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Volumn 6, Issue , 2015, Pages 319-345

Biocatalysis: A Status Report

Author keywords

biocatalyst; enzyme; protein engineering; stabilization

Indexed keywords

BIOCATALYSTS; BIOCHEMICAL ENGINEERING; CATALYSIS; GENETIC ENGINEERING; PROTEINS; STABILIZATION;

EID: 84938796452     PISSN: 19475438     EISSN: None     Source Type: Journal    
DOI: 10.1146/annurev-chembioeng-061114-123415     Document Type: Article
Times cited : (131)

References (110)
  • 1
    • 68049106179 scopus 로고    scopus 로고
    • Directed evolution drives the next generation of biocatalysts
    • Turner NJ. 2009. Directed evolution drives the next generation of biocatalysts. Nat. Chem. Biol. 5:568-74
    • (2009) Nat. Chem. Biol. , vol.5 , pp. 568-574
    • Turner, N.J.1
  • 3
    • 84883272014 scopus 로고    scopus 로고
    • Biocatalysis in organic chemistry and biotechnology: Past, present, and future
    • Reetz MT. 2013. Biocatalysis in organic chemistry and biotechnology: past, present, and future. J. Am. Chem. Soc. 135:12480-96
    • (2013) J. Am. Chem. Soc. , vol.135 , pp. 12480-12496
    • Reetz, M.T.1
  • 4
    • 0022730806 scopus 로고
    • The structure of the mouse glutathione-peroxidase gene: The selenocysteine in the active-site is encoded by the 'termination' codon, TGA
    • Chambers I, Frampton J, Goldfarb P, Affara N, McBain W, Harrison PR. 1986. The structure of the mouse glutathione-peroxidase gene: the selenocysteine in the active-site is encoded by the 'termination' codon, TGA. EMBO J. 5:1221-27
    • (1986) EMBO J. , vol.5 , pp. 1221-1227
    • Chambers, I.1    Frampton, J.2    Goldfarb, P.3    Affara, N.4    McBain, W.5    Harrison, P.R.6
  • 5
    • 0001256080 scopus 로고
    • Nucleotide-sequence and expression of the selenocysteine-containing polypeptide of formate dehydrogenase (formate-hydrogen-lyase-linked) from Escherichia coli
    • Zinoni F, Birkmann A, Stadtman TC, Bock A. 1986. Nucleotide-sequence and expression of the selenocysteine-containing polypeptide of formate dehydrogenase (formate-hydrogen-lyase-linked) from Escherichia coli. Proc. Natl. Acad. Sci. USA 83:4650-54
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 4650-4654
    • Zinoni, F.1    Birkmann, A.2    Stadtman, T.C.3    Bock, A.4
  • 6
    • 0037166006 scopus 로고    scopus 로고
    • Pyrrolysine encoded by UAG in Archaea: Charging of a UAG-decoding specialized tRNA
    • Srinivasan G, James CM, Krzycki JA. 2002. Pyrrolysine encoded by UAG in Archaea: charging of a UAG-decoding specialized tRNA. Science 296:1459-62
    • (2002) Science , vol.296 , pp. 1459-1462
    • Srinivasan, G.1    James, C.M.2    Krzycki, J.A.3
  • 7
  • 8
    • 80053013322 scopus 로고    scopus 로고
    • Noncanonical amino acids in the interrogation of cellular protein synthesis
    • Ngo JT, Tirrell DA. 2011. Noncanonical amino acids in the interrogation of cellular protein synthesis. Acc. Chem. Res. 44:677-85
    • (2011) Acc. Chem. Res. , vol.44 , pp. 677-685
    • Ngo, J.T.1    Tirrell, D.A.2
  • 10
    • 84902209981 scopus 로고    scopus 로고
    • Bringing dynamic molecular machines into focus by methyl-TROSY NMR
    • Rosenzweig R, Kay LE. 2014. Bringing dynamic molecular machines into focus by methyl-TROSY NMR. Annu. Rev. Biochem. 83:291-15
    • (2014) Annu. Rev. Biochem. , vol.83 , pp. 291-315
    • Rosenzweig, R.1    Kay, L.E.2
  • 11
    • 0031765407 scopus 로고    scopus 로고
    • Total synthesis of solanapyrone A via enzymatic Diels-Alder reaction of prosolanapyrone
    • Oikawa H, Kobayashi T, Katayama K, Suzuki Y, Ichihara A. 1998. Total synthesis of solanapyrone A via enzymatic Diels-Alder reaction of prosolanapyrone. J. Organ. Chem. 63:8748-56
    • (1998) J. Organ. Chem. , vol.63 , pp. 8748-8756
    • Oikawa, H.1    Kobayashi, T.2    Katayama, K.3    Suzuki, Y.4    Ichihara, A.5
  • 12
    • 33846828574 scopus 로고    scopus 로고
    • Enzyme promiscuity: First protein-catalyzed Morita-Baylis-Hillman reaction
    • Reetz MT, Mondiere R, Carballeira JD. 2007. Enzyme promiscuity: first protein-catalyzed Morita-Baylis-Hillman reaction. Tetrahedron Lett. 48:1679-81
    • (2007) Tetrahedron Lett. , vol.48 , pp. 1679-1681
    • Reetz, M.T.1    Mondiere, R.2    Carballeira, J.D.3
  • 15
    • 84872495336 scopus 로고    scopus 로고
    • Olefin cyclopropanation via carbene transfer catalyzed by engineered cytochrome P450 enzymes
    • Coelho PS, Brustad EM, Kannan A, Arnold FH. 2013. Olefin cyclopropanation via carbene transfer catalyzed by engineered cytochrome P450 enzymes. Science 339:307-10
    • (2013) Science , vol.339 , pp. 307-310
    • Coelho, P.S.1    Brustad, E.M.2    Kannan, A.3    Arnold, F.H.4
  • 17
  • 18
    • 0034812536 scopus 로고    scopus 로고
    • The lesser burden borne by o-succinylbenzoate synthase: An easy reaction involving a carboxylate carbon acid
    • Taylor EA, Palmer DRJ, Gerlt JA. 2001. The lesser burden borne by o-succinylbenzoate synthase: an easy reaction involving a carboxylate carbon acid. J. Am. Chem. Soc. 123:5824-25
