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Volumn 99, Issue 11, 2015, Pages 4615-4627

Multienzymatic synthesis of nucleic acid derivatives: a general perspective

Author keywords

Biocatalysis; Cells; Multienzymatic systems; NADs

Indexed keywords

BIOCATALYSTS; BIOMOLECULES; CATALYSIS; CELLS; NUCLEIC ACIDS; ORGANIC COMPOUNDS;

EID: 84929521655     PISSN: 01757598     EISSN: 14320614     Source Type: Journal    
DOI: 10.1007/s00253-015-6642-x     Document Type: Review
Times cited : (48)

References (81)
  • 4
    • 33644699687 scopus 로고    scopus 로고
    • Hydrolytic approach for production of deoxyribonucleoside-and ribonucleoside-5′-monophosphates and enzymatic synthesis of their polyphosphates
    • COI: 1:CAS:528:DC%2BD28Xht12lsbk%3D, PID: 16457623
    • Bochkov D, Khomov V, Tolstikova T (2006) Hydrolytic approach for production of deoxyribonucleoside-and ribonucleoside-5′-monophosphates and enzymatic synthesis of their polyphosphates. Biochemistry 71:79–83
    • (2006) Biochemistry , vol.71 , pp. 79-83
    • Bochkov, D.1    Khomov, V.2    Tolstikova, T.3
  • 5
    • 42149084530 scopus 로고    scopus 로고
    • Reactions of transglycosylation in the nucleoside chemistry
    • COI: 1:CAS:528:DC%2BD1cXnsVyjtL4%3D
    • Boryski J (2008) Reactions of transglycosylation in the nucleoside chemistry. Curr Org Chem 12:309–325
    • (2008) Curr Org Chem , vol.12 , pp. 309-325
    • Boryski, J.1
  • 6
    • 80052555950 scopus 로고    scopus 로고
    • Biosynthetic origin and mechanism of formation of the aminoribosyl moiety of peptidyl nucleoside antibiotics
    • COI: 1:CAS:528:DC%2BC3MXhtVGjur%2FN, PID: 21819104
    • Chi X, Pahari P, Nonaka K, Van Lanen SG (2011) Biosynthetic origin and mechanism of formation of the aminoribosyl moiety of peptidyl nucleoside antibiotics. J Am Chem Soc 133:14452–14459
    • (2011) J Am Chem Soc , vol.133 , pp. 14452-14459
    • Chi, X.1    Pahari, P.2    Nonaka, K.3    Van Lanen, S.G.4
  • 7
    • 33744464514 scopus 로고    scopus 로고
    • Substrate specificity in enzymatic fluorination. The fluorinase from Streptomyces cattleya accepts 2′-deoxyadenosine substrates
    • COI: 1:CAS:528:DC%2BD28Xkt1Kht78%3D, PID: 16604208
    • Cobb SL, Deng H, McEwan AR, Naismith JH, O’Hagan D, Robinson DA (2006) Substrate specificity in enzymatic fluorination. The fluorinase from Streptomyces cattleya accepts 2′-deoxyadenosine substrates. Org Biomol Chem 4:1458–1460
    • (2006) Org Biomol Chem , vol.4 , pp. 1458-1460
    • Cobb, S.L.1    Deng, H.2    McEwan, A.R.3    Naismith, J.H.4    O’Hagan, D.5    Robinson, D.A.6
  • 9
    • 33947363701 scopus 로고    scopus 로고
    • 8-Azaguanine reporter of purine ionization states in structured RNAs
    • PID: 17326637
    • Da Costa CP, Fedor MJ, Scott LG (2007) 8-Azaguanine reporter of purine ionization states in structured RNAs. J Am Chem Soc 129:3426–3432
    • (2007) J Am Chem Soc , vol.129 , pp. 3426-3432
    • Da Costa, C.P.1    Fedor, M.J.2    Scott, L.G.3
  • 10
    • 84867399630 scopus 로고    scopus 로고
    • Biotransformation of 2,6‐diaminopurine nucleosides by immobilized Geobacillus stearothermophilus
    • De Benedetti EC, Rivero CW, Britos CN, Lozano ME, Trelles JA (2012) Biotransformation of 2,6‐diaminopurine nucleosides by immobilized Geobacillus stearothermophilus. Biotechnol Progr 28:1251–1256
    • (2012) Biotechnol Progr , vol.28 , pp. 1251-1256
    • De Benedetti, E.C.1    Rivero, C.W.2    Britos, C.N.3    Lozano, M.E.4    Trelles, J.A.5
  • 11
    • 23444445718 scopus 로고    scopus 로고
    • Antiviral drug discovery and development: where chemistry meets with biomedicine
    • PID: 16046240
    • De Clercq E (2005a) Antiviral drug discovery and development: where chemistry meets with biomedicine. Antivir Res 67:56–75
    • (2005) Antivir Res , vol.67 , pp. 56-75
    • De Clercq, E.1
  • 12
    • 25144513582 scopus 로고    scopus 로고
    • Recent highlights in the development of new antiviral drugs
    • PID: 16125443
    • De Clercq E (2005b) Recent highlights in the development of new antiviral drugs. Curr Opin Microbiol 8:552–560
