메뉴 건너뛰기




Volumn 6, Issue SEP, 2015, Pages

A water-forming NADH oxidase from Lactobacillus pentosus suitable for the regeneration of synthetic biomimetic cofactors

Author keywords

Biomimetic cofactors; Cofactor regeneration; Flavin adenine dinucleotide; H2O forming NADH oxidase; Hydrogen peroxide; Lactobacillus pentosus; Synthetic cofactors

Indexed keywords

FLAVINE ADENINE NUCLEOTIDE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE DEHYDROGENASE;

EID: 84946707080     PISSN: None     EISSN: 1664302X     Source Type: Journal    
DOI: 10.3389/fmicb.2015.00957     Document Type: Article
Times cited : (65)

References (44)
  • 2
    • 84855968755 scopus 로고    scopus 로고
    • Enzymatic biofuel cells utilizing a biomimetic cofactor
    • Campbell, E., Meredith, M., Minteer, S. D., and Banta, S. (2012). Enzymatic biofuel cells utilizing a biomimetic cofactor. Chem. Commun. 48, 1898-1900. doi: 10.1039/c2cc16156g
    • (2012) Chem. Commun , vol.48 , pp. 1898-1900
    • Campbell, E.1    Meredith, M.2    Minteer, S.D.3    Banta, S.4
  • 3
    • 0027215943 scopus 로고
    • A simple and rapid method for the preparation of gram-negative bacterial genomic DNA
    • Chen, W. P., and Kuo, T. T. (1993). A simple and rapid method for the preparation of gram-negative bacterial genomic DNA. Nucleic Acids Res. 21, 2260. doi: 10.1093/nar/21.9.2260
    • (1993) Nucleic Acids Res , vol.21 , pp. 2260
    • Chen, W.P.1    Kuo, T.T.2
  • 4
    • 0026773434 scopus 로고
    • Identification of novel reduced pyridinium derivatives as synthetic cofactors for the enzyme DT diophorase (NAD(P)H dehydrogenase (quinone), EC 1.6.99.2)
    • Friedlos, F., Jarman, M., Davies, L. C., Boland, M. P., and Knox, R. J. (1992). Identification of novel reduced pyridinium derivatives as synthetic cofactors for the enzyme DT diophorase (NAD(P)H dehydrogenase (quinone), EC 1.6.99.2). Biochem. Pharmacol. 44, 25-31. doi: 10.1016/0006-2952(92)90033-f
    • (1992) Biochem. Pharmacol , vol.44 , pp. 25-31
    • Friedlos, F.1    Jarman, M.2    Davies, L.C.3    Boland, M.P.4    Knox, R.J.5
  • 5
    • 84857367018 scopus 로고    scopus 로고
    • Characterization of H2O-forming NADH oxidase from Streptococcus pyogenes and its application in l-rare sugar production
    • Gao, H., Tiwari, M. K., Kang, Y. C., and Lee, J.-K. (2012). Characterization of H2O-forming NADH oxidase from Streptococcus pyogenes and its application in l-rare sugar production. Bioorg. Med. Chem. Lett. 22, 1931-1935. doi: 10.1016/j.bmcl.2012.01.049
    • (2012) Bioorg. Med. Chem. Lett , vol.22 , pp. 1931-1935
    • Gao, H.1    Tiwari, M.K.2    Kang, Y.C.3    Lee, J.-K.4
  • 6
    • 0037415359 scopus 로고    scopus 로고
    • NADH oxidase from Lactobacillus brevis: a new catalyst for the regeneration of NAD
    • Geueke, B., Riebel, B., and Hummel, W. (2003). NADH oxidase from Lactobacillus brevis: a new catalyst for the regeneration of NAD. Enzyme Microbial. Technol. 32, 205-211. doi: 10.1016/S0141-0229(02)00290-9
