메뉴 건너뛰기




Volumn 101, Issue 20, 2017, Pages 7557-7565

Coupled reactions by coupled enzymes: alcohol to lactone cascade with alcohol dehydrogenase–cyclohexanone monooxygenase fusions

Author keywords

Alcohol dehydrogenase; Cascade; Cyclohexanone monooxygenase; Enzyme fusion

Indexed keywords

CASCADES (FLUID MECHANICS); ENZYME ACTIVITY; ENZYME IMMOBILIZATION; ESTERS; GENES; REDOX REACTIONS;

EID: 85029527704     PISSN: 01757598     EISSN: 14320614     Source Type: Journal    
DOI: 10.1007/s00253-017-8501-4     Document Type: Article
Times cited : (58)

References (28)
  • 1
    • 84950123144 scopus 로고    scopus 로고
    • Enhancing the productivity of the bi-enzymatic convergent cascade for ɛ-caprolactone synthesis through design of experiments and a biphasic system
    • COI: 1:CAS:528:DC%2BC2MXitVKrsbrF
    • Bornadel A, Hatti-Kaul R, Hollmann F, Kara S (2016) Enhancing the productivity of the bi-enzymatic convergent cascade for ɛ-caprolactone synthesis through design of experiments and a biphasic system. Tetrahedron 72(46):7222–7228
    • (2016) Tetrahedron , vol.72 , Issue.46 , pp. 7222-7228
    • Bornadel, A.1    Hatti-Kaul, R.2    Hollmann, F.3    Kara, S.4
  • 2
    • 0028607161 scopus 로고
    • Engineering the quaternary structure of an enzyme: construction and analysis of a monomeric form of malate dehydrogenase from Escherichia coli
    • COI: 1:CAS:528:DyaK2MXivFGnu7c%3D, PID: 7703849
    • Breiter DR, Resnik E, Banaszak LJ (1994) Engineering the quaternary structure of an enzyme: construction and analysis of a monomeric form of malate dehydrogenase from Escherichia coli. Protein Sci 3(11):2023–2032
    • (1994) Protein Sci , vol.3 , Issue.11 , pp. 2023-2032
    • Breiter, D.R.1    Resnik, E.2    Banaszak, L.J.3
  • 3
    • 84881018686 scopus 로고    scopus 로고
    • Fusion protein linkers: property, design and functionality
    • COI: 1:CAS:528:DC%2BC38XhsFWitbvN, PID: 23026637
    • Chen X, Zaro JL, Shen WC (2013) Fusion protein linkers: property, design and functionality. Adv Drug Deliv Rev 65(10):1357–1369
    • (2013) Adv Drug Deliv Rev , vol.65 , Issue.10 , pp. 1357-1369
    • Chen, X.1    Zaro, J.L.2    Shen, W.C.3
  • 4
    • 84924302954 scopus 로고    scopus 로고
    • Bringing functions together with fusion enzymes—from nature’s inventions to biotechnological applications
    • COI: 1:CAS:528:DC%2BC2cXitFClsLfJ, PID: 25535094
    • Elleuche S (2015) Bringing functions together with fusion enzymes—from nature’s inventions to biotechnological applications. Appl Microbiol Biotechnol 99(4):1545–1556
    • (2015) Appl Microbiol Biotechnol , vol.99 , Issue.4 , pp. 1545-1556
    • Elleuche, S.1
  • 5
    • 65349155431 scopus 로고    scopus 로고
    • ThermoFAD, a Thermofluor®-adapted flavin ad hoc detection system for protein folding and ligand binding
    • COI: 1:CAS:528:DC%2BD1MXmt1Cmtrk%3D, PID: 19459938
    • Forneris F, Orru R, Bonivento D, Chiarelli LR, Mattevi A (2009) ThermoFAD, a Thermofluor®-adapted flavin ad hoc detection system for protein folding and ligand binding. FEBS J 276(10):2833–2840
    • (2009) FEBS J , vol.276 , Issue.10 , pp. 2833-2840
    • Forneris, F.1    Orru, R.2    Bonivento, D.3    Chiarelli, L.R.4    Mattevi, A.5
  • 7
    • 77950198763 scopus 로고    scopus 로고
    • Preparation and characterization of a bifunctional aldolase/kinase enzyme: a more efficient biocatalyst for C-C bond formation
    • COI: 1:CAS:528:DC%2BC3cXktFGrsLs%3D, PID: 20198665
    • Iturrate L, Sánchez-Moreno I, Oroz-Guinea I, Pérez-Gil J, García-Junceda E (2010) Preparation and characterization of a bifunctional aldolase/kinase enzyme: a more efficient biocatalyst for C-C bond formation. Chem Eur J 16(13):4018–4030
    • (2010) Chem Eur J , vol.16 , Issue.13 , pp. 4018-4030
