová V., Oubrechtová P., Křen V. Laboratory evolution of an epoxide hydrolase - towards an enantioconvergent biocatalyst. J Biotechnol 2011, 156:1-10.
    • (2011) J Biotechnol , vol.156 , pp. 1-10
    • Kotik, M.1    Archelas, A.2    Faměrová, V.3    Oubrechtová, P.4    Křen, V.5
  • 38
    • 4644259619 scopus 로고    scopus 로고
    • Enzymatic transformations. Part 58. Enantioconvergent biohydrolysis of styrene oxide derivatives catalysed by the Solanum tuberosum epoxide hydrolase
    • Monterde M.I., Lombard M., Archelas A., Cronin A., Arand M., Furstoss R. Enzymatic transformations. Part 58. Enantioconvergent biohydrolysis of styrene oxide derivatives catalysed by the Solanum tuberosum epoxide hydrolase. Tetrahedron Assym 2004, 15:2801-2805.
    • (2004) Tetrahedron Assym , vol.15 , pp. 2801-2805
    • Monterde, M.I.1    Lombard, M.2    Archelas, A.3    Cronin, A.4    Arand, M.5    Furstoss, R.6
  • 39
    • 84891886130 scopus 로고    scopus 로고
    • Heterologous overexpression of Vigna radiata epoxide hydrolase in Escherichia coli and its catalytic performance in enantioconvergent hydrolysis of p-nitrostyrene oxide into (R)-p-nitrophenyl glycol
    • Zhu Q.Q., He W.H., Kong X.D., Fan L.Q., Zhao J., Li S.X., Xu J.H. Heterologous overexpression of Vigna radiata epoxide hydrolase in Escherichia coli and its catalytic performance in enantioconvergent hydrolysis of p-nitrostyrene oxide into (R)-p-nitrophenyl glycol. Appl Microbiol Biotechnol 2014, 98:207-218.
    • (2014) Appl Microbiol Biotechnol , vol.98 , pp. 207-218
    • Zhu, Q.Q.1    He, W.H.2    Kong, X.D.3    Fan, L.Q.4    Zhao, J.5    Li, S.X.6    Xu, J.H.7
  • 40
    • 79960895883 scopus 로고    scopus 로고
    • Site-directed mutagenesis of epoxide hydrolase to probe catalytic amino acid residues and reaction mechanism
    • Pan H., Xie Z., Bao W., Cheng Y., Zhang J., Li Y. Site-directed mutagenesis of epoxide hydrolase to probe catalytic amino acid residues and reaction mechanism. FEBS Lett 2011, 585:2545-2550.
    • (2011) FEBS Lett , vol.585 , pp. 2545-2550
    • Pan, H.1    Xie, Z.2    Bao, W.3    Cheng, Y.4    Zhang, J.5    Li, Y.6
  • 41
    • 84862278505 scopus 로고    scopus 로고
    • Active site analysis of cis-epoxysuccinate hydrolase from Nocardia tartaricans using homology modeling and site-directed mutagenesis
    • Vasu V., Kumaresan J., Ganesh Babu M., Meenakshisundaram S. Active site analysis of cis-epoxysuccinate hydrolase from Nocardia tartaricans using homology modeling and site-directed mutagenesis. Appl Microbiol Biotechnol 2012, 93:2377-2386.
    • (2012) Appl Microbiol Biotechnol , vol.93 , pp. 2377-2386
    • Vasu, V.1    Kumaresan, J.2    Ganesh Babu, M.3    Meenakshisundaram, S.4
  • 42
    • 84878885779 scopus 로고    scopus 로고
    • Purification and characterization of a cis-epoxysuccinic acid hydrolase from Nocardia tartaricans CAS-52, and expression in Escherichia coli
    • Wang Z., Wang Y., Su Z. Purification and characterization of a cis-epoxysuccinic acid hydrolase from Nocardia tartaricans CAS-52, and expression in Escherichia coli. Appl Microbiol Biotechnol 2013, 97:2433-2441.
    • (2013) Appl Microbiol Biotechnol , vol.97 , pp. 2433-2441
    • Wang, Z.1    Wang, Y.2    Su, Z.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.