    • (2003) Enzyme Microbial. Technol , vol.32 , pp. 205-211
    • Geueke, B.1    Riebel, B.2    Hummel, W.3
  • 7
    • 0035929741 scopus 로고    scopus 로고
    • Enhanced acid stability of a reduced nicotinamide adenine dinucleotide (NADH) analogue
    • Hentall, P. L., Flowers, N., and Bugg, T. D. H. (2001). Enhanced acid stability of a reduced nicotinamide adenine dinucleotide (NADH) analogue. Chem. Commun. 2098-2099. doi: 10.1039/B107634P
    • (2001) Chem. Commun , pp. 2098-2099
    • Hentall, P.L.1    Flowers, N.2    Bugg, T.D.H.3
  • 9
    • 33746891860 scopus 로고    scopus 로고
    • Cofactor engineering in Saccharomyces cerevisiae: expression of a H2O-forming NADH oxidase and impact on redox metabolism
    • Heux, S., Cachon, R., and Dequin, S. (2006). Cofactor engineering in Saccharomyces cerevisiae: expression of a H2O-forming NADH oxidase and impact on redox metabolism. Metab. Eng. 8, 303-314. doi: 10.1016/j.ymben.2005.12.003
    • (2006) Metab. Eng , vol.8 , pp. 303-314
    • Heux, S.1    Cachon, R.2    Dequin, S.3
  • 10
    • 0027442902 scopus 로고
    • Identification of two distinct NADH oxidases corresponding to H2O2-forming oxidase and H2O-forming oxidase induced in Streptococcus mutans
    • Higuchi, M., Shimada, M., Yamamoto, Y., Hayashi, T., Koga, T., and Kamio, Y. (1993). Identification of two distinct NADH oxidases corresponding to H2O2-forming oxidase and H2O-forming oxidase induced in Streptococcus mutans. J. Gen. Microbiol. 139, 2343-2351. doi: 10.1099/00221287-139-10-2343
    • (1993) J. Gen. Microbiol , vol.139 , pp. 2343-2351
    • Higuchi, M.1    Shimada, M.2    Yamamoto, Y.3    Hayashi, T.4    Koga, T.5    Kamio, Y.6
  • 11
    • 0037262411 scopus 로고    scopus 로고
    • Isolation and biochemical characterization of a new NADH oxidase from Lactobacillus brevis
    • Hummel, W., and Riebel, B. (2003). Isolation and biochemical characterization of a new NADH oxidase from Lactobacillus brevis. Biotechnol. Lett. 25, 51-54. doi: 10.1023/a:1021730131633
    • (2003) Biotechnol. Lett , vol.25 , pp. 51-54
    • Hummel, W.1    Riebel, B.2
  • 12
    • 53849112300 scopus 로고    scopus 로고
    • Hexameric ring structure of a thermophilic archaeon NADH oxidase that produces predominantly H2O
    • Jia, B., Park, S.-C., Lee, S., Pham, B. P., Yu, R., Le, T. L., et al. (2008). Hexameric ring structure of a thermophilic archaeon NADH oxidase that produces predominantly H2O. FEBS J. 275, 5355-5366. doi: 10.1111/j.1742-4658.2008.06665.x
    • (2008) FEBS J , vol.275 , pp. 5355-5366
    • Jia, B.1    Park, S.-C.2    Lee, S.3    Pham, B.P.4    Yu, R.5    Le, T.L.6
  • 13
    • 4644234429 scopus 로고    scopus 로고
    • Hydrogen peroxide-producing NADH oxidase (nox-1) from Lactococcus lactis
    • Jiang, R., and Bommarius, A. S. (2004). Hydrogen peroxide-producing NADH oxidase (nox-1) from Lactococcus lactis. Tetrahedron Asymmetry 15, 2939-2944. doi: 10.1016/j.tetasy.2004.07.057