    • (2005) Curr Opin Microbiol , vol.8 , pp. 552-560
    • De Clercq, E.1
  • 14
    • 84895075028 scopus 로고    scopus 로고
    • Identification of fluorinases from Streptomyces sp MA37, Norcardia brasiliensis, and Actinoplanes sp N902‐109 by Genome Mining
    • COI: 1:CAS:528:DC%2BC2cXpslSjsw%3D%3D, PID: 24449539
    • Deng H, Ma L, Bandaranayaka N, Qin Z, Mann G, Kyeremeh K, Yu Y, Shepherd T, Naismith JH, O’Hagan D (2014) Identification of fluorinases from Streptomyces sp MA37, Norcardia brasiliensis, and Actinoplanes sp N902‐109 by Genome Mining. ChemBioChem 15:364–368
    • (2014) ChemBioChem , vol.15 , pp. 364-368
    • Deng, H.1    Ma, L.2    Bandaranayaka, N.3    Qin, Z.4    Mann, G.5    Kyeremeh, K.6    Yu, Y.7    Shepherd, T.8    Naismith, J.H.9    O’Hagan, D.10
  • 15
    • 37249024344 scopus 로고    scopus 로고
    • Discovery and characterization of a marine bacterial SAM-dependent chlorinase
    • PID: 18059261
    • Eustáquio AS, Pojer F, Noel JP, Moore BS (2007) Discovery and characterization of a marine bacterial SAM-dependent chlorinase. Nat Chem Biol 4:69–74
    • (2007) Nat Chem Biol , vol.4 , pp. 69-74
    • Eustáquio, A.S.1    Pojer, F.2    Noel, J.P.3    Moore, B.S.4
  • 16
    • 84872783399 scopus 로고    scopus 로고
    • Enhancement of cytidine production by coexpression of gnd, zwf, and prs genes in recombinant Escherichia coli CYT15
    • COI: 1:CAS:528:DC%2BC3sXhsVOhurw%3D, PID: 23070626
    • Fang H, Xie X, Xu Q, Zhang C, Chen N (2013) Enhancement of cytidine production by coexpression of gnd, zwf, and prs genes in recombinant Escherichia coli CYT15. Biotechnol Lett 35:245–251
    • (2013) Biotechnol Lett , vol.35 , pp. 245-251
    • Fang, H.1    Xie, X.2    Xu, Q.3    Zhang, C.4    Chen, N.5
  • 17
    • 84885933463 scopus 로고    scopus 로고
    • New insights on nucleoside 2′-deoxyribosyltransferases: a versatile biocatalyst for one-pot one-step synthesis of nucleoside analogs
    • COI: 1:CAS:528:DC%2BC3sXlvV2hsbs%3D, PID: 23529679
    • Fresco-Taboada A, de la Mata I, Arroyo M, Fernández-Lucas J (2013) New insights on nucleoside 2′-deoxyribosyltransferases: a versatile biocatalyst for one-pot one-step synthesis of nucleoside analogs. Appl Microbiol Biotechnol 97:3773–3785
    • (2013) Appl Microbiol Biotechnol , vol.97 , pp. 3773-3785
    • Fresco-Taboada, A.1    de la Mata, I.2    Arroyo, M.3    Fernández-Lucas, J.4
  • 18
    • 0031147732 scopus 로고    scopus 로고
    • High level expression of XMP aminase in Escherichia coli and its application for the industrial production of 5′-guanylic acid
    • COI: 1:CAS:528:DyaK2sXjsVygs7Y%3D, PID: 9178561
    • Fujio T, Nishi T, Ito S, Maruyama A (1997) High level expression of XMP aminase in Escherichia coli and its application for the industrial production of 5′-guanylic acid. Biosci Biotechnol Biochem 61:840–845
    • (1997) Biosci Biotechnol Biochem , vol.61 , pp. 840-845
    • Fujio, T.1    Nishi, T.2    Ito, S.3    Maruyama, A.4
  • 19
    • 0036636579 scopus 로고    scopus 로고
    • Nucleoside analogues and nucleobases in cancer treatment
    • COI: 1:CAS:528:DC%2BD38Xls1Wisrw%3D, PID: 12142171
    • Galmarini CM, Mackey JR, Dumontet C (2002) Nucleoside analogues and nucleobases in cancer treatment. Lancet Oncol 3:415–424
    • (2002) Lancet Oncol , vol.3 , pp. 415-424
    • Galmarini, C.M.1    Mackey, J.R.2    Dumontet, C.3
  • 21
    • 70350566113 scopus 로고    scopus 로고
    • Co-expression of recombinant nucleoside phosphorylase from Escherichia coli and its application
    • COI: 1:CAS:528:DC%2BD1MXhtFyhsbvP, PID: 19099210
    • Ge C, OuYang L, Ding Q, Ou L (2009) Co-expression of recombinant nucleoside phosphorylase from Escherichia coli and its application. Appl Biochem Biotechnol 159:168–177
    • (2009) Appl Biochem Biotechnol , vol.159 , pp. 168-177
    • Ge, C.1    OuYang, L.2    Ding, Q.3    Ou, L.4
  • 22
    • 78650678548 scopus 로고    scopus 로고
    • Defining a process operating window for the synthesis of 5-methyluridine by transglycosylation of guanosine and thymine
    • COI: 1:CAS:528:DC%2BC3MXht1SlsQ%3D%3D, PID: 21112359
