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Volumn 12, Issue 1, 2010, Pages 8-17

Engineering the Pichia pastoris methanol oxidation pathway for improved NADH regeneration during whole-cell biotransformation

Author keywords

Alcohol oxidase; Cofactor regeneration; Formaldehyde dehydrogenase; Formate dehydrogenase; Methanol pathway; Pathway engineering; Pichia pastoris; Whole cell biocatalysis

Indexed keywords

ALCOHOL OXIDASE; COFACTOR REGENERATION; FORMALDEHYDE DEHYDROGENASE; FORMATE DEHYDROGENASE; PATHWAY ENGINEERING; PICHIA PASTORIS; WHOLE-CELL BIOCATALYSIS;

EID: 70449530436     PISSN: 10967176     EISSN: 10967184     Source Type: Journal    
DOI: 10.1016/j.ymben.2009.08.006     Document Type: Article
Times cited : (65)

References (69)
  • 1
    • 0342417999 scopus 로고
    • Oxidation of methanol by the yeast, Pichia pastoris, purification and properties of the formaldehyde dehydrogenase
    • Allais J.J., Louktibi A., and Baratti J. Oxidation of methanol by the yeast, Pichia pastoris, purification and properties of the formaldehyde dehydrogenase. Agric. Biol. Chem. 47 7 (1983) 1509-1516
    • (1983) Agric. Biol. Chem. , vol.47 , Issue.7 , pp. 1509-1516
    • Allais, J.J.1    Louktibi, A.2    Baratti, J.3
  • 2
    • 0013676374 scopus 로고
    • Oxidation of methanol by the yeast Pichia pastoris: purification and properties of the formate dehydrogenase
    • Allais J.J., Louktibi A., and Baratti J. Oxidation of methanol by the yeast Pichia pastoris: purification and properties of the formate dehydrogenase. Agric. Biol. Chem. 47 11 (1983) 2547-2554
    • (1983) Agric. Biol. Chem. , vol.47 , Issue.11 , pp. 2547-2554
    • Allais, J.J.1    Louktibi, A.2    Baratti, J.3
  • 4
    • 0022348589 scopus 로고
    • Biosynthesis, isolation and properties of NAD-dependent formate dehydrogenase from the yeast Candida methylica
    • Avilova T.V., Egorova O.A., Ioanesyan L.S., and Egorov A.M. Biosynthesis, isolation and properties of NAD-dependent formate dehydrogenase from the yeast Candida methylica. Eur. J. Biochem. 152 (1985) 657-662
    • (1985) Eur. J. Biochem. , vol.152 , pp. 657-662
    • Avilova, T.V.1    Egorova, O.A.2    Ioanesyan, L.S.3    Egorov, A.M.4
  • 5
    • 0032579440 scopus 로고    scopus 로고
    • Designer deletion strains derived from Saccharomyces cerevisiae S288C: a useful set of strains and plasmids for PCR-mediated gene disruption and other applications
    • Baker Brachmann C., Davies A., Cost G.J., Caputo E., Li J., Hieter P., and Boeke J.D. Designer deletion strains derived from Saccharomyces cerevisiae S288C: a useful set of strains and plasmids for PCR-mediated gene disruption and other applications. Yeast 14 (1998) 115-132
    • (1998) Yeast , vol.14 , pp. 115-132
    • Baker Brachmann, C.1    Davies, A.2    Cost, G.J.3    Caputo, E.4    Li, J.5    Hieter, P.6    Boeke, J.D.7
  • 7
    • 48649109598 scopus 로고    scopus 로고
    • Metabolic capacity estimation of Escherichia coli as platform for redox biocatalysis: constraint-based modeling and experimental verification
    • Blank L.M., Ebert B.E., Bühler B., and Schmid A. Metabolic capacity estimation of Escherichia coli as platform for redox biocatalysis: constraint-based modeling and experimental verification. Biotechnol. Bioeng. 100 6 (2008) 1050-1065