    • (2001) J. Am. Chem. Soc. , vol.123 , pp. 5824-5825
    • Taylor, E.A.1    Palmer, D.R.J.2    Gerlt, J.A.3
  • 19
    • 0035543093 scopus 로고    scopus 로고
    • The depth of chemical time and the power of enzymes as catalysts
    • Wolfenden R, Snider MJ. 2001. The depth of chemical time and the power of enzymes as catalysts. Acc. Chem. Res. 34:938-45
    • (2001) Acc. Chem. Res. , vol.34 , pp. 938-945
    • Wolfenden, R.1    Snider, M.J.2
  • 20
    • 59649089569 scopus 로고    scopus 로고
    • Molecular determinants of the regioselectivity of toluene/o-xylene monooxygenase from Pseudomonas sp
    • Notomista E, Cafaro V, Bozza G, Di Donato A. 2009. Molecular determinants of the regioselectivity of toluene/o-xylene monooxygenase from Pseudomonas sp. strain OX1. Appl. Environ. Microbiol. 75:823-36
    • (2009) Strain OX1. Appl. Environ. Microbiol. , vol.75 , pp. 823-836
    • Notomista, E.1    Cafaro, V.2    Bozza, G.3    Di Donato, A.4
  • 21
    • 0033969462 scopus 로고    scopus 로고
    • Characterization of hydroxylaminobenzenemutase from pNBZ139 cloned from Pseudomonas pseudoalcaligenes JS45
    • He ZQ,Nadeau LJ, Spain JC. 2000. Characterization of hydroxylaminobenzenemutase from pNBZ139 cloned from Pseudomonas pseudoalcaligenes JS45. Eur. J. Biochem. 267:1110-16
    • (2000) Eur. J. Biochem. , vol.267 , pp. 1110-1116
    • He, Z.Q.1    Nadeau, L.J.2    Spain, J.C.3
  • 22
    • 77956928315 scopus 로고    scopus 로고
    • Altering the regioselectivity of cytochrome P450 BM-3 by saturation mutagenesis for the biosynthesis of indirubin
    • Hu S, Huang J, Mei LH, Yu Q, Yao SJ, Jin ZH. 2010. Altering the regioselectivity of cytochrome P450 BM-3 by saturation mutagenesis for the biosynthesis of indirubin. J. Mol. Catal. B: Enzymatic 67:29-35
    • (2010) J. Mol. Catal. B: Enzymatic , vol.67 , pp. 29-35
    • Hu, S.1    Huang, J.2    Mei, L.H.3    Yu, Q.4    Yao, S.J.5    Jin, Z.H.6
  • 23
    • 33845183768 scopus 로고
    • Kinetic resolution of unnatural and rarely occurring amino acids: Enantioselective hydrolysis of N-acyl amino acids catalyzed by acylase i
    • Chenault HK, Dahmer J, Whitesides GM. 1989. Kinetic resolution of unnatural and rarely occurring amino acids: enantioselective hydrolysis of N-acyl amino acids catalyzed by acylase I. J. Am. Chem. Soc. 111:6354-64
    • (1989) J. Am. Chem. Soc. , vol.111 , pp. 6354-6364
    • Chenault, H.K.1    Dahmer, J.2    Whitesides, G.M.3
  • 24
    • 84873346530 scopus 로고    scopus 로고
    • Laboratory evolution of enantiocomplementary Candida antarctica lipase B mutants with broad substrate scope
    • Wu Q, Soni P, Reetz MT. 2013. Laboratory evolution of enantiocomplementary Candida antarctica lipase B mutants with broad substrate scope. J. Am. Chem. Soc. 135:1872-81
    • (2013) J. Am. Chem. Soc. , vol.135 , pp. 1872-1881
    • Wu, Q.1    Soni, P.2    Reetz, M.T.3
  • 25
    • 33744475011 scopus 로고    scopus 로고
    • Directed evolution of enantioselective enzymes: Iterative cycles of CASTing for probing protein-sequence space
    • ReetzMT, Wang LW, BocolaM. 2006. Directed evolution of enantioselective enzymes: iterative cycles of CASTing for probing protein-sequence space. Angew. Chem. Int. Ed. 45:1236-41
    • (2006) Angew. Chem. Int. Ed. , vol.45 , pp. 1236-1241
    • Reetz, M.T.1    Wang, L.W.2    Bocola, M.3
  • 27
    • 84879209057 scopus 로고    scopus 로고
    • The evolution of an amine dehydrogenase biocatalyst for the asymmetric production of chiral amines
    • AbrahamsonMJ, Wong JW, Bommarius AS. 2013. The evolution of an amine dehydrogenase biocatalyst for the asymmetric production of chiral amines. Adv. Synth. Catal. 355:1780-86
    • (2013) Adv. Synth. Catal. , vol.355 , pp. 1780-1786
    • Abrahamson, M.J.1    Wong, J.W.2    Bommarius, A.S.3
  • 28
    • 54349090614 scopus 로고    scopus 로고
    • Addressing the numbers problem in directed evolution
    • Reetz MT, Kahakeaw D, Lohmer R. 2008. Addressing the numbers problem in directed evolution. ChemBioChem 9:1797-804
    • (2008) ChemBioChem , vol.9 , pp. 1797-1804
    • Reetz, M.T.1    Kahakeaw, D.2    Lohmer, R.3
  • 29
    • 22144485602 scopus 로고    scopus 로고
    • Expanding the range of substrate acceptance of enzymes: Combinatorial active-site saturation test
    • ReetzMT, Bocola M, Carballeira JD, Zha DX, Vogel A. 2005. Expanding the range of substrate acceptance of enzymes: combinatorial active-site saturation test. Angew. Chem. Int. Ed. 44:4192-96
    • (2005) Angew. Chem. Int. Ed. , vol.44 , pp. 4192-4196
    • Reetz, M.T.1    Bocola, M.2    Carballeira, J.D.3    Zha, D.X.4    Vogel, A.5
  • 30
    • 78149432825 scopus 로고    scopus 로고
    • Laboratory evolution of stereoselective enzymes: A prolific source of catalysts for asymmetric reactions
    • Reetz MT. 2011. Laboratory evolution of stereoselective enzymes: a prolific source of catalysts for asymmetric reactions. Angew. Chem. Int. Ed. 50:138-74
    • (2011) Angew. Chem. Int. Ed. , vol.50 , pp. 138-174
    • Reetz, M.T.1