    • Gordon GE, Visser DF, Brady D, Raseroka N, Bode ML (2011) Defining a process operating window for the synthesis of 5-methyluridine by transglycosylation of guanosine and thymine. J Biotechnol 151:108–113
    • (2011) J Biotechnol , vol.151 , pp. 108-113
    • Gordon, G.E.1    Visser, D.F.2    Brady, D.3    Raseroka, N.4    Bode, M.L.5
  • 23
    • 0019725394 scopus 로고
    • A study on the mechanism of DNA excretion from P. aeruginosa KYU-1. Effect of mitomycin C on extracellular DNA production
    • COI: 1:CAS:528:DyaL38XhslSrtg%3D%3D
    • Hara T, Ueda S (1981) A study on the mechanism of DNA excretion from P. aeruginosa KYU-1. Effect of mitomycin C on extracellular DNA production. Agric Biol Chem 45:2457–2461
    • (1981) Agric Biol Chem , vol.45 , pp. 2457-2461
    • Hara, T.1    Ueda, S.2
  • 24
    • 36849007038 scopus 로고    scopus 로고
    • Synthesis of 5-fluoropyrimidine nucleotides as sensitive NMR probes of RNA structure
    • COI: 1:CAS:528:DC%2BD2sXht12gs7zN, PID: 17990877
    • Hennig M, Scott LG, Sperling E, Bermel W, Williamson JR (2007) Synthesis of 5-fluoropyrimidine nucleotides as sensitive NMR probes of RNA structure. J Am Chem Soc 129:14911–14921
    • (2007) J Am Chem Soc , vol.129 , pp. 14911-14921
    • Hennig, M.1    Scott, L.G.2    Sperling, E.3    Bermel, W.4    Williamson, J.R.5
  • 25
    • 77955055053 scopus 로고    scopus 로고
    • Production of 2-deoxyribose 5-phosphate from fructose to demonstrate a potential of artificial bio-synthetic pathway using thermophilic enzymes
    • COI: 1:CAS:528:DC%2BC3cXptlWmtbc%3D, PID: 20547190
    • Honda K, Maya S, Omasa T, Hirota R, Kuroda A, Ohtake H (2010) Production of 2-deoxyribose 5-phosphate from fructose to demonstrate a potential of artificial bio-synthetic pathway using thermophilic enzymes. J Biotechnol 148:204–207
    • (2010) J Biotechnol , vol.148 , pp. 204-207
    • Honda, K.1    Maya, S.2    Omasa, T.3    Hirota, R.4    Kuroda, A.5    Ohtake, H.6
  • 27
    • 33745500982 scopus 로고    scopus 로고
    • Efficient production of 2-deoxyribose 5-phosphate from glucose and acetaldehyde by coupling of the alcoholic fermentation system of Baker’s yeast and deoxyriboaldolase-expressing Escherichia coli
    • COI: 1:CAS:528:DC%2BD28XmslWktbo%3D, PID: 16794316
    • Horinouchi N, Ogawa J, Kawano T, Sakai T, Saito K, Matsumoto S, Sasaki M, Mikami Y, Shimizu S (2006b) Efficient production of 2-deoxyribose 5-phosphate from glucose and acetaldehyde by coupling of the alcoholic fermentation system of Baker’s yeast and deoxyriboaldolase-expressing Escherichia coli. Biosci Biotechnol Biochem 70:1371–1378
    • (2006) Biosci Biotechnol Biochem , vol.70 , pp. 1371-1378
    • Horinouchi, N.1    Ogawa, J.2    Kawano, T.3    Sakai, T.4    Saito, K.5    Matsumoto, S.6    Sasaki, M.7    Mikami, Y.8    Shimizu, S.9
  • 28
  • 29
    • 71749116843 scopus 로고    scopus 로고
    • Screening and characterization of a phosphopentomutase useful for enzymatic production of 2′-deoxyribonucleoside
    • COI: 1:CAS:528:DC%2BD1MXht1GmtbnF, PID: 19818317
    • Horinouchi N, Kawano T, Sakai T, Matsumoto S, Sasaki M, Mikami Y, Ogawa J, Shimizu S (2009) Screening and characterization of a phosphopentomutase useful for enzymatic production of 2′-deoxyribonucleoside. N Biotechnol 26:75–82
    • (2009) N Biotechnol , vol.26 , pp. 75-82
    • Horinouchi, N.1    Kawano, T.2    Sakai, T.3    Matsumoto, S.4    Sasaki, M.5    Mikami, Y.6    Ogawa, J.7    Shimizu, S.8
  • 30
    • 84862216636 scopus 로고    scopus 로고
    • Construction of microbial platform for an energy-requiring bioprocess: practical 2′-deoxyribonucleoside production involving a C−C coupling reaction with high energy substrates
    • COI: 1:CAS:528:DC%2BC38XhtlWrs7nN, PID: 22709572
    • Horinouchi N, Sakai T, Kawano T, Matsumoto S, Sasaki M, Hibi M, Shima J, Shimizu S, Ogawa J (2012) Construction of microbial platform for an energy-requiring bioprocess: practical 2′-deoxyribonucleoside production involving a C−C coupling reaction with high energy substrates. Microb Cell Fact 11:82
    • (2012) Microb Cell Fact , vol.11 , pp. 82