    • (2008) Biotechnol. Bioeng. , vol.100 , Issue.6 , pp. 1050-1065
    • Blank, L.M.1    Ebert, B.E.2    Bühler, B.3    Schmid, A.4
  • 8
    • 33745751462 scopus 로고    scopus 로고
    • Analysis of two-liquid-phase multistep biooxidation based on a process model: indications for biological energy shortage
    • Bühler B., Straathof A.J.J., Witholt B., and Schmid A. Analysis of two-liquid-phase multistep biooxidation based on a process model: indications for biological energy shortage. Org. Process Res. Dev. 10 (2006) 628-643
    • (2006) Org. Process Res. Dev. , vol.10 , pp. 628-643
    • Bühler, B.1    Straathof, A.J.J.2    Witholt, B.3    Schmid, A.4
  • 9
    • 40549093298 scopus 로고    scopus 로고
    • NADH Availability limits asymmetric biocatalytic epoxidation in a growing recombinant Escherichia coli strain
    • Bühler B., Park J.-B., Blank L.M., and Schmid A. NADH Availability limits asymmetric biocatalytic epoxidation in a growing recombinant Escherichia coli strain. Appl. Environ. Microbiol. 74 5 (2008) 1436-1446
    • (2008) Appl. Environ. Microbiol. , vol.74 , Issue.5 , pp. 1436-1446
    • Bühler, B.1    Park, J.-B.2    Blank, L.M.3    Schmid, A.4
  • 10
    • 46249123194 scopus 로고    scopus 로고
    • Determination of the cytosolic free NAD/NADH ratio in Saccharomyces cerevisiae under steady-state and highly dynamic conditions
    • Canelas A.B., van Gulik W.M., and Heijnen J.J. Determination of the cytosolic free NAD/NADH ratio in Saccharomyces cerevisiae under steady-state and highly dynamic conditions. Biotechnol. Bioeng. 100 4 (2008) 734-743
    • (2008) Biotechnol. Bioeng. , vol.100 , Issue.4 , pp. 734-743
    • Canelas, A.B.1    van Gulik, W.M.2    Heijnen, J.J.3
  • 11
    • 0033955337 scopus 로고    scopus 로고
    • Heterologous protein expression in the methylotrophic yeast Pichia pastoris
    • Cereghino J.L., and Cregg J.M. Heterologous protein expression in the methylotrophic yeast Pichia pastoris. FEMS Microbiol. Rev. 24 (2000) 45-66
    • (2000) FEMS Microbiol. Rev. , vol.24 , pp. 45-66
    • Cereghino, J.L.1    Cregg, J.M.2
  • 12
    • 84998237581 scopus 로고
    • Oxidation of methanol by the yeast, Pichia pastoris: purification and properties of the alcohol oxidase
    • Couderc R., and Baratti J. Oxidation of methanol by the yeast, Pichia pastoris: purification and properties of the alcohol oxidase. Agric. Biol. Chem. 44 (1980) 2279-2289
    • (1980) Agric. Biol. Chem. , vol.44 , pp. 2279-2289
    • Couderc, R.1    Baratti, J.2
  • 13
    • 0024636430 scopus 로고
    • Functional characterization of the two alcohol oxidase genes from the yeast Pichia pastoris
    • Cregg J.M., Madden K.R., Barringer K.J., Thill G.P., and Stillman C.A. Functional characterization of the two alcohol oxidase genes from the yeast Pichia pastoris. Mol. Cell Biol. 9 (1989) 1316-1323
    • (1989) Mol. Cell Biol. , vol.9 , pp. 1316-1323
    • Cregg, J.M.1    Madden, K.R.2    Barringer, K.J.3    Thill, G.P.4    Stillman, C.A.5
  • 14
    • 0035424201 scopus 로고    scopus 로고
    • Using proteins in their natural environment: potential and limitations of microbial whole-cell hydroxylations in applied biocatalysis
    • Duetz W.A., van Beilen J.B., and Witholt B. Using proteins in their natural environment: potential and limitations of microbial whole-cell hydroxylations in applied biocatalysis. Curr. Opin. Biotechnol. 12 4 (2001) 419-425