    • (2004) Tetrahedron Asymmetry , vol.15 , pp. 2939-2944
    • Jiang, R.1    Bommarius, A.S.2
  • 14
    • 20544438578 scopus 로고    scopus 로고
    • Comparison of alkyl hydroperoxide reductase (AhpR) and water-forming NADH oxidase from Lactococcus lactis ATCC 19435
    • Jiang, R., Riebel, B. R., and Bommarius, A. S. (2005). Comparison of alkyl hydroperoxide reductase (AhpR) and water-forming NADH oxidase from Lactococcus lactis ATCC 19435. Adv. Synth. Catalysis 347, 1139-1146. doi: 10.1002/adsc.200505063
    • (2005) Adv. Synth. Catalysis , vol.347 , pp. 1139-1146
    • Jiang, R.1    Riebel, B.R.2    Bommarius, A.S.3
  • 16
    • 84982337797 scopus 로고
    • N-Alkyl-o-dihydro-nicotinsäure-amide
    • Karrer, P., and Stare, F. J. (1937). N-Alkyl-o-dihydro-nicotinsäure-amide. Helvetica Chimica Acta 20, 418-423. doi: 10.1002/hlca.19370200167
    • (1937) Helvetica Chimica Acta , vol.20 , pp. 418-423
    • Karrer, P.1    Stare, F.J.2
  • 17
    • 1842637847 scopus 로고    scopus 로고
    • Purification and characterization of an H2O-forming NADH oxidase from Clostridium aminovalericum: existence of an oxygen-detoxifying enzyme in an obligate anaerobic bacteria
    • Kawasaki, S., Ishikura, J., Chiba, D., Nishino, T., and Niimura, Y. (2004). Purification and characterization of an H2O-forming NADH oxidase from Clostridium aminovalericum: existence of an oxygen-detoxifying enzyme in an obligate anaerobic bacteria. Arch. Microbiol. 181, 324-330. doi: 10.1007/s00203-004-0659-653
    • (2004) Arch. Microbiol , vol.181 , pp. 324-330
    • Kawasaki, S.1    Ishikura, J.2    Chiba, D.3    Nishino, T.4    Niimura, Y.5
  • 18
    • 0029009389 scopus 로고
    • Virtual cofactors for an Escherichia coli nitroreductase enzyme: relevance to reductively activated prodrugs in antibody directed enzyme prodrug therapy (ADEPT)
    • Knox, R. J., Friedlos, F., Jarman, M., Davies, L. C., Goddard, P., Anlezark, G. M., et al. (1995). Virtual cofactors for an Escherichia coli nitroreductase enzyme: relevance to reductively activated prodrugs in antibody directed enzyme prodrug therapy (ADEPT). Biochem. Pharmacol. 49, 1641-1647. doi: 10.1016/0006-2952(95)00077-d
    • (1995) Biochem. Pharmacol , vol.49 , pp. 1641-1647
    • Knox, R.J.1    Friedlos, F.2    Jarman, M.3    Davies, L.C.4    Goddard, P.5    Anlezark, G.M.6
  • 19
    • 0033871181 scopus 로고    scopus 로고
    • Bioactivation of 5-(aziridin-1-yl)-2,4-dinitrobenzamide (CB 1954) by human NAD(P)H quinone oxidoreductase 2: a novel co-substrate-mediated antitumor prodrug therapy
    • Knox, R. J., Jenkins, T. C., Hobbs, S. M., Chen, S. A., Melton, R. G., and Burke, P. J. (2000). Bioactivation of 5-(aziridin-1-yl)-2,4-dinitrobenzamide (CB 1954) by human NAD(P)H quinone oxidoreductase 2: a novel co-substrate-mediated antitumor prodrug therapy. Cancer Res. 60, 4179-4186.