  • 31
    • 34248567845 scopus 로고    scopus 로고
    • Iterative saturation mutagenesis (ISM) for rapid directed evolution of functional enzymes
    • Reetz MT, Carballeira JD. 2007. Iterative saturation mutagenesis (ISM) for rapid directed evolution of functional enzymes. Nat. Protoc. 2:891-903
    • (2007) Nat. Protoc. , vol.2 , pp. 891-903
    • Reetz, M.T.1    Carballeira, J.D.2
  • 32
    • 0035650018 scopus 로고    scopus 로고
    • Comparison of different chemoenzymatic process routes to enantiomerically pure amino acids
    • Bommarius AS, Schwarm M, Drauz K. 2001. Comparison of different chemoenzymatic process routes to enantiomerically pure amino acids. Chimia 55:50-59
    • (2001) Chimia , vol.55 , pp. 50-59
    • Bommarius, A.S.1    Schwarm, M.2    Drauz, K.3
  • 33
    • 0033423330 scopus 로고    scopus 로고
    • Biocatalysis at commercial scale:myths and realities
    • Rozzell JD. 1999. Biocatalysis at commercial scale:myths and realities. Chim. Oggi-Chem. Today 17:42-47
    • (1999) Chim. Oggi-Chem. Today , vol.17 , pp. 42-47
    • Rozzell, J.D.1
  • 35
    • 0001002352 scopus 로고
    • Conformation changes of proteins
    • Lumry R, Eyring H. 1954. Conformation changes of proteins. J. Phys. Chem. 58:110-20
    • (1954) J. Phys. Chem. , vol.58 , pp. 110-120
    • Lumry, R.1    Eyring, H.2
  • 36
    • 76549099302 scopus 로고    scopus 로고
    • Utilizing simple biochemical measurements to predict lifetime output of biocatalysts in continuous isothermal processes
    • Rogers TA, Bommarius AS. 2010. Utilizing simple biochemical measurements to predict lifetime output of biocatalysts in continuous isothermal processes. Chem. Eng. Sci. 65:2118-24
    • (2010) Chem. Eng. Sci. , vol.65 , pp. 2118-2124
    • Rogers, T.A.1    Bommarius, A.S.2
  • 37
    • 34248596352 scopus 로고    scopus 로고
    • Catalytic efficiency and kcat/KM: A useful comparator?
    • Eisenthal R, Danson MJ, Hough DW. 2007. Catalytic efficiency and kcat/KM: a useful comparator? Trends Biotechnol. 25:247-49
    • (2007) Trends Biotechnol. , vol.25 , pp. 247-249
    • Eisenthal, R.1    Danson, M.J.2    Hough, D.W.3
  • 39
    • 60349127519 scopus 로고    scopus 로고
    • Catalytic effectiveness, a measure of enzyme proficiency for industrial applications
    • Fox RJ, Clay MD. 2009. Catalytic effectiveness, a measure of enzyme proficiency for industrial applications. Trends Biotechnol. 27:137-40
    • (2009) Trends Biotechnol. , vol.27 , pp. 137-140
    • Fox, R.J.1    Clay, M.D.2
  • 41
    • 0036289574 scopus 로고    scopus 로고
    • Protein building blocks preserved by recombination, Nature Struct
    • Voigt CA, Martinez C, Wang Z-G, Mayo SL, Arnold FH. 2002. Protein building blocks preserved by recombination, Nature Struct. Biol. 9:553-58
    • (2002) Biol. , vol.9 , pp. 553-558
    • Voigt, C.A.1    Martinez, C.2    Wang, Z.-G.3    Mayo, S.L.4    Arnold, F.H.5
  • 43
    • 65249175725 scopus 로고    scopus 로고
    • A family of thermostable fungal cellulases created by structure-guided recombination
    • Heinzelman P, Snow CD, Wu I, Nguyen C, Villalobos A, et al. 2009. A family of thermostable fungal cellulases created by structure-guided recombination. Proc. Natl. Acad. Sci. USA 106:5610-15
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 5610-5615
    • Heinzelman, P.1    Snow, C.D.2    Wu, I.3    Nguyen, C.4    Villalobos, A.5
  • 44
    • 70350351556 scopus 로고    scopus 로고
    • SCHEMArecombination of a fungal cellulase uncovers a single mutation that contributes markedly to stability
    • Heinzelman P, SnowCD, SmithMA, Yu XL,Kannan A, et al. 2009. SCHEMArecombination of a fungal cellulase uncovers a single mutation that contributes markedly to stability. J. Biol. Chem. 284:26229-33
    • (2009) J. Biol. Chem. , vol.284 , pp. 26229-26233
    • Heinzelman, P.1    Snow, C.D.2    Smith, M.A.3    Yu, X.L.4    Kannan, A.5
  • 45
    • 77958179580 scopus 로고    scopus 로고
    • Efficient screening of fungal cellobiohydrolase class i enzymes for thermostabilizing sequence blocks by SCHEMA structure-guided recombination
    • Heinzelman P, Komor R, Kanaan A, Romero P, Yu XL, et al. 2010. Efficient screening of fungal cellobiohydrolase class I enzymes for thermostabilizing sequence blocks by SCHEMA structure-guided recombination. Protein Eng. Des. Select. 23:871-80
    • (2010) Protein Eng. Des. Select. , vol.23 , pp. 871-880
    • Heinzelman, P.1    Komor, R.2    Kanaan, A.3    Romero, P.4    Yu, X.L.5
  • 46
    • 84861158254 scopus 로고    scopus 로고
    • Approaches for improving thermostability characteristics in cellulases
    • Anbar M, Bayer EA. 2012. Approaches for improving thermostability characteristics in cellulases. Cellulases 510:261-71
    • (2012) Cellulases , vol.510 , pp. 261-271
    • Anbar, M.1    Bayer, E.A.2
  • 47
    • 0028111743 scopus 로고
    • Sequence statistics reliably predict stabilizing mutations in a protein domain
    • Steipe B, Schiller B, Pluckthun A, Steinbacher S. 1994. Sequence statistics reliably predict stabilizing mutations in a protein domain. J. Mol. Biol. 240:188-92