    • (2001) Curr. Opin. Biotechnol. , vol.12 , Issue.4 , pp. 419-425
    • Duetz, W.A.1    van Beilen, J.B.2    Witholt, B.3
  • 15
    • 8144220807 scopus 로고    scopus 로고
    • Stereoselective reduction of ethyl 4-chloro acetoacetate with recombinant Pichia pastoris
    • Engelking H., Pfaller R., Wich G., and Weuster-Botz D. Stereoselective reduction of ethyl 4-chloro acetoacetate with recombinant Pichia pastoris. Tetrahedron: Asymmetry 15 22 (2004) 3591-3593
    • (2004) Tetrahedron: Asymmetry , vol.15 , Issue.22 , pp. 3591-3593
    • Engelking, H.1    Pfaller, R.2    Wich, G.3    Weuster-Botz, D.4
  • 17
    • 0015543341 scopus 로고
    • Reactions of nucleic acids and nucleoproteins with formaldehyde
    • Feldman M.Y. Reactions of nucleic acids and nucleoproteins with formaldehyde. Prog. Nucleic Acid Res. Mol. Biol. 13 (1973) 1-49
    • (1973) Prog. Nucleic Acid Res. Mol. Biol. , vol.13 , pp. 1-49
    • Feldman, M.Y.1
  • 18
    • 33749490202 scopus 로고    scopus 로고
    • Physiological and genetic engineering of cytosolic redox metabolism in Saccharomyces cerevisiae for improved glycerol production
    • Geertman J.-M.A., van Maris A.J.A., van Dijken J.P., and Pronk J.T. Physiological and genetic engineering of cytosolic redox metabolism in Saccharomyces cerevisiae for improved glycerol production. Metab. Eng. 8 (2006) 532-542
    • (2006) Metab. Eng. , vol.8 , pp. 532-542
    • Geertman, J.-M.A.1    van Maris, A.J.A.2    van Dijken, J.P.3    Pronk, J.T.4
  • 19
    • 0034537455 scopus 로고    scopus 로고
    • Heterologous protein production in methylotrophic yeasts
    • Gellissen G. Heterologous protein production in methylotrophic yeasts. Appl. Microbiol. Biotechnol. 54 6 (2000) 741-750
    • (2000) Appl. Microbiol. Biotechnol. , vol.54 , Issue.6 , pp. 741-750
    • Gellissen, G.1
  • 20
    • 33846862850 scopus 로고    scopus 로고
    • Pichia pastoris formate dehydrogenase and uses therefore
    • US patent 7,087,418 B2 Bristol-Myers Squibb Company, Princeton, NJ, USA
    • Goldberg, S.L., Cino, P.M., Patel, R.N., Nanduri, V.B., Johnston, R.M., 2006. Pichia pastoris formate dehydrogenase and uses therefore. US patent 7,087,418 B2 (Bristol-Myers Squibb Company, Princeton, NJ, USA).
    • (2006)
    • Goldberg, S.L.1    Cino, P.M.2    Patel, R.N.3    Nanduri, V.B.4    Johnston, R.M.5
  • 21
    • 34547127384 scopus 로고    scopus 로고
    • Biocatalytic ketone reduction - a powerful tool for the production of chiral alcohols - Part I: Processes with isolated enzymes
    • Goldberg K., Schroer K., Lütz S., and Liese A. Biocatalytic ketone reduction - a powerful tool for the production of chiral alcohols - Part I: Processes with isolated enzymes. Appl. Microbiol. Biotechnol 76 2 (2007) 237-248
    • (2007) Appl. Microbiol. Biotechnol , vol.76 , Issue.2 , pp. 237-248
    • Goldberg, K.1    Schroer, K.2    Lütz, S.3    Liese, A.4
  • 22
    • 0034680769 scopus 로고    scopus 로고
    • Characterization of a (2R,3R)-2,3-butanediol dehydrogenase as the Saccharomyces cerevisiae YAL060W gene product
    • González E., Fernández M.R., Larroy C., Solà L., Pericàs M.A., Parés X., and Biosca J.A. Characterization of a (2R,3R)-2,3-butanediol dehydrogenase as the Saccharomyces cerevisiae YAL060W gene product. J. Biol. Chem. 275 (2000) 35876-35885