    • Horinouchi, N.1    Sakai, T.2    Kawano, T.3    Matsumoto, S.4    Sasaki, M.5    Hibi, M.6    Shima, J.7    Shimizu, S.8    Ogawa, J.9
  • 32
    • 16244376449 scopus 로고    scopus 로고
    • Whole organism biocatalysis
    • COI: 1:CAS:528:DC%2BD2MXivFSlsrk%3D, PID: 15811802
    • Ishige T, Honda K, Shimizu S (2005) Whole organism biocatalysis. Curr Opin Chem Biol 9:174–180
    • (2005) Curr Opin Chem Biol , vol.9 , pp. 174-180
    • Ishige, T.1    Honda, K.2    Shimizu, S.3
  • 33
    • 33749480823 scopus 로고    scopus 로고
    • Recombinant Escherichia coli-catalyzed production of cytidine 5′-triphosphate from cytidine 5′-monophosphate
    • COI: 1:CAS:528:DC%2BD28XhtVKgurzP
    • Lee S, Kim B (2006) Recombinant Escherichia coli-catalyzed production of cytidine 5′-triphosphate from cytidine 5′-monophosphate. J Ind Eng Chem 12:757
    • (2006) J Ind Eng Chem , vol.12 , pp. 757
    • Lee, S.1    Kim, B.2
  • 34
  • 35
    • 84925880416 scopus 로고    scopus 로고
    • One-pot process of 2′-deoxyguanylic acid catalyzed by a multi-enzyme system
    • Li Y, Ding Q, Ou L, Qian Y, Zhang J (2015) One-pot process of 2′-deoxyguanylic acid catalyzed by a multi-enzyme system. Biotechnol Bioprocess Eng 20:37–43
    • (2015) Biotechnol Bioprocess Eng , vol.20 , pp. 37-43
    • Li, Y.1    Ding, Q.2    Ou, L.3    Qian, Y.4    Zhang, J.5
  • 36
    • 77954309447 scopus 로고    scopus 로고
    • Enzymatic synthesis of 2′-deoxyadenosine and 6-methylpurine-2′-deoxyriboside by Escherichia coli DH5α overexpressing nucleoside phosphorylases from Escherichia coli BL21
    • COI: 1:CAS:528:DC%2BC3cXhtlyqtbbF, PID: 20547356
    • Liang S, Li W, Gao T, Zhu X, Yang G, Ren D (2010) Enzymatic synthesis of 2′-deoxyadenosine and 6-methylpurine-2′-deoxyriboside by Escherichia coli DH5α overexpressing nucleoside phosphorylases from Escherichia coli BL21. J Biosci Bioeng 110:165–168
    • (2010) J Biosci Bioeng , vol.110 , pp. 165-168
    • Liang, S.1    Li, W.2    Gao, T.3    Zhu, X.4    Yang, G.5    Ren, D.6
  • 38
  • 40
    • 67649984188 scopus 로고    scopus 로고
    • Synthesis of 9-beta-d-arabinofuranosylguanine by combined use of two whole cell biocatalysts
    • PID: 19523826
    • Médici R, Lewkowicz ES, Iribarren AM (2009) Synthesis of 9-beta-d-arabinofuranosylguanine by combined use of two whole cell biocatalysts. Bioorg Med Chem Lett 19:4210–4212
    • (2009) Bioorg Med Chem Lett , vol.19 , pp. 4210-4212
    • Médici, R.1    Lewkowicz, E.S.2    Iribarren, A.M.3
  • 41
    • 33847766105 scopus 로고    scopus 로고
    • Biotechnology of nucleic acid constituents—state of the art and perspectives
    • COI: 1:CAS:528:DC%2BD2sXis1ars7k%3D
    • Mikhailopulo IA (2007) Biotechnology of nucleic acid constituents—state of the art and perspectives. Curr Org Chem 11:317–335
    • (2007) Curr Org Chem , vol.11 , pp. 317-335
    • Mikhailopulo, I.A.1
  • 42
    • 79953840829 scopus 로고    scopus 로고
    • Biologically important nucleosides: modern trends in biotechnology and application
    • COI: 1:CAS:528:DC%2BC3MXksFGlsLc%3D
    • Mikhailopulo IA, Miroshnikov AI (2011) Biologically important nucleosides: modern trends in biotechnology and application. Mendeleev Commun 21:57–68
    • (2011) Mendeleev Commun , vol.21 , pp. 57-68
    • Mikhailopulo, I.A.1    Miroshnikov, A.I.2
  • 43
    • 0031435281 scopus 로고    scopus 로고
    • A novel process of inosine 5′-monophosphate production using overexpressed guanosine/inosine kinase
    • COI: 1:CAS:528:DyaK1cXht1altLg%3D, PID: 9457797
    • Mori H, Iida A, Fujio T, Teshiba S (1997) A novel process of inosine 5′-monophosphate production using overexpressed guanosine/inosine kinase. Appl Microbiol Biotechnol 48:693–698
    • (1997) Appl Microbiol Biotechnol , vol.48 , pp. 693-698
    • Mori, H.1    Iida, A.2    Fujio, T.3    Teshiba, S.4
  • 44
    • 84922016929 scopus 로고    scopus 로고
    • Nucleoside antibiotics: biosynthesis, regulation, and biotechnology
    • PID: 25468791
    • Niu G, Tan H (2014) Nucleoside antibiotics: biosynthesis, regulation, and biotechnology. Trends Microbiol 23:110–119
    • (2014) Trends Microbiol , vol.23 , pp. 110-119