    • (1994) J. Mol. Biol. , vol.240 , pp. 188-192
    • Steipe, B.1    Schiller, B.2    Pluckthun, A.3    Steinbacher, S.4
  • 49
    • 0036271498 scopus 로고    scopus 로고
    • The consensus concept for thermostability engineering of proteins: Further proof of concept
    • Lehmann M, Loch C, Middendorf A, Studer D, Lassen SF, et al. 2002. The consensus concept for thermostability engineering of proteins: further proof of concept. Protein Eng. 15:403-11
    • (2002) Protein Eng. , vol.15 , pp. 403-411
    • Lehmann, M.1    Loch, C.2    Middendorf, A.3    Studer, D.4    Lassen, S.F.5
  • 50
    • 14644390952 scopus 로고    scopus 로고
    • Construction of stabilized proteins by combinatorial consensus mutagenesis
    • Amin N, Liu AD, Ramer S, Aehle W, Meijer D, et al. 2004. Construction of stabilized proteins by combinatorial consensus mutagenesis. Protein Eng. Des. Sel. 17:787-93
    • (2004) Protein Eng. Des. Sel. , vol.17 , pp. 787-793
    • Amin, N.1    Liu, A.D.2    Ramer, S.3    Aehle, W.4    Meijer, D.5
  • 51
    • 54249164978 scopus 로고    scopus 로고
    • Thermostable variants constructed via the structure-guided consensus method also show increased stability in salts solutions and homogeneous aqueous-organic media
    • Vazquez-Figueroa E, Yeh V, Broering JM, Chaparro-Riggers JF, Bommarius AS. 2008. Thermostable variants constructed via the structure-guided consensus method also show increased stability in salts solutions and homogeneous aqueous-organic media. Protein Eng. Des. Sel. 21:673-80
    • (2008) Protein Eng. Des. Sel. , vol.21 , pp. 673-680
    • Vazquez-Figueroa, E.1    Yeh, V.2    Broering, J.M.3    Chaparro-Riggers, J.F.4    Bommarius, A.S.5
  • 53
    • 70350110646 scopus 로고    scopus 로고
    • Creation of an amino acid network of structurally coupled residues in the directed evolution of a thermostable enzyme
    • Reetz MT, Soni P, Acevedo JP, Sanchis J. 2009. Creation of an amino acid network of structurally coupled residues in the directed evolution of a thermostable enzyme. Angew. Chem. Int. Ed. 48:8268-72
    • (2009) Angew. Chem. Int. Ed. , vol.48 , pp. 8268-8272
    • Reetz, M.T.1    Soni, P.2    Acevedo, J.P.3    Sanchis, J.4
  • 54
    • 84864073832 scopus 로고    scopus 로고
    • Improved thermostability of AEH by combining B-FIT analysis and structure-guided consensus method
    • Blum JK, Ricketts MD, Bommarius AS. 2012. Improved thermostability of AEH by combining B-FIT analysis and structure-guided consensus method. J. Biotechnol. 160:214-21
    • (2012) J. Biotechnol. , vol.160 , pp. 214-221
    • Blum, J.K.1    Ricketts, M.D.2    Bommarius, A.S.3
  • 57
    • 0031280508 scopus 로고    scopus 로고
    • Thermophilic proteins: Stability and function in aqueous and organic solvents
    • Cowan DA. 1997. Thermophilic proteins: stability and function in aqueous and organic solvents. Comp. Biochem. Physiol.-Mol. Integr. Physiol. 118:429-38
    • (1997) Comp. Biochem. Physiol.-Mol. Integr. Physiol. , vol.118 , pp. 429-438
    • Cowan, D.A.1
  • 58
    • 0024726863 scopus 로고
    • Correlation between microbial protein thermostability and resistance to denaturation in aqueous-organic solvent 2-phase systems
    • Owusu RK, Cowan DA. 1989. Correlation between microbial protein thermostability and resistance to denaturation in aqueous-organic solvent 2-phase systems. Enzyme Microb. Technol. 11:568-74
    • (1989) Enzyme Microb. Technol. , vol.11 , pp. 568-574
    • Owusu, R.K.1    Cowan, D.A.2
  • 59
    • 18044366809 scopus 로고    scopus 로고
    • A thermostable variant of fructose bisphosphate aldolase constructed by directed evolution also shows increased stability in organic solvents
    • Hao JJ, Berry A. 2004. A thermostable variant of fructose bisphosphate aldolase constructed by directed evolution also shows increased stability in organic solvents. Protein Eng. Des. Sel. 17:689-97
    • (2004) Protein Eng. Des. Sel. , vol.17 , pp. 689-697
    • Hao, J.J.1    Berry, A.2
  • 60
    • 78149450306 scopus 로고    scopus 로고
    • Increasing the stability of an enzyme toward hostile organic solvents by directed evolution based on iterative saturation mutagenesis using the B-FIT method
    • ReetzMT, Soni P, Fernandez L,Gumulya Y, Carballeira JD. 2010. Increasing the stability of an enzyme toward hostile organic solvents by directed evolution based on iterative saturation mutagenesis using the B-FIT method. Chem. Commun. 46:8657-58
    • (2010) Chem. Commun. , vol.46 , pp. 8657-8658
    • Reetz, M.T.1    Soni, P.2    Fernandez, L.3    Gumulya, Y.4    Carballeira, J.D.5
  • 61
    • 76649087954 scopus 로고    scopus 로고
    • Biocatalysis with thermostable enzymes: Structure and properties of a thermophilic 'ene'-reductase related to old yellow enzyme
    • Adalbjörnsson BV, Toogood HS, Fryszkowska A, Pudney CR, Jowitt TA, et al. 2010. Biocatalysis with thermostable enzymes: structure and properties of a thermophilic 'ene'-reductase related to old yellow enzyme. ChemBioChem 11:197-207