    • Iturrate, L.1    Sánchez-Moreno, I.2    Oroz-Guinea, I.3    Pérez-Gil, J.4    García-Junceda, E.5
  • 8
    • 84937639365 scopus 로고    scopus 로고
    • Enzyme fusion for whole-cell biotransformation of long-chain sec-alcohols into esters
    • COI: 1:CAS:528:DC%2BC2MXhvFCitrs%3D, PID: 25636834
    • Jeon EY, Baek AH, Bornscheuer UT, Park JB (2015) Enzyme fusion for whole-cell biotransformation of long-chain sec-alcohols into esters. Appl Microbiol Biotechnol 99(15):6267–6275
    • (2015) Appl Microbiol Biotechnol , vol.99 , Issue.15 , pp. 6267-6275
    • Jeon, E.Y.1    Baek, A.H.2    Bornscheuer, U.T.3    Park, J.B.4
  • 9
    • 0019554714 scopus 로고
    • Potential applications of an alcohol-aldehyde/ketone oxidoreductase from thermophilic bacteria
    • COI: 1:CAS:528:DyaL3MXktVGisrk%3D
    • Lamed RJ, Keinan EJGZ, Zeikus JG (1981) Potential applications of an alcohol-aldehyde/ketone oxidoreductase from thermophilic bacteria. Enzym Microb Technol 3(2):144–148
    • (1981) Enzym Microb Technol , vol.3 , Issue.2 , pp. 144-148
    • Lamed, R.J.1    Keinan, E.J.G.Z.2    Zeikus, J.G.3
  • 11
    • 84881555309 scopus 로고    scopus 로고
    • A self-sufficient Baeyer–Villiger biocatalysis system for the synthesis of ɛ-caprolactone from cyclohexanol
    • COI: 1:CAS:528:DC%2BC3sXisVyhtrg%3D
    • Mallin H, Wulf H, Bornscheuer UT (2013) A self-sufficient Baeyer–Villiger biocatalysis system for the synthesis of ɛ-caprolactone from cyclohexanol. Enzym Microb Technol 53(4):283–287
    • (2013) Enzym Microb Technol , vol.53 , Issue.4 , pp. 283-287
    • Mallin, H.1    Wulf, H.2    Bornscheuer, U.T.3
  • 13
    • 84925355800 scopus 로고    scopus 로고
    • Cascade catalysis–strategies and challenges en route to preparative synthetic biology
    • COI: 1:CAS:528:DC%2BC2cXitFeht77K, PID: 25654472
    • Muschiol J, Peters C, Oberleitner N, Mihovilovic MD, Bornscheuer UT, Rudroff F (2015) Cascade catalysis–strategies and challenges en route to preparative synthetic biology. Chem Comm 51(27):5798–5811
    • (2015) Chem Comm , vol.51 , Issue.27 , pp. 5798-5811
    • Muschiol, J.1    Peters, C.2    Oberleitner, N.3    Mihovilovic, M.D.4    Bornscheuer, U.T.5    Rudroff, F.6
  • 14
    • 85002647242 scopus 로고    scopus 로고
    • Fusion proteins of an enoate reductase and a Baeyer-Villiger monooxygenase facilitate the synthesis of chiral lactones
    • COI: 1:CAS:528:DC%2BC28XhvFykurvE, PID: 27289001
    • Peters C, Rudroff F, Mihovilovic MD, Bornscheuer T, U. (2017) Fusion proteins of an enoate reductase and a Baeyer-Villiger monooxygenase facilitate the synthesis of chiral lactones. Biol Chem 398(1):31–37
    • (2017) Biol Chem , vol.398 , Issue.1 , pp. 31-37
    • Peters, C.1    Rudroff, F.2    Mihovilovic, M.D.3    Bornscheuer, T.4
  • 15
    • 85003707576 scopus 로고    scopus 로고
    • Characterization and crystal structure of a robust cyclohexanone monooxygenase
    • Romero E, Castellanos J, Mattevi A, Fraaije MW (2016) Characterization and crystal structure of a robust cyclohexanone monooxygenase. Angew Chem 128(51):16084–16087
    • (2016) Angew Chem , vol.128 , Issue.51 , pp. 16084-16087
    • Romero, E.1    Castellanos, J.2    Mattevi, A.3    Fraaije, M.W.4
  • 16
  • 17
    • 85027956629 scopus 로고    scopus 로고
    • A fed-batch synthetic strategy for a three-step enzymatic synthesis of poly-ϵ-caprolactone
    • COI: 1:CAS:528:DC%2BC28XhsVCqtLzO
    • Scherkus C, Schmidt S, Bornscheuer UT, Gröger H, Kara S, Liese A (2016) A fed-batch synthetic strategy for a three-step enzymatic synthesis of poly-ϵ-caprolactone. ChemCatChem 8(22):3446–3452
    • (2016) ChemCatChem , vol.8 , Issue.22 , pp. 3446-3452
    • Scherkus, C.1    Schmidt, S.2    Bornscheuer, U.T.3    Gröger, H.4    Kara, S.5    Liese, A.6
  • 20
    • 84881552218 scopus 로고    scopus 로고