    • Niu, G.1    Tan, H.2
  • 45
    • 84870836233 scopus 로고    scopus 로고
    • Use of Citrobacter koseri whole cells for the production of arabinonucleosides: a larger scale approach
    • Nóbile M, Médici R, Terreni M, Lewkowicz ES, Iribarren AM (2012) Use of Citrobacter koseri whole cells for the production of arabinonucleosides: a larger scale approach. Process Biochem 47:2182–2188
    • (2012) Process Biochem , vol.47 , pp. 2182-2188
    • Nóbile, M.1    Médici, R.2    Terreni, M.3    Lewkowicz, E.S.4    Iribarren, A.M.5
  • 47
    • 84921734722 scopus 로고    scopus 로고
    • Enzymatic fluorination and biotechnological developments of the fluorinase
    • PID: 25253234
    • O’Hagan D, Deng H (2014) Enzymatic fluorination and biotechnological developments of the fluorinase. Chem Rev 115:634–649
    • (2014) Chem Rev , vol.115 , pp. 634-649
    • O’Hagan, D.1    Deng, H.2
  • 48
    • 0037604645 scopus 로고    scopus 로고
    • Microbial production of 2-deoxyribose 5-phosphate from acetaldehyde and triosephosphate for the synthesis of 2′-deoxyribonucleosides
    • COI: 1:CAS:528:DC%2BD3sXjslOmu7o%3D, PID: 12784646
    • Ogawa J, Saito K, Sakai T, Horinouchi N, Kawano T, Matsumoto S, Sasaki M, Mikami Y, Shimizu S (2003) Microbial production of 2-deoxyribose 5-phosphate from acetaldehyde and triosephosphate for the synthesis of 2′-deoxyribonucleosides. Biosci Biotechnol Biochem 67:933–936
    • (2003) Biosci Biotechnol Biochem , vol.67 , pp. 933-936
    • Ogawa, J.1    Saito, K.2    Sakai, T.3    Horinouchi, N.4    Kawano, T.5    Matsumoto, S.6    Sasaki, M.7    Mikami, Y.8    Shimizu, S.9
  • 50
    • 84876733182 scopus 로고    scopus 로고
    • Enzyme catalysed tandem reactions
    • COI: 1:CAS:528:DC%2BC3sXjvVOgtbk%3D, PID: 23490810
    • Oroz-Guinea I, García-Junceda E (2013) Enzyme catalysed tandem reactions. Curr Opin Chem Biol 17:236–249
    • (2013) Curr Opin Chem Biol , vol.17 , pp. 236-249
    • Oroz-Guinea, I.1    García-Junceda, E.2
  • 51
    • 0031462433 scopus 로고    scopus 로고
    • Enzymatic synthesis of thymidine using bacterial whole cells and isolated purine nucleoside phosphorylase
    • COI: 1:CAS:528:DyaK2sXnvFWrsLo%3D
    • Pal S, Nair V (1997) Enzymatic synthesis of thymidine using bacterial whole cells and isolated purine nucleoside phosphorylase. Biocatal Biotransformation 15:147–158
    • (1997) Biocatal Biotransformation , vol.15 , pp. 147-158
    • Pal, S.1    Nair, V.2
  • 52
    • 67650685040 scopus 로고    scopus 로고
    • Enzymology of purine and pyrimidine antimetabolites used in the treatment of cancer
    • COI: 1:CAS:528:DC%2BD1MXmsFanu70%3D, PID: 19476376
    • Parker WB (2009) Enzymology of purine and pyrimidine antimetabolites used in the treatment of cancer. Chem Rev 109:2880–2893
    • (2009) Chem Rev , vol.109 , pp. 2880-2893
    • Parker, W.B.1
  • 53
    • 0032853663 scopus 로고    scopus 로고
    • Nucleoside synthesis mediated by glycosyl transferring enzymes
    • COI: 1:CAS:528:DyaK1MXivVWrsr4%3D
    • Prasad AK, Trikha S, Parmar VS (1999) Nucleoside synthesis mediated by glycosyl transferring enzymes. Bioorg Chem 27:135–154
    • (1999) Bioorg Chem , vol.27 , pp. 135-154
    • Prasad, A.K.1    Trikha, S.2    Parmar, V.S.3
  • 54
    • 84908070020 scopus 로고    scopus 로고
    • Phosphorylation of uridine and cytidine by uridine–cytidine kinase
    • COI: 1:CAS:528:DC%2BC2cXhsVOnu7nP
    • Qian Y, Ding Q, Li Y, Zou Z, Yan B, Ou L (2014) Phosphorylation of uridine and cytidine by uridine–cytidine kinase. J Biotechnol 188:81–87
    • (2014) J Biotechnol , vol.188 , pp. 81-87
    • Qian, Y.1    Ding, Q.2    Li, Y.3    Zou, Z.4    Yan, B.5    Ou, L.6
  • 55
    • 80052812654 scopus 로고    scopus 로고
    • Multi‐enzymatic cascade reactions: overview and perspectives
    • COI: 1:CAS:528:DC%2BC3MXhtVOmsb7E
    • Ricca E, Brucher B, Schrittwieser JH (2011) Multi‐enzymatic cascade reactions: overview and perspectives. Adv Synth Catal 353:2239–2262
    • (2011) Adv Synth Catal , vol.353 , pp. 2239-2262
    • Ricca, E.1    Brucher, B.2    Schrittwieser, J.H.3
  • 57
    • 33750601477 scopus 로고    scopus 로고