    • (2000) Cancer Res , vol.60 , pp. 4179-4186
    • Knox, R.J.1    Jenkins, T.C.2    Hobbs, S.M.3    Chen, S.A.4    Melton, R.G.5    Burke, P.J.6
  • 20
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. (1970). Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-685. doi: 10.1038/227680a0
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 21
    • 33747497810 scopus 로고    scopus 로고
    • The crystal structure of NAD (P)H oxidase from Lactobacillus sanfranciscensis: insights into the conversion of O-2 into two water molecules by the flavoenzyme
    • Lountos, G. T., Jiang, R., Wellborn, W. B., Thaler, T. L., Bommarius, A. S., and Orville, A. M. (2006). The crystal structure of NAD (P)H oxidase from Lactobacillus sanfranciscensis: insights into the conversion of O-2 into two water molecules by the flavoenzyme. Biochemistry 45, 9648-9659. doi: 10.1021/bi060692p
    • (2006) Biochemistry , vol.45 , pp. 9648-9659
    • Lountos, G.T.1    Jiang, R.2    Wellborn, W.B.3    Thaler, T.L.4    Bommarius, A.S.5    Orville, A.M.6
  • 22
    • 11844296083 scopus 로고    scopus 로고
    • Bioorganometallic chemistry: biocatalytic oxidation reactions with biomimetic NAD+/NADH co-factors and [Cp*Rh(bpy)H]+ for selective organic synthesis
    • Lutz, J., Hollmann, F., Ho, T. V., Schnyder, A., Fish, R. H., and Schmid, A. (2004). Bioorganometallic chemistry: biocatalytic oxidation reactions with biomimetic NAD+/NADH co-factors and [Cp*Rh(bpy)H]+ for selective organic synthesis. J. Organomet. Chem. 689, 4783-4790. doi: 10.1016/j.jorganchem.2004.09.044
    • (2004) J. Organomet. Chem , vol.689 , pp. 4783-4790
    • Lutz, J.1    Hollmann, F.2    Ho, T.V.3    Schnyder, A.4    Fish, R.H.5    Schmid, A.6
  • 23
    • 79952053501 scopus 로고    scopus 로고
    • Iron catalysis for in situ regeneration of oxidized cofactors by activation and reduction of molecular oxygen: a synthetic metalloporphyrin as a biomimetic NAD(P)H oxidase
    • Maid, H., Böhm, P., Huber, S. M., Bauer, W., Hummel, W., Jux, N., et al. (2011). Iron catalysis for in situ regeneration of oxidized cofactors by activation and reduction of molecular oxygen: a synthetic metalloporphyrin as a biomimetic NAD(P)H oxidase. Angew. Chem. Int. Ed.Engl. 50, 2397-2400. doi: 10.1002/anie.201004101
    • (2011) Angew. Chem. Int. Ed.Engl , vol.50 , pp. 2397-2400
    • Maid, H.1    Böhm, P.2    Huber, S.M.3    Bauer, W.4    Hummel, W.5    Jux, N.6
  • 24
    • 65349190562 scopus 로고    scopus 로고
    • Recent progress in biocatalysis for asymmetric oxidation and reduction
    • Matsuda, T., Yamanaka, R., and Nakamura, K. (2009). Recent progress in biocatalysis for asymmetric oxidation and reduction. Tetrahedron Asymmetry 20, 513-557. doi: 10.1016/j.tetasy.2008.12.035
    • (2009) Tetrahedron Asymmetry , vol.20 , pp. 513-557
    • Matsuda, T.1    Yamanaka, R.2    Nakamura, K.3
  • 25
    • 33947466443 scopus 로고
    • 1-Benzyldihydronicotinamide-a model for reduced DPN
    • Mauzerall, D., and Westheimer, F. H. (1955). 1-Benzyldihydronicotinamide-a model for reduced DPN. J. Am. Chem. Soc. 77, 2261-2264. doi: 10.1021/ja01613a070