    • Direct biocatalytic one-pot-transformation of cyclohexanol with molecular oxygen into ɛ-caprolactone
    • COI: 1:CAS:528:DC%2BC3sXot1ChsL4%3D
    • Staudt S, Bornscheuer UT, Menyes U, Hummel W, Gröger H (2013) Direct biocatalytic one-pot-transformation of cyclohexanol with molecular oxygen into ɛ-caprolactone. Enzym Microb Technol 53(4):288–292
    • (2013) Enzym Microb Technol , vol.53 , Issue.4 , pp. 288-292
    • Staudt, S.1    Bornscheuer, U.T.2    Menyes, U.3    Hummel, W.4    Gröger, H.5
  • 22
    • 41049111588 scopus 로고    scopus 로고
    • Self-sufficient Baeyer–Villiger monooxygenases: effective coenzyme regeneration for biooxygenation by fusion engineering
    • Torres Pazmiño DE, Snajdrova R, Baas BJ, Ghobrial M, Mihovilovic MD, Fraaije MW (2008) Self-sufficient Baeyer–Villiger monooxygenases: effective coenzyme regeneration for biooxygenation by fusion engineering. Angew Chem 120(12):2307–2310
    • (2008) Angew Chem , vol.120 , Issue.12 , pp. 2307-2310
    • Torres Pazmiño, D.E.1    Snajdrova, R.2    Baas, B.J.3    Ghobrial, M.4    Mihovilovic, M.D.5    Fraaije, M.W.6
  • 23
    • 0034826251 scopus 로고    scopus 로고
    • Genetic and biochemical characterization of a short-chain alcohol dehydrogenase from the hyperthermophilic archaeon Pyrococcus furiosus
    • PID: 11358525
    • van der Oost J, Voorhorst WG, Kengen SW, Geerling A, Wittenhorst V, Gueguen Y, de Vos WM (2001) Genetic and biochemical characterization of a short-chain alcohol dehydrogenase from the hyperthermophilic archaeon Pyrococcus furiosus. Eur J Biochem 268(10):3062–3068
    • (2001) Eur J Biochem , vol.268 , Issue.10 , pp. 3062-3068
    • van der Oost, J.1    Voorhorst, W.G.2    Kengen, S.W.3    Geerling, A.4    Wittenhorst, V.5    Gueguen, Y.6    de Vos, W.M.7
  • 24
    • 84961644292 scopus 로고    scopus 로고
    • Substrate channelling as an approach to cascade reactions
    • COI: 1:CAS:528:DC%2BC28Xks1Cru7Y%3D, PID: 27001725
    • Wheeldon I, Minteer SD, Banta S, Barton SC, Atanassov P, Sigman M (2016) Substrate channelling as an approach to cascade reactions. Nat Chem 8(4):299–309
    • (2016) Nat Chem , vol.8 , Issue.4 , pp. 299-309
    • Wheeldon, I.1    Minteer, S.D.2    Banta, S.3    Barton, S.C.4    Atanassov, P.5    Sigman, M.6
  • 25
    • 33750378958 scopus 로고    scopus 로고
    • Blue native PAGE
    • COI: 1:CAS:528:DC%2BD28XhtFOitbnI, PID: 17406264
    • Wittig I, Braun HP, Schagger H (2006) Blue native PAGE. Nat Protoc 1(1):418
    • (2006) Nat Protoc , vol.1 , Issue.1 , pp. 418
    • Wittig, I.1    Braun, H.P.2    Schagger, H.3
  • 26
    • 84876726128 scopus 로고    scopus 로고
    • Protein engineering of enzymes for process applications
    • COI: 1:CAS:528:DC%2BC3sXlsFerurc%3D, PID: 23562542
    • Woodley JM (2013) Protein engineering of enzymes for process applications. Curr Opin Chem Biol 17(2):310–316
    • (2013) Curr Opin Chem Biol , vol.17 , Issue.2 , pp. 310-316
    • Woodley, J.M.1
  • 27
    • 84861458813 scopus 로고    scopus 로고
    • Process technology for multi-enzymatic reaction systems
    • COI: 1:CAS:528:DC%2BC38XnvVOrsbo%3D, PID: 22531164
    • Xue R, Woodley JM (2012) Process technology for multi-enzymatic reaction systems. Bioresour Technol 115:183–195
    • (2012) Bioresour Technol , vol.115 , pp. 183-195
    • Xue, R.1    Woodley, J.M.2
  • 28
    • 84982295410 scopus 로고    scopus 로고
    • The promises and challenges of fusion constructs in protein biochemistry and enzymology
    • COI: 1:CAS:528:DC%2BC28Xhtlyksr3E, PID: 27541749
    • Yang H, Liu L, Xu F (2016) The promises and challenges of fusion constructs in protein biochemistry and enzymology. Appl Microbiol Biotechnol 100(19):8273–8281
    • (2016) Appl Microbiol Biotechnol , vol.100 , Issue.19 , pp. 8273-8281
    • Yang, H.1    Liu, L.2    Xu, F.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.