    • (2000) J. Biol. Chem. , vol.275 , pp. 35876-35885
    • González, E.1    Fernández, M.R.2    Larroy, C.3    Solà, L.4    Pericàs, M.A.5    Parés, X.6    Biosca, J.A.7
  • 23
    • 0020630539 scopus 로고
    • Formaldehyde damage to DNA and inhibition of DNA repair in human bronchial cells
    • Grafstrom R.C., Fornace A.J., Autrup H., Lechner J.F., and Harris C.C. Formaldehyde damage to DNA and inhibition of DNA repair in human bronchial cells. Science 220 (1983) 216-218
    • (1983) Science , vol.220 , pp. 216-218
    • Grafstrom, R.C.1    Fornace, A.J.2    Autrup, H.3    Lechner, J.F.4    Harris, C.C.5
  • 24
    • 33748530708 scopus 로고    scopus 로고
    • Enantioselective reduction of ketones with "Designer Cells" at high substrate concentrations: highly efficient access to functionalized optically active alcohols
    • Gröger H., Chamouleau F., Orologas N., Rollmann C., Drauz K., Hummel W., Weckbecker A., and May O. Enantioselective reduction of ketones with "Designer Cells" at high substrate concentrations: highly efficient access to functionalized optically active alcohols. Angew. Chem. Int. Ed. 45 (2006) 5677-5681
    • (2006) Angew. Chem. Int. Ed. , vol.45 , pp. 5677-5681
    • Gröger, H.1    Chamouleau, F.2    Orologas, N.3    Rollmann, C.4    Drauz, K.5    Hummel, W.6    Weckbecker, A.7    May, O.8
  • 27
    • 33846886702 scopus 로고    scopus 로고
    • Regulation of methanol utilisation pathway genes in yeasts
    • Hartner F.S., and Glieder A. Regulation of methanol utilisation pathway genes in yeasts. Microb. Cell Fact. 5 (2006) 39
    • (2006) Microb. Cell Fact. , vol.5 , pp. 39
    • Hartner, F.S.1    Glieder, A.2
  • 31
    • 63649094973 scopus 로고    scopus 로고
    • 2 and expression of a putative sugar permease from Leuconostoc pseudomesenteroides
    • 2 and expression of a putative sugar permease from Leuconostoc pseudomesenteroides. Metab. Eng. 11 (2009) 178-183
    • (2009) Metab. Eng. , vol.11 , pp. 178-183
    • Heuser, F.1    Marin, K.2    Kaup, B.3    Bringer, S.4    Sahm, H.5
  • 32
    • 0035846723 scopus 로고    scopus 로고
    • Full-scale model of glycolysis in Saccharomyces cerevisiae
    • Hynne F., Dano S., and Sorensen P.G. Full-scale model of glycolysis in Saccharomyces cerevisiae. Biophys. Chem. 94 1-2 (2001) 121-163
    • (2001) Biophys. Chem. , vol.94 , Issue.1-2 , pp. 121-163
    • Hynne, F.1    Dano, S.2    Sorensen, P.G.3
  • 36
    • 70449528841 scopus 로고    scopus 로고
    • Ketoreductases: general stereoselective catalysts for the facile synthesis of a broad range of chiral alcohols
    • Kambourakis S., and Rozzell J.D. Ketoreductases: general stereoselective catalysts for the facile synthesis of a broad range of chiral alcohols. Pharma Chem. 5 9 (2006) 2-5
    • (2006) Pharma Chem. , vol.5 , Issue.9 , pp. 2-5
    • Kambourakis, S.1    Rozzell, J.D.2
  • 37
    • 0019972145 scopus 로고
    • Purification and properties of a transketolase responsible for formaldehyde fixation in a methanol-utilizing yeast, Candida boidinii (Kloeckera sp.) no. 2201
    • Kato N., Higuchi T., Sakazawa C., Nichizawa T., Tani Y., and Yamada H. Purification and properties of a transketolase responsible for formaldehyde fixation in a methanol-utilizing yeast, Candida boidinii (Kloeckera sp.) no. 2201. Biochim. Biophys. Acta 715 2 (1982) 143-150