    • (2010) ChemBioChem , vol.11 , pp. 197-207
    • Adalbjörnsson, B.V.1    Toogood, H.S.2    Fryszkowska, A.3    Pudney, C.R.4    Jowitt, T.A.5
  • 62
    • 33751167596 scopus 로고    scopus 로고
    • Improved stabilization of microencapsulated Cathepsin B in harsh conditions
    • Sharma S, Mittal A, Gupta VK, Singh H. 2007. Improved stabilization of microencapsulated Cathepsin B in harsh conditions. Enzyme Microb. Technol. 40:337-42
    • (2007) Enzyme Microb. Technol. , vol.40 , pp. 337-342
    • Sharma, S.1    Mittal, A.2    Gupta, V.K.3    Singh, H.4
  • 63
    • 0034011107 scopus 로고    scopus 로고
    • Stabilization of NAD-dependent formate dehydrogenase from Candida boidinii by site-directedmutagenesis of cysteine residues
    • Slusarczyk H, Felber S, Kula MR, Pohl M. 2000. Stabilization of NAD-dependent formate dehydrogenase from Candida boidinii by site-directedmutagenesis of cysteine residues. Eur. J. Biochem. 267:1280-89
    • (2000) Eur. J. Biochem. , vol.267 , pp. 1280-1289
    • Slusarczyk, H.1    Felber, S.2    Kula, M.R.3    Pohl, M.4
  • 64
    • 28844501226 scopus 로고    scopus 로고
    • Deactivation of formate dehydrogenase (FDH) in solution and at gasliquid interfaces
    • Bommarius AS, Karau A. 2005. Deactivation of formate dehydrogenase (FDH) in solution and at gasliquid interfaces. Biotechnol. Prog. 21:1663-72
    • (2005) Biotechnol. Prog. , vol.21 , pp. 1663-1672
    • Bommarius, A.S.1    Karau, A.2
  • 66
    • 80051682587 scopus 로고    scopus 로고
    • A stereoselective inverting sec-alkylsulfatase for the deracemization of sec-alcohols
    • Schober M, Gadler P, Knaus T, Kayer H, Birner-Grunberger R, et al. 2011. A stereoselective inverting sec-alkylsulfatase for the deracemization of sec-alcohols. Org. Lett. 13:4296-99
    • (2011) Org. Lett. , vol.13 , pp. 4296-4299
    • Schober, M.1    Gadler, P.2    Knaus, T.3    Kayer, H.4    Birner-Grunberger, R.5
  • 68
    • 84874834871 scopus 로고    scopus 로고
    • One-pot deracemization of secalcohols: Enantioconvergent enzymatic hydrolysis of alkyl sulfates using stereocomplementary sulfatases
    • SchoberM, ToeschM, Knaus T, Strohmeier GA, van Loo B, et al. 2013. One-pot deracemization of secalcohols: enantioconvergent enzymatic hydrolysis of alkyl sulfates using stereocomplementary sulfatases. Angew. Chem. Int. Ed. 52:3277-79
    • (2013) Angew. Chem. Int. Ed. , vol.52 , pp. 3277-3279
    • Schober, M.1    Toesch, M.2    Knaus, T.3    Strohmeier, G.A.4    Van Loo, B.5
  • 69
    • 53749094146 scopus 로고    scopus 로고
    • Biocatalytic cleavage of alkenes with O2 and Trametes hirsuta G FCC 047
    • Lara M, Mutti FG, Glueck SM, Kroutil W. 2008. Biocatalytic cleavage of alkenes with O2 and Trametes hirsuta G FCC 047. Eur. J. Organ. Chem. 2008(21):3668-72
    • (2008) Eur. J. Organ. Chem. , vol.2008 , Issue.21 , pp. 3668-3672
    • Lara, M.1    Mutti, F.G.2    Glueck, S.M.3    Kroutil, W.4
  • 70
    • 84938769508 scopus 로고    scopus 로고
    • Biocatalytic cleavage of alkenes with oxygen and Trametes hirsuta G FCC047
    • ed. J. Whittall, P. Sutton,. West Sussex, UK:Wiley. 388 pp
    • Rajagopalan A, Mutti FG, Kroutil W. 2012. Biocatalytic cleavage of alkenes with oxygen and Trametes hirsuta G FCC047. In PracticalMethods for Biocatalysis and Biotransformations 2, ed. J. Whittall, P. Sutton, pp. 199-202. West Sussex, UK:Wiley. 388 pp.
    • (2012) PracticalMethods for Biocatalysis and Biotransformations 2 , pp. 199-202
    • Rajagopalan, A.1    Mutti, F.G.2    Kroutil, W.3
  • 71
    • 67849122416 scopus 로고    scopus 로고
    • Oxidative enzymatic alkene cleavage: Indications for a nonclassical enzyme mechanism
    • Lara M, Mutti FG, Glueck SM, Kroutil W. 2009. Oxidative enzymatic alkene cleavage: indications for a nonclassical enzyme mechanism. J. Am. Chem. Soc. 131:5368-69
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 5368-5369
    • Lara, M.1    Mutti, F.G.2    Glueck, S.M.3    Kroutil, W.4
  • 72
    • 84890118106 scopus 로고    scopus 로고
    • Enzymatic aerobic alkene cleavage catalyzed by a Mn3+-dependent proteinase A homologue
    • Rajagopalan A, SchoberM,Emmerstorfer A, HammererL,Migglautsch A, et al. 2013. Enzymatic aerobic alkene cleavage catalyzed by a Mn3+-dependent proteinase A homologue. ChemBioChem 14:2427-30
    • (2013) ChemBioChem , vol.14 , pp. 2427-2430
    • Rajagopalan, A.1    Schober, M.2    Emmerstorfer, A.3    Hammerer, L.4    Migglautsch, A.5
  • 73
    • 84864700906 scopus 로고    scopus 로고
    • Catalytic and structural role of a conserved active site histidine in berberine bridge enzyme
    • Wallner S, Winkler A, Riedl S, Dully C, Horvath S, et al. 2012. Catalytic and structural role of a conserved active site histidine in berberine bridge enzyme. Biochemistry 51:6139-47
    • (2012) Biochemistry , vol.51 , pp. 6139-6147
    • Wallner, S.1    Winkler, A.2    Riedl, S.3    Dully, C.4    Horvath, S.5
  • 75
    • 80052788484 scopus 로고    scopus 로고