    • Purine nucleoside analogs as immunosuppressive and antineoplastic agents: mechanism of action and clinical activity
    • COI: 1:CAS:528:DC%2BD28XhtVClurjN, PID: 17168705
    • Robak T, Lech-Maranda E, Korycka A, Robak E (2006) Purine nucleoside analogs as immunosuppressive and antineoplastic agents: mechanism of action and clinical activity. Curr Med Chem 13:3165–3189
    • (2006) Curr Med Chem , vol.13 , pp. 3165-3189
    • Robak, T.1    Lech-Maranda, E.2    Korycka, A.3    Robak, E.4
  • 58
    • 9744235812 scopus 로고    scopus 로고
    • Immobilization and stabilization of recombinant multimeric uridine and purine nucleoside phosphorylases from Bacillus subtilis
    • COI: 1:CAS:528:DC%2BD2cXnt12gsrw%3D, PID: 15530033
    • Rocchietti S, Ubiali D, Terreni M, Albertini AM, Fernández-Lafuente R, Guisán JM, Pregnolato M (2004) Immobilization and stabilization of recombinant multimeric uridine and purine nucleoside phosphorylases from Bacillus subtilis. Biomacromolecules 5:2195–2200
    • (2004) Biomacromolecules , vol.5 , pp. 2195-2200
    • Rocchietti, S.1    Ubiali, D.2    Terreni, M.3    Albertini, A.M.4    Fernández-Lafuente, R.5    Guisán, J.M.6    Pregnolato, M.7
  • 59
    • 84929521862 scopus 로고    scopus 로고
    • Sánchez-Moreno I, Oroz-Guinea I, Iturrate L, García-Junceda E (2012) ChemInform Abstract: Multienzyme Reactions (Weinheim: Wiley-VCH) 44 (29)
    • Sánchez-Moreno I, Oroz-Guinea I, Iturrate L, García-Junceda E (2012) ChemInform Abstract: Multienzyme Reactions (Weinheim: Wiley-VCH) 44 (29)
  • 60
    • 53149118243 scopus 로고    scopus 로고
    • Pathway engineered enzymatic de novo purine nucleotide synthesis
    • COI: 1:CAS:528:DC%2BD1cXpvVSis7g%3D, PID: 18707057
    • Schultheisz HL, Szymczyna BR, Scott LG, Williamson JR (2008) Pathway engineered enzymatic de novo purine nucleotide synthesis. ACS Chem Biol 3:499–511
    • (2008) ACS Chem Biol , vol.3 , pp. 499-511
    • Schultheisz, H.L.1    Szymczyna, B.R.2    Scott, L.G.3    Williamson, J.R.4
  • 62
    • 35548961049 scopus 로고    scopus 로고
    • Synthesis of nucleotide analogues by a promiscuous phosphoribosyltransferase
    • COI: 1:CAS:528:DC%2BD2sXhtVarsrvI, PID: 17854193
    • Scism RA, Stec DF, Bachmann BO (2007) Synthesis of nucleotide analogues by a promiscuous phosphoribosyltransferase. Org Lett 9:4179–4182
    • (2007) Org Lett , vol.9 , pp. 4179-4182
    • Scism, R.A.1    Stec, D.F.2    Bachmann, B.O.3
  • 63
    • 75649116134 scopus 로고    scopus 로고
    • Five‐component cascade synthesis of nucleotide analogues in an engineered self‐immobilized enzyme aggregate
    • COI: 1:CAS:528:DC%2BD1MXhs1SqtLvL, PID: 19918830
    • Scism RA, Bachmann BO (2010) Five‐component cascade synthesis of nucleotide analogues in an engineered self‐immobilized enzyme aggregate. ChemBioChem 11:67–70
    • (2010) ChemBioChem , vol.11 , pp. 67-70
    • Scism, R.A.1    Bachmann, B.O.2
  • 64
    • 4644322804 scopus 로고    scopus 로고
    • Enzymatic synthesis and 19F NMR studies of 2-fluoroadenine-substituted RNA
    • COI: 1:CAS:528:DC%2BD2cXntFGhs7w%3D, PID: 15382896
    • Scott LG, Geierstanger BH, Williamson JR, Hennig M (2004) Enzymatic synthesis and 19F NMR studies of 2-fluoroadenine-substituted RNA. J Am Chem Soc 126:11776–11777
    • (2004) J Am Chem Soc , vol.126 , pp. 11776-11777
    • Scott, L.G.1    Geierstanger, B.H.2    Williamson, J.R.3    Hennig, M.4
  • 65
    • 84874143770 scopus 로고    scopus 로고
    • Developing a collection of immobilized nucleoside phosphorylases for the preparation of nucleoside analogues: enzymatic synthesis of arabinosyladenine and 2′, 3′‐dideoxyinosine
    • COI: 1:CAS:528:DC%2BC3sXis12qu7g%3D
    • Serra I, Ubiali D, Piškur J, Christoffersen S, Lewkowicz ES, Iribarren AM, Albertini AM, Terreni M (2013) Developing a collection of immobilized nucleoside phosphorylases for the preparation of nucleoside analogues: enzymatic synthesis of arabinosyladenine and 2′, 3′‐dideoxyinosine. Chem Plus Chem 78:157–165
    • (2013) Chem Plus Chem , vol.78 , pp. 157-165
    • Serra, I.1    Ubiali, D.2    Piškur, J.3    Christoffersen, S.4    Lewkowicz, E.S.5    Iribarren, A.M.6    Albertini, A.M.7    Terreni, M.8