    • (1982) Biochim. Biophys. Acta , vol.715 , Issue.2 , pp. 143-150
    • Kato, N.1    Higuchi, T.2    Sakazawa, C.3    Nichizawa, T.4    Tani, Y.5    Yamada, H.6
  • 40
    • 0036738121 scopus 로고    scopus 로고
    • Physiological role of the glutathione-dependent formaldehyde dehydrogenase in the methylotrophic yeast Candida boidinii
    • Lee B., Yurimoto H., Sakai Y., and Kato N. Physiological role of the glutathione-dependent formaldehyde dehydrogenase in the methylotrophic yeast Candida boidinii. Microbiology 148 Pt 9 (2002) 2697-2704
    • (2002) Microbiology , vol.148 , Issue.PART 9 , pp. 2697-2704
    • Lee, B.1    Yurimoto, H.2    Sakai, Y.3    Kato, N.4
  • 42
    • 0033955337 scopus 로고    scopus 로고
    • Heterologous protein expression in the methylotrophic yeast Pichia pastoris
    • Lin-Cereghino J., and Cregg J.M. Heterologous protein expression in the methylotrophic yeast Pichia pastoris. FEMS Microbiol. Rev. 24 1 (2000) 45-66
    • (2000) FEMS Microbiol. Rev. , vol.24 , Issue.1 , pp. 45-66
    • Lin-Cereghino, J.1    Cregg, J.M.2
  • 45
    • 49949115796 scopus 로고    scopus 로고
    • Overexpression of the riboflavin biosynthetic pathway in Pichia pastoris
    • Marx H., Mattanovich D., and Sauer M. Overexpression of the riboflavin biosynthetic pathway in Pichia pastoris. Microb. Cell Fact. 7 (2008) 23
    • (2008) Microb. Cell Fact. , vol.7 , pp. 23
    • Marx, H.1    Mattanovich, D.2    Sauer, M.3
  • 48
    • 18844417483 scopus 로고    scopus 로고
    • Beyond oil and gas: the methanol economy
    • Olah G.A. Beyond oil and gas: the methanol economy. Angew. Chem. Int. Ed. Engl. 44 (2005) 2636-2639
    • (2005) Angew. Chem. Int. Ed. Engl. , vol.44 , pp. 2636-2639
    • Olah, G.A.1
  • 49
    • 0019618664 scopus 로고
    • Microbial oxidation of methanol: properties of crystallized alcohol oxidase from a yeast, Pichia sp
    • Patel R.N., Hou C.T., Laskin A.I., and Derelanko P. Microbial oxidation of methanol: properties of crystallized alcohol oxidase from a yeast, Pichia sp. Arch. Biochem. Biophys. 210 (1981) 481-488
    • (1981) Arch. Biochem. Biophys. , vol.210 , pp. 481-488
    • Patel, R.N.1    Hou, C.T.2    Laskin, A.I.3    Derelanko, P.4
  • 50
    • 0021103537 scopus 로고
    • Microbial oxidation of methanol: purification and properties of formaldehyde dehydrogenase from a Pichia sp. NRRL-Y-11328
    • Patel R.N., Hou C.T., and Derelanko P. Microbial oxidation of methanol: purification and properties of formaldehyde dehydrogenase from a Pichia sp. NRRL-Y-11328. Arch. Biochem. Biophys. 221 1 (1983) 135-142
    • (1983) Arch. Biochem. Biophys. , vol.221 , Issue.1 , pp. 135-142
    • Patel, R.N.1    Hou, C.T.2    Derelanko, P.3
  • 51
    • 0030745824 scopus 로고    scopus 로고
    • Engineering Pichia pastoris for biocatalysis: co-production of two active enzymes
    • Payne M.S., Petrillo K.L., Gavagan J.E., DiCosimo R., Wagner L.W., and Anton D.L. Engineering Pichia pastoris for biocatalysis: co-production of two active enzymes. Gene 194 (1997) 179-182
    • (1997) Gene , vol.194 , pp. 179-182
    • Payne, M.S.1    Petrillo, K.L.2    Gavagan, J.E.3    DiCosimo, R.4    Wagner, L.W.5    Anton, D.L.6
  • 52
    • 59049091116 scopus 로고    scopus 로고