    • Biocatalytic oxidative C-C bond formation catalysed by the berberine bridge enzyme: Optimal reaction conditions
    • Resch V, Schrittwieser JH, Wallner S, Macheroux P, Kroutil W. 2011. Biocatalytic oxidative C-C bond formation catalysed by the berberine bridge enzyme: optimal reaction conditions. Adv. Synth. Catal. 353:2377-83
    • (2011) Adv. Synth. Catal. , vol.353 , pp. 2377-2383
    • Resch, V.1    Schrittwieser, J.H.2    Wallner, S.3    Macheroux, P.4    Kroutil, W.5
  • 77
    • 84880831531 scopus 로고    scopus 로고
    • Engineering an enantioselective amine oxidase for the synthesis of pharmaceutical building blocks and alkaloid natural products
    • Ghislieri D, Green AP, Pontini M, Willies SC, Rowles I, et al. 2013. Engineering an enantioselective amine oxidase for the synthesis of pharmaceutical building blocks and alkaloid natural products. J. Am. Chem. Soc. 135:10863-69
    • (2013) J. Am. Chem. Soc. , vol.135 , pp. 10863-10869
    • Ghislieri, D.1    Green, A.P.2    Pontini, M.3    Willies, S.C.4    Rowles, I.5
  • 78
    • 56949104426 scopus 로고    scopus 로고
    • The structure of monoamine oxidase from Aspergillus Niger provides a molecular context for improvements in activity obtained by directed evolution
    • Atkin KE, Reiss R, Koehler V, Bailey KR, Hart S, et al. 2008. The structure of monoamine oxidase from Aspergillus niger provides a molecular context for improvements in activity obtained by directed evolution. J. Mol. Biol. 384:1218-31
    • (2008) J. Mol. Biol. , vol.384 , pp. 1218-1231
    • Atkin, K.E.1    Reiss, R.2    Koehler, V.3    Bailey, K.R.4    Hart, S.5
  • 79
    • 34147177502 scopus 로고    scopus 로고
    • Enantioselective oxidation of O-methyl-N-hydroxylamines using monoamine oxidase N as catalyst
    • Eve TSC,Wells A, Turner NJ. 2007. Enantioselective oxidation of O-methyl-N-hydroxylamines using monoamine oxidase N as catalyst. Chem. Commun. 2007(15):1530-31
    • (2007) Chem. Commun. , vol.2007 , Issue.15 , pp. 1530-1531
    • Eve, T.S.C.1    Wells, A.2    Turner, N.J.3
  • 81
    • 77958485628 scopus 로고    scopus 로고
    • A highly efficient synthesis of telaprevir by strategic use of biocatalysis and multicomponent reactions
    • Znabet A, Polak MM, Janssen E, de Kanter FJJ, Turner NJ, et al. 2010. A highly efficient synthesis of telaprevir by strategic use of biocatalysis and multicomponent reactions. Chem. Commun. 46:7918-20
    • (2010) Chem. Commun. , vol.46 , pp. 7918-7920
    • Znabet, A.1    Polak, M.M.2    Janssen, E.3    De Kanter, F.J.J.4    Turner, N.J.5
  • 82
    • 84894450875 scopus 로고    scopus 로고
    • A regio-and stereoselective w-transaminase/monoamine oxidase cascade for the synthesis of chiral 2,5-disubstituted pyrrolidines
    • O'Reilly E, Iglesias C, Ghislieri D, Hopwood J, Galman JL, et al. 2014. A regio-and stereoselective w-transaminase/monoamine oxidase cascade for the synthesis of chiral 2,5-disubstituted pyrrolidines. Angew. Chem. Int. Ed. 53:2447-50
    • (2014) Angew. Chem. Int. Ed. , vol.53 , pp. 2447-2450
    • O'Reilly, E.1    Iglesias, C.2    Ghislieri, D.3    Hopwood, J.4    Galman, J.L.5
  • 83
    • 34250862807 scopus 로고    scopus 로고
    • Key green chemistry research areas-A perspective from pharmaceutical manufacturers
    • Constable DJC, Dunn PJ, Hayler JD, Humphrey GR, Leazer JL, et al. 2007. Key green chemistry research areas-a perspective from pharmaceutical manufacturers. Green Chem. 9:411-20
    • (2007) Green Chem. , vol.9 , pp. 411-420
    • Constable, D.J.C.1    Dunn, P.J.2    Hayler, J.D.3    Humphrey, G.R.4    Leazer, J.L.5
  • 84
    • 0034622509 scopus 로고    scopus 로고
    • Rhodococcus L-phenylalanine dehydrogenase: Kinetics, mechanism, and structural basis for catalytic specificity
    • Brunhuber NMW, Thoden JB, Blanchard JS, Vanhooke JL. 2000. Rhodococcus L-phenylalanine dehydrogenase: kinetics, mechanism, and structural basis for catalytic specificity. Biochemistry 39:9174-87
    • (2000) Biochemistry , vol.39 , pp. 9174-9187
    • Brunhuber, N.M.W.1    Thoden, J.B.2    Blanchard, J.S.3    Vanhooke, J.L.4
  • 85
    • 79960505418 scopus 로고    scopus 로고
    • Merging the best of two worlds: Artificial metalloenzymes for enantioselective catalysis
    • Ringenberg MR, Ward TR. 2011. Merging the best of two worlds: artificial metalloenzymes for enantioselective catalysis. Chem. Commun. 47:8470-76
    • (2011) Chem. Commun. , vol.47 , pp. 8470-8476
    • Ringenberg, M.R.1    Ward, T.R.2
  • 86
    • 80155179922 scopus 로고    scopus 로고
    • Artificial metalloenzymes for olefin metathesis based on the biotin-(strept)avidin technology
    • Lo C, Ringenberg MR, Gnandt D, Wilson Y, Ward TR. 2011. Artificial metalloenzymes for olefin metathesis based on the biotin-(strept)avidin technology. Chem. Commun. 47:12065-67
    • (2011) Chem. Commun. , vol.47 , pp. 12065-12067
    • Lo, C.1    Ringenberg, M.R.2    Gnandt, D.3    Wilson, Y.4    Ward, T.R.5
  • 87
    • 84895771303 scopus 로고    scopus 로고
    • Recent achievements in the design and engineering of artificial metalloenzymes