  • 66
    • 0034846337 scopus 로고    scopus 로고
    • Recombinant bacterial cells as efficient biocatalysts for the production of nucleosides
    • COI: 1:CAS:528:DC%2BD3MXmslGju7w%3D
    • Spoldi E, Ghisotti D, Cali S, Grisa M, Orsini G, Tonon G, Zuffi G (2001) Recombinant bacterial cells as efficient biocatalysts for the production of nucleosides. Nucleos Nucleot Nucl 20:977–979
    • (2001) Nucleos Nucleot Nucl , vol.20 , pp. 977-979
    • Spoldi, E.1    Ghisotti, D.2    Cali, S.3    Grisa, M.4    Orsini, G.5    Tonon, G.6    Zuffi, G.7
  • 67
    • 0342599734 scopus 로고
    • Extracellular accumulation of DNA by hydrocarbonutilizing bacteria
    • COI: 1:CAS:528:DyaE38XhtFShsLw%3D
    • Tomita F, Suzuki T (1972) Extracellular accumulation of DNA by hydrocarbonutilizing bacteria. Agric Biol Chem 36:133–140
    • (1972) Agric Biol Chem , vol.36 , pp. 133-140
    • Tomita, F.1    Suzuki, T.2
  • 68
    • 0037450932 scopus 로고    scopus 로고
    • Purine nucleoside synthesis from uridine using immobilised Enterobacter gergoviae CECT 875 whole cells
    • COI: 1:CAS:528:DC%2BD3sXhs1alsLk%3D
    • Trelles J, Fernandez M, Lewkowicz E, Iribarren A, Sinisterra J (2003) Purine nucleoside synthesis from uridine using immobilised Enterobacter gergoviae CECT 875 whole cells. Tetrahedron Lett 44:2605–2609
    • (2003) Tetrahedron Lett , vol.44 , pp. 2605-2609
    • Trelles, J.1    Fernandez, M.2    Lewkowicz, E.3    Iribarren, A.4    Sinisterra, J.5
  • 69
    • 7044263040 scopus 로고    scopus 로고
    • Synthesis of 2′‐deoxynucleosides by transglycosylation with new immobilized and stabilized uridine phosphorylase and purine nucleoside phosphorylase
    • COI: 1:CAS:528:DC%2BD2cXoslegt70%3D
    • Ubiali D, Rocchietti S, Scaramozzino F, Terreni M, Albertini AM, Fernández‐Lafuente R, Guisán JM, Pregnolato M (2004) Synthesis of 2′‐deoxynucleosides by transglycosylation with new immobilized and stabilized uridine phosphorylase and purine nucleoside phosphorylase. Adv Synth Catal 346:1361–1366
    • (2004) Adv Synth Catal , vol.346 , pp. 1361-1366
    • Ubiali, D.1    Rocchietti, S.2    Scaramozzino, F.3    Terreni, M.4    Albertini, A.M.5    Fernández‐Lafuente, R.6    Guisán, J.M.7    Pregnolato, M.8
  • 70
    • 0033545518 scopus 로고    scopus 로고
    • Enzymatic preparation of nucleoside antibiotics
    • COI: 1:CAS:528:DyaK1MXnsl2rtA%3D%3D
    • Utagawa T (1999) Enzymatic preparation of nucleoside antibiotics. J Mol Catal B Enzym 6:215–222
    • (1999) J Mol Catal B Enzym , vol.6 , pp. 215-222
    • Utagawa, T.1
  • 71
    • 84940004083 scopus 로고    scopus 로고
    • New biocatalysts for one pot multistep enzymatic synthesis of pyrimidine nucleoside diphosphates from readily available reagents
    • Valino AL, Iribarren AM, Lewkowicz E (2015) New biocatalysts for one pot multistep enzymatic synthesis of pyrimidine nucleoside diphosphates from readily available reagents. J Mol Catal B Enzym 114:58–64
    • (2015) J Mol Catal B Enzym , vol.114 , pp. 58-64
    • Valino, A.L.1    Iribarren, A.M.2    Lewkowicz, E.3
  • 73
    • 78651404436 scopus 로고    scopus 로고
    • Stabilization of Escherichia coli uridine phosphorylase by evolution and immobilization
    • COI: 1:CAS:528:DC%2BC3MXmsV2huw%3D%3D
    • Visser DF, Hennessy F, Rashamuse J, Pletschke B, Brady D (2011) Stabilization of Escherichia coli uridine phosphorylase by evolution and immobilization. J Mol Catal B Enzym 68:279–285
    • (2011) J Mol Catal B Enzym , vol.68 , pp. 279-285
    • Visser, D.F.1    Hennessy, F.2    Rashamuse, J.3    Pletschke, B.4    Brady, D.5
  • 74
    • 0038288783 scopus 로고    scopus 로고
    • A combination chemical and enzymatic approach for the preparation of azole carboxamide nucleoside triphosphate
    • COI: 1:CAS:528:DC%2BD3sXis1ertb0%3D, PID: 12737564
    • Wu W, Bergstrom DE, Davisson VJ (2003) A combination chemical and enzymatic approach for the preparation of azole carboxamide nucleoside triphosphate. J Org Chem 68:3860–3865
    • (2003) J Org Chem , vol.68 , pp. 3860-3865