    • (1955) J. Am. Chem. Soc , vol.77 , pp. 2261-2264
    • Mauzerall, D.1    Westheimer, F.H.2
  • 26
    • 79957979256 scopus 로고    scopus 로고
    • NAD(P)H oxidase V from Lactobacillus plantarum (NoxV) displays enhanced operational stability even in absence of reducing agents
    • Park, J. T., Hirano, J.-I., Thangavel, V., Riebel, B. R., and Bommarius, A. S. (2011). NAD(P)H oxidase V from Lactobacillus plantarum (NoxV) displays enhanced operational stability even in absence of reducing agents. J. Mol. Catalysis B Enzymatic 71, 159-165. doi: 10.1016/j.molcatb.2011.04.013
    • (2011) J. Mol. Catalysis B Enzymatic , vol.71 , pp. 159-165
    • Park, J.T.1    Hirano, J.-I.2    Thangavel, V.3    Riebel, B.R.4    Bommarius, A.S.5
  • 27
    • 84896749362 scopus 로고    scopus 로고
    • Is simpler better? Synthetic Nicotinamide cofactor analogues for redox chemistry
    • Paul, C. E., Arends, I. W. C. E., and Hollmann, F. (2014a). Is simpler better? Synthetic Nicotinamide cofactor analogues for redox chemistry. Acs Catalysis 4, 788-797. doi: 10.1021/cs4011056
    • (2014) Acs Catalysis , vol.4 , pp. 788-797
    • Paul, C.E.1    Arends, I.W.C.E.2    Hollmann, F.3
  • 29
    • 84874045759 scopus 로고    scopus 로고
    • Mimicking nature: synthetic nicotinamide cofactors for c-c bioreduction using enoate reductases
    • Paul, C. E., Gargiulo, S., Opperman, D. J., Lavandera, I., Gotor-Fernandez, V., Gotor, V., et al. (2013). Mimicking nature: synthetic nicotinamide cofactors for c-c bioreduction using enoate reductases. Org. Lett. 15, 180-183. doi: 10.1021/ol303240a
    • (2013) Org. Lett , vol.15 , pp. 180-183
    • Paul, C.E.1    Gargiulo, S.2    Opperman, D.J.3    Lavandera, I.4    Gotor-Fernandez, V.5    Gotor, V.6
  • 30
    • 84929497790 scopus 로고    scopus 로고
    • Nonenzymatic regeneration of styrene Monooxygenase for catalysis
    • Paul, C. E., Tischler, D., Riedel, A., Heine, T., Itoh, N., and Hollmann, F. (2015). Nonenzymatic regeneration of styrene Monooxygenase for catalysis. Acs Catalysis 5, 2961-2965. doi: 10.1021/acscatal.5b00041
    • (2015) Acs Catalysis , vol.5 , pp. 2961-2965
    • Paul, C.E.1    Tischler, D.2    Riedel, A.3    Heine, T.4    Itoh, N.5    Hollmann, F.6
  • 32
    • 0242607605 scopus 로고    scopus 로고
    • Cofactor regeneration of both NAD(+) from NADH and NADP(+) from NADPH: NADH oxidase from Lactobacillus sanfranciscensis
    • Riebel, B. R., Gibbs, P. R., Wellborn, W. B., and Bommarius, A. S. (2003). Cofactor regeneration of both NAD(+) from NADH and NADP(+) from NADPH: NADH oxidase from Lactobacillus sanfranciscensis. Adv. Synth. Catalysis 345, 707-712. doi: 10.1002/adsc.200303039
    • (2003) Adv. Synth. Catalysis , vol.345 , pp. 707-712
    • Riebel, B.R.1    Gibbs, P.R.2    Wellborn, W.B.3    Bommarius, A.S.4
  • 33
    • 83355167105 scopus 로고    scopus 로고
    • New biotechnological perspectives of a NADH oxidase variant from Thermus thermophilus HB27 as NAD+-recycling enzyme