    • Durrenberger M, Ward TR. 2014. Recent achievements in the design and engineering of artificial metalloenzymes. Curr. Opin. Chem. Biol. 19:99-106
    • (2014) Curr. Opin. Chem. Biol. , vol.19 , pp. 99-106
    • Durrenberger, M.1    Ward, T.R.2
  • 88
    • 84896520980 scopus 로고    scopus 로고
    • Expanding P450 catalytic reaction space through evolution and engineering
    • Mclntosh JA, Farwell CC, Arnold FH. 2014. Expanding P450 catalytic reaction space through evolution and engineering. Curr. Opin. Chem. Biol. 19:126-34
    • (2014) Curr. Opin. Chem. Biol. , vol.19 , pp. 126-134
    • McLntosh, J.A.1    Farwell, C.C.2    Arnold, F.H.3
  • 89
    • 84883040115 scopus 로고    scopus 로고
    • Enantioselective intramolecular C-H amination catalyzed by engineered cytochrome P450 enzymes in vitro and in vivo
    • McIntosh JA, Coelho PS, Farwell CC, Wang ZJ, Lewis JC, et al. 2013. Enantioselective intramolecular C-H amination catalyzed by engineered cytochrome P450 enzymes in vitro and in vivo. Angew. Chem. Int. Ed. 52:9309-12
    • (2013) Angew. Chem. Int. Ed. , vol.52 , pp. 9309-9312
    • McIntosh, J.A.1    Coelho, P.S.2    Farwell, C.C.3    Wang, Z.J.4    Lewis, J.C.5
  • 90
    • 84891459977 scopus 로고    scopus 로고
    • Cytochrome P450-catalyzed insertion of carbenoids into N-H bonds
    • Wang ZJ, Peck NE, Renata H, Arnold FH. 2014. Cytochrome P450-catalyzed insertion of carbenoids into N-H bonds. Chem. Sci. 5:598-601
    • (2014) Chem. Sci. , vol.5 , pp. 598-601
    • Wang, Z.J.1    Peck, N.E.2    Renata, H.3    Arnold, F.H.4
  • 91
    • 84941144686 scopus 로고    scopus 로고
    • Structural, functional, and spectroscopic characterization of the substrate scope of the novel nitrating cytochrome P450 TxtE
    • Dodani SC, Cahn JKB, Heinisch T, Brinkmann-Chen S, McIntosh JA, Arnold FH. 2014. Structural, functional, and spectroscopic characterization of the substrate scope of the novel nitrating cytochrome P450 TxtE. Chembiochem 15:2259-67
    • (2014) Chembiochem , vol.15 , pp. 2259-2267
    • Dodani, S.C.1    Cahn, J.K.B.2    Heinisch, T.3    Brinkmann-Chen, S.4    McIntosh, J.A.5    Arnold, F.H.6
  • 92
    • 84880921220 scopus 로고    scopus 로고
    • A serine-substituted P450 catalyzes highly efficient carbene transfer to olefins in vivo
    • Coelho PS, Wang ZJ, Ener ME, Baril SA, Kannan A, et al. 2013. A serine-substituted P450 catalyzes highly efficient carbene transfer to olefins in vivo. Nat. Chem. Biol. 9:485-87
    • (2013) Nat. Chem. Biol. , vol.9 , pp. 485-487
    • Coelho, P.S.1    Wang, Z.J.2    Ener, M.E.3    Baril, S.A.4    Kannan, A.5
  • 93
    • 84903168457 scopus 로고    scopus 로고
    • Improved cyclopropanation activity of histidine-ligated cytochrome P450 enables the enantioselective formal synthesis of levomilnacipran
    • Wang ZJ, Renata H, Peck NE, Farwell CC, Coelho PS, Arnold FH. 2014. Improved cyclopropanation activity of histidine-ligated cytochrome P450 enables the enantioselective formal synthesis of levomilnacipran. Angew. Chem. Int. Ed. 53:6810-13
    • (2014) Angew. Chem. Int. Ed. , vol.53 , pp. 6810-6813
    • Wang, Z.J.1    Renata, H.2    Peck, N.E.3    Farwell, C.C.4    Coelho, P.S.5    Arnold, F.H.6
  • 94
    • 77649271939 scopus 로고    scopus 로고
    • Evolutionary optimization of computationally designed enzymes: Kemp eliminases of the KE07 series
    • Khersonsky O, Rothlisberger D, Dym O, Albeck S, Jackson CJ, et al. 2010. Evolutionary optimization of computationally designed enzymes: Kemp eliminases of the KE07 series. J. Mol. Biol. 396:1025-42
    • (2010) J. Mol. Biol. , vol.396 , pp. 1025-1042
    • Khersonsky, O.1    Rothlisberger, D.2    Dym, O.3    Albeck, S.4    Jackson, C.J.5
  • 95
    • 84863000087 scopus 로고    scopus 로고
    • Bridging the gaps in design methodologies by evolutionary optimization of the stability and proficiency of designed Kemp eliminase KE59
    • Khersonsky O, Kiss G, Rothlisberger D, Dym O, Albeck S, et al. 2012. Bridging the gaps in design methodologies by evolutionary optimization of the stability and proficiency of designed Kemp eliminase KE59. Proc. Natl. Acad. Sci. USA 109:10358-63
    • (2012) Proc. Natl. Acad. Sci. USA , vol.109 , pp. 10358-10363
    • Khersonsky, O.1    Kiss, G.2    Rothlisberger, D.3    Dym, O.4    Albeck, S.5
  • 96
    • 84888034901 scopus 로고    scopus 로고
    • Precision is essential for efficient catalysis in an evolved Kemp eliminase
    • Blomberg R, KriesH, PinkasDM, Mittl PRE, GrutterMG, et al. 2013. Precision is essential for efficient catalysis in an evolved Kemp eliminase. Nature 503:418-21
    • (2013) Nature , vol.503 , pp. 418-421
    • Blomberg, R.1    Kries, H.2    Pinkas, D.M.3    Mittl, P.R.E.4    Grutter, M.G.5
  • 97
    • 84893961776 scopus 로고    scopus 로고
    • Protein engineering from scratch is maturing
    • Hohne M, Bornscheuer UT. 2014. Protein engineering from scratch is maturing. Angew. Chem. Int. Ed. 53:1200-2
    • (2014) Angew. Chem. Int. Ed. , vol.53 , pp. 1200-1202