    • Wu, W.1    Bergstrom, D.E.2    Davisson, V.J.3
  • 75
    • 0034605579 scopus 로고    scopus 로고
    • A novel enzymatic method for the production of purine-2′-deoxyribonucleosides
    • COI: 1:CAS:528:DC%2BD3cXltVGqs7o%3D
    • Yokozeki K, Tsuji T (2000) A novel enzymatic method for the production of purine-2′-deoxyribonucleosides. J Mol Catal B 10:207–213
    • (2000) J Mol Catal B , vol.10 , pp. 207-213
    • Yokozeki, K.1    Tsuji, T.2
  • 76
    • 84875364367 scopus 로고    scopus 로고
    • Recombinant purine nucleoside phosphorylases from thermophiles: preparation, properties and activity towards purine and pyrimidine nucleosides
    • COI: 1:CAS:528:DC%2BC3sXjvFWlt7c%3D, PID: 23332162
    • Zhou X, Szeker K, Janocha B, Böhme T, Albrecht D, Mikhailopulo IA, Neubauer P (2013) Recombinant purine nucleoside phosphorylases from thermophiles: preparation, properties and activity towards purine and pyrimidine nucleosides. FEBS J 280:1475–1490
    • (2013) FEBS J , vol.280 , pp. 1475-1490
    • Zhou, X.1    Szeker, K.2    Janocha, B.3    Böhme, T.4    Albrecht, D.5    Mikhailopulo, I.A.6    Neubauer, P.7
  • 77
    • 84926631127 scopus 로고    scopus 로고
    • Synthesis of 2,6‐dihalogenated purine nucleosides by thermostable nucleoside phosphorylases
    • COI: 1:CAS:528:DC%2BC2MXltlKhtrg%3D
    • Zhou X, Szeker K, Jiao L, Oestreich M, Mikhailopulo IA, Neubauer P (2015a) Synthesis of 2,6‐dihalogenated purine nucleosides by thermostable nucleoside phosphorylases. Adv Synt Catal 357:1237–1244
    • (2015) Adv Synt Catal , vol.357 , pp. 1237-1244
    • Zhou, X.1    Szeker, K.2    Jiao, L.3    Oestreich, M.4    Mikhailopulo, I.A.5    Neubauer, P.6
  • 78
    • 84924346264 scopus 로고    scopus 로고
    • Immobilization of thermostable nucleoside phosphorylases on MagReSyn® epoxide microspheres and their application for the synthesis of 2,6-dihalogenated purine nucleosides
    • COI: 1:CAS:528:DC%2BC2MXjs1aitLg%3D
    • Zhou X, Mikhailopulo IA, Bournazou MNC, Neubauer P (2015b) Immobilization of thermostable nucleoside phosphorylases on MagReSyn® epoxide microspheres and their application for the synthesis of 2,6-dihalogenated purine nucleosides. J Mol Catal B Enzym 115:119–127
    • (2015) J Mol Catal B Enzym , vol.115 , pp. 119-127
    • Zhou, X.1    Mikhailopulo, I.A.2    Bournazou, M.N.C.3    Neubauer, P.4
  • 79
    • 84862786921 scopus 로고    scopus 로고
    • Two-step efficient synthesis of 5-methyluridine via two thermostable nucleoside phosphorylase from Aeropyrum pernix
    • COI: 1:CAS:528:DC%2BC38XitFyjt7k%3D, PID: 22325947
    • Zhu S, Ren L, Wang J, Zheng G, Tang P (2012) Two-step efficient synthesis of 5-methyluridine via two thermostable nucleoside phosphorylase from Aeropyrum pernix. Bioorg Med Chem Lett 22:2102–2104
    • (2012) Bioorg Med Chem Lett , vol.22 , pp. 2102-2104
    • Zhu, S.1    Ren, L.2    Wang, J.3    Zheng, G.4    Tang, P.5
  • 80
    • 0025356904 scopus 로고
    • Synthesis of 9-(β-d-arabinofuranosyl) guanine using whole cells of Escherichia coli
    • COI: 1:CAS:528:DyaK3cXitFGisbw%3D, PID: 1367439
    • Zinchenko A, Barai V, Bokut S, Kvasyuk E, Mikhailopulo I (1990) Synthesis of 9-(β-d-arabinofuranosyl) guanine using whole cells of Escherichia coli. Appl Microbiol Biotechnol 32:658–661
    • (1990) Appl Microbiol Biotechnol , vol.32 , pp. 658-661
    • Zinchenko, A.1    Barai, V.2    Bokut, S.3    Kvasyuk, E.4    Mikhailopulo, I.5
  • 81
    • 1842588409 scopus 로고    scopus 로고
    • Immobilized biocatalysts for the production of nucleosides and nucleoside analogues by enzymatic transglycosylation reactions
    • COI: 1:CAS:528:DC%2BD2cXjtFKqu7o%3D
    • Zuffi G, Ghisotti D, Oliva I, Capra E, Frascotti G, Tonon G, Orsini G (2004) Immobilized biocatalysts for the production of nucleosides and nucleoside analogues by enzymatic transglycosylation reactions. Biocatal Biotransformation 22:25–33
    • (2004) Biocatal Biotransformation , vol.22 , pp. 25-33
    • Zuffi, G.1    Ghisotti, D.2    Oliva, I.3    Capra, E.4    Frascotti, G.5    Tonon, G.6    Orsini, G.7


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