    • Rocha-Martin, J., Vega, D., Bolivar, J. M., Godoy, C. A., Hidalgo, A., Berenguer, J., et al. (2011). New biotechnological perspectives of a NADH oxidase variant from Thermus thermophilus HB27 as NAD+-recycling enzyme. BMC Biotechnol. 11:101. doi: 10.1186/1472-6750-11-101
    • (2011) BMC Biotechnol , vol.11 , pp. 101
    • Rocha-Martin, J.1    Vega, D.2    Bolivar, J.M.3    Godoy, C.A.4    Hidalgo, A.5    Berenguer, J.6
  • 34
    • 84882379836 scopus 로고    scopus 로고
    • New biotechnology paradigm: cell-free biosystems for biomanufacturing
    • Rollin, J. A., Tam, T. K., and Zhang, Y. H. P. (2013). New biotechnology paradigm: cell-free biosystems for biomanufacturing. Green Chem. 15, 1708-1719. doi: 10.1039/C3GC40625C
    • (2013) Green Chem , vol.15 , pp. 1708-1719
    • Rollin, J.A.1    Tam, T.K.2    Zhang, Y.H.P.3
  • 35
    • 0032526286 scopus 로고    scopus 로고
    • Study of NADH stability using ultraviolet-visible spectrophotometric analysis and factorial design
    • Rover, L. Jr., Fernandes, J. C. B., Neto, G. D. O., Kubota, L. T., Katekawa, E., and Serrano, S. L. H. P. (1998). Study of NADH stability using ultraviolet-visible spectrophotometric analysis and factorial design. Anal. Biochem. 260, 50-55. doi: 10.1006/abio.1998.2656
    • (1998) Anal. Biochem , vol.260 , pp. 50-55
    • Rover, L.1    Fernandes, J.C.B.2    Neto, G.D.O.3    Kubota, L.T.4    Katekawa, E.5    Serrano, S.L.H.P.6
  • 36
    • 59449108061 scopus 로고    scopus 로고
    • Engineering cytochrome p450 enzymes for improved activity towards biomimetic 1,4-NADH-cofactors
    • Ryan, J. D., Fish, R. H., and Clark, D. S. (2008). Engineering cytochrome p450 enzymes for improved activity towards biomimetic 1,4-NADH-cofactors. ChemBioChem 9, 2579-2582. doi: 10.1002/cbic.200800246
    • (2008) ChemBioChem , vol.9 , pp. 2579-2582
    • Ryan, J.D.1    Fish, R.H.2    Clark, D.S.3
  • 37
    • 0022558921 scopus 로고
    • Isolation and properties of an H2O-forming NADH oxidase from Streptococcus faecalis
    • Schmidt, H.-L., Stöcklein, W., Danzer, J., Kirch, P., and Limbach, B. (1986). Isolation and properties of an H2O-forming NADH oxidase from Streptococcus faecalis. Eur. J. Biochem. 156, 149-155. doi: 10.1111/j.1432-1033.1986.tb09560.x
    • (1986) Eur. J. Biochem , vol.156 , pp. 149-155
    • Schmidt, H.-L.1    Stöcklein, W.2    Danzer, J.3    Kirch, P.4    Limbach, B.5
  • 38
    • 14844294424 scopus 로고    scopus 로고
    • Protein production by auto-induction in high-density shaking cultures
    • Studier, F. W. (2005). Protein production by auto-induction in high-density shaking cultures. Protein Exp. Purif. 41, 207-234. doi: 10.1016/j.pep.2005.01.016
    • (2005) Protein Exp. Purif , vol.41 , pp. 207-234
    • Studier, F.W.1
  • 39
    • 9144264649 scopus 로고
    • Steric and electronic effects of methyl substituents at 2-and 6-positions on N-Benzyl-1,4-dihydronicotinamide
    • Takeda, J., Ohta, S., and Hirobe, M. (1987). Steric and electronic effects of methyl substituents at 2-and 6-positions on N-Benzyl-1,4-dihydronicotinamide. Chem. Pharm. Bull 35, 2661-2667. doi: 10.1248/cpb.35.2661