    • Hohne, M.1    Bornscheuer, U.T.2
  • 98
    • 72149100480 scopus 로고    scopus 로고
    • Biocatalytic synthesis of atorvastatin intermediates
    • Patel JM. 2009. Biocatalytic synthesis of atorvastatin intermediates. J. Mol. Catal. B: Enzym. 61:123-28
    • (2009) J. Mol. Catal. B: Enzym. , vol.61 , pp. 123-128
    • Patel, J.M.1
  • 99
    • 12344273661 scopus 로고    scopus 로고
    • Chemoenzymatic synthesis of building blocks for statin side chains
    • Muller M. 2005. Chemoenzymatic synthesis of building blocks for statin side chains. Angew. Chem. Int. Ed. 44:362-65
    • (2005) Angew. Chem. Int. Ed. , vol.44 , pp. 362-365
    • Muller, M.1
  • 100
    • 0034605876 scopus 로고    scopus 로고
    • Highly regio-and enantioselective reduction of 3,5-dioxocarboxylates
    • Wolberg M, Hummel W, Wandrey C, Muller M. 2000. Highly regio-and enantioselective reduction of 3,5-dioxocarboxylates. Angew. Chem. Int. Ed. 39:4306-8
    • (2000) Angew. Chem. Int. Ed. , vol.39 , pp. 4306-4308
    • Wolberg, M.1    Hummel, W.2    Wandrey, C.3    Muller, M.4
  • 101
    • 41049101364 scopus 로고    scopus 로고
    • Chemoenzymatic synthesis of the chiral side-chain of statins: Application of an alcohol dehydrogenase catalysed ketone reduction on a large scale
    • Wolberg M, Villela M, Bode S, Geilenkirchen P, Feldmann R, et al. 2008. Chemoenzymatic synthesis of the chiral side-chain of statins: application of an alcohol dehydrogenase catalysed ketone reduction on a large scale. Bioprocess Biosyst. Eng. 31:183-91
    • (2008) Bioprocess Biosyst. Eng. , vol.31 , pp. 183-191
    • Wolberg, M.1    Villela, M.2    Bode, S.3    Geilenkirchen, P.4    Feldmann, R.5
  • 102
    • 0035813841 scopus 로고    scopus 로고
    • Biocatalytic reduction of diketo esters: A highly stereoselective approach to all four stereoisomers of a chlorinated dihydroxy hexanoate
    • Wolberg M, Hummel W, Muller M. 2001. Biocatalytic reduction of diketo esters: a highly stereoselective approach to all four stereoisomers of a chlorinated dihydroxy hexanoate. Chem. Eur. J. 7:4562-71
    • (2001) Chem. Eur. J. , vol.7 , pp. 4562-4571
    • Wolberg, M.1    Hummel, W.2    Muller, M.3
  • 103
    • 65249128025 scopus 로고    scopus 로고
    • Biocatalysis in development of green pharmaceutical processes
    • Tao JH, Xu JH. 2009. Biocatalysis in development of green pharmaceutical processes. Curr. Opin. Chem. Biol. 13:43-50
    • (2009) Curr. Opin. Chem. Biol. , vol.13 , pp. 43-50
    • Tao, J.H.1    Xu, J.H.2
  • 106
    • 84873964850 scopus 로고    scopus 로고
    • Chemoenzymatic asymmetric synthesis of pregabalin precursors via asymmetric bioreduction of cyanoacrylate esters using ene-reductases
    • Winkler CK, Clay D, Davies S, O'Neill P, McDaid P, et al. 2013. Chemoenzymatic asymmetric synthesis of pregabalin precursors via asymmetric bioreduction of cyanoacrylate esters using ene-reductases. J. Organ. Chem. 78:1525-33
    • (2013) J. Organ. Chem. , vol.78 , pp. 1525-1533
    • Winkler, C.K.1    Clay, D.2    Davies, S.3    O'Neill, P.4    McDaid, P.5
  • 107
    • 84901358321 scopus 로고    scopus 로고
    • Nitrile as activating group in the asymmetric bioreduction of cyanoacrylic acids catalyzed by ene-reductases
    • Winkler CK, Clay D, Turrini NG, Lechner H, Kroutil W, et al. 2014. Nitrile as activating group in the asymmetric bioreduction of cyanoacrylic acids catalyzed by ene-reductases. Adv. Synth. Catal. 356:1878-82
    • (2014) Adv. Synth. Catal. , vol.356 , pp. 1878-1882
    • Winkler, C.K.1    Clay, D.2    Turrini, N.G.3    Lechner, H.4    Kroutil, W.5
  • 108
    • 34547223622 scopus 로고    scopus 로고
    • Preparation of an amino acid intermediate for the dipeptidyl peptidase IV inhibitor, saxagliptin, using a modified phenylalanine dehydrogenase
    • Hanson RL,Goldberg SL, BrzozowskiDB, Tully TP, CazzulinoD, et al. 2007. Preparation of an amino acid intermediate for the dipeptidyl peptidase IV inhibitor, saxagliptin, using a modified phenylalanine dehydrogenase. Adv. Synth. Catal. 349:1369-78
    • (2007) Adv. Synth. Catal. , vol.349 , pp. 1369-1378
    • Hanson, R.L.1    Goldberg, S.L.2    Brzozowski, D.B.3    Tully, T.P.4    Cazzulino, D.5
  • 109
    • 77954797329 scopus 로고    scopus 로고
    • Biocatalytic asymmetric synthesis of chiral amines from ketones applied to sitagliptin manufacture
    • Savile CK, Janey JM, Mundorff EC,Moore JC, Tam S, et al. 2010. Biocatalytic asymmetric synthesis of chiral amines from ketones applied to sitagliptin manufacture. Science 329:305-9
    • (2010) Science , vol.329 , pp. 305-309
    • Savile, C.K.1    Janey, J.M.2    Mundorff, E.C.3    Moore, J.C.4    Tam, S.5
  • 110
    • 79960612358 scopus 로고    scopus 로고
    • Enantioenriched compounds via enzyme-catalyzed redox reactions
    • Hall M, Bommarius AS. 2011. Enantioenriched compounds via enzyme-catalyzed redox reactions. Chem. Rev. 111:4088-110
    • (2011) Chem. Rev. , vol.111 , pp. 4088-4110
    • Hall, M.1    Bommarius, A.S.2


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