    • (1987) Chem. Pharm. Bull , vol.35 , pp. 2661-2667
    • Takeda, J.1    Ohta, S.2    Hirobe, M.3
  • 40
    • 79954522978 scopus 로고    scopus 로고
    • A highly efficient ADH-coupled NADH-recycling system for the asymmetric bioreduction of carbon-carbon double bonds using enoate reductases
    • Tauber, K., Hall, M., Kroutil, W., Fabian, W. M. F., Faber, K., and Glueck, S. M. (2011). A highly efficient ADH-coupled NADH-recycling system for the asymmetric bioreduction of carbon-carbon double bonds using enoate reductases. Biotechnol. Bioeng. 108, 1462-1467. doi: 10.1002/bit.23078
    • (2011) Biotechnol. Bioeng , vol.108 , pp. 1462-1467
    • Tauber, K.1    Hall, M.2    Kroutil, W.3    Fabian, W.M.F.4    Faber, K.5    Glueck, S.M.6
  • 41
    • 41949130006 scopus 로고    scopus 로고
    • Flexibility and enzyme activity of NADH oxidase from Thermus thermophilus in the presence of monovalent cations of Hofmeister series
    • Tóth, K., Sedlak, E., Sprinzl, M., and Zoldak, G. (2008). Flexibility and enzyme activity of NADH oxidase from Thermus thermophilus in the presence of monovalent cations of Hofmeister series. Biochim. Biophys. Acta 1784, 789-795. doi: 10.1016/j.bbapap.2008.01.022
    • (2008) Biochim. Biophys. Acta , vol.1784 , pp. 789-795
    • Tóth, K.1    Sedlak, E.2    Sprinzl, M.3    Zoldak, G.4
  • 42
    • 77954251837 scopus 로고    scopus 로고
    • 'Regeneration of nicotinamide coenzymes: principles and applications for the synthesis of chiral compounds,'
    • eds C. Wittmann and R. Krull (Berlin: Springer)
    • Weckbecker, A., Gröger, H., and Hummel, W. (2010). "Regeneration of nicotinamide coenzymes: principles and applications for the synthesis of chiral compounds," in Biosystems Engineering I, eds C. Wittmann and R. Krull (Berlin: Springer), 195-242.
    • (2010) Biosystems Engineering I , pp. 195-242
    • Weckbecker, A.1    Gröger, H.2    Hummel, W.3
  • 43
    • 79952439080 scopus 로고    scopus 로고
    • A fluorometric assay for high-throughput screening targeting nicotinamide phosphoribosyltransferase
    • Zhang, R.-Y., Qin, Y., Lv, X.-Q., Wang, P., Xu, T.-Y., Zhang, L., et al. (2011). A fluorometric assay for high-throughput screening targeting nicotinamide phosphoribosyltransferase. Anal. Biochem. 412, 18-25. doi: 10.1016/j.ab.2010.12.035
    • (2011) Anal. Biochem , vol.412 , pp. 18-25
    • Zhang, R.-Y.1    Qin, Y.2    Lv, X.-Q.3    Wang, P.4    Xu, T.-Y.5    Zhang, L.6
  • 44
    • 84862830721 scopus 로고    scopus 로고
    • Cloning and characterization of a thermostable H2O-forming NADH oxidase from Lactobacillus rhamnosus
    • Zhang, Y.-W., Tiwari, M. K., Gao, H., Dhiman, S. S., Jeya, M., and Lee, J.-K. (2012). Cloning and characterization of a thermostable H2O-forming NADH oxidase from Lactobacillus rhamnosus. Enzyme Microb. Technol. 50, 255-262. doi: 10.1016/j.enzmictec.2012.01.009
    • (2012) Enzyme Microb. Technol , vol.50 , pp. 255-262
    • Zhang, Y.-W.1    Tiwari, M.K.2    Gao, H.3    Dhiman, S.S.4    Jeya, M.5    Lee, J.-K.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.