    • Yeast cell factories for fine chemical and API production
    • Pscheidt B., and Glieder A. Yeast cell factories for fine chemical and API production. Microb. Cell Fact. 7 (2008) 25
    • (2008) Microb. Cell Fact. , vol.7 , pp. 25
    • Pscheidt, B.1    Glieder, A.2
  • 53
    • 70349338910 scopus 로고    scopus 로고
    • Metabolomics for biotransformations: intracellular redox cofactor analysis and enzyme kinetics offer insight into whole cell processes
    • Schroer K., Zelic B., Oldiges M., and Lütz S. Metabolomics for biotransformations: intracellular redox cofactor analysis and enzyme kinetics offer insight into whole cell processes. Biotechnol. Bioeng 104 2 (2009) 251-260
    • (2009) Biotechnol. Bioeng , vol.104 , Issue.2 , pp. 251-260
    • Schroer, K.1    Zelic, B.2    Oldiges, M.3    Lütz, S.4
  • 54
    • 0141482140 scopus 로고    scopus 로고
    • Enhanced production of α-galactosyl epitopes by metabolically engineered Pichia pastoris
    • Shao J., Hayashi T., and Wang P.G. Enhanced production of α-galactosyl epitopes by metabolically engineered Pichia pastoris. Appl. Environ. Microbiol. 69 9 (2003) 5238-5242
    • (2003) Appl. Environ. Microbiol. , vol.69 , Issue.9 , pp. 5238-5242
    • Shao, J.1    Hayashi, T.2    Wang, P.G.3
  • 55
    • 0032541478 scopus 로고    scopus 로고
    • A strong nitrogen source-regulated promoter for controlled expression of foreign genes in the yeast Pichia pastoris
    • Shen S., Sulter G., Jeffries T.W., and Cregg J.M. A strong nitrogen source-regulated promoter for controlled expression of foreign genes in the yeast Pichia pastoris. Gene 216 (1998) 93-102
    • (1998) Gene , vol.216 , pp. 93-102
    • Shen, S.1    Sulter, G.2    Jeffries, T.W.3    Cregg, J.M.4
  • 57
    • 0018382593 scopus 로고
    • Complete nucleotide sequence of the Escherichia coli plasmid pBR322
    • Sutcliffe J.G. Complete nucleotide sequence of the Escherichia coli plasmid pBR322. Cold Spring Harb. Symp. Quant. Biol. 43 Part 1 (1979) 77-90
    • (1979) Cold Spring Harb. Symp. Quant. Biol. , vol.43 , Issue.PART 1 , pp. 77-90
    • Sutcliffe, J.G.1
  • 59
    • 0343471961 scopus 로고    scopus 로고
    • In vivo analysis of metabolic dynamics in Saccharomyces cerevisiae: I. Experimental observations
    • Theobald U., Mailinger W., Baltes M., Rizzi M., and Reuss M. In vivo analysis of metabolic dynamics in Saccharomyces cerevisiae: I. Experimental observations. Biotechnol. Bioeng. 55 2 (1997) 305-316
    • (1997) Biotechnol. Bioeng. , vol.55 , Issue.2 , pp. 305-316
    • Theobald, U.1    Mailinger, W.2    Baltes, M.3    Rizzi, M.4    Reuss, M.5
  • 60
    • 0042933788 scopus 로고    scopus 로고
    • Recent developments in pyridine nucleotide regeneration
    • Van der Donk W.A., and Zhao H. Recent developments in pyridine nucleotide regeneration. Curr. Opin. Biotechnol. 14 4 (2003) 421-426
    • (2003) Curr. Opin. Biotechnol. , vol.14 , Issue.4 , pp. 421-426
    • Van der Donk, W.A.1    Zhao, H.2
  • 61
    • 33845329876 scopus 로고    scopus 로고
    • The significance of peroxisomes in methanol metabolism in methylotrophic yeast
    • Van der Klei I.J., Yurimoto H., Sakai Y., and Veenhuis M. The significance of peroxisomes in methanol metabolism in methylotrophic yeast. Biochim. Biophys. Acta 1763 12 (2006) 1453-1462
    • (2006) Biochim. Biophys. Acta , vol.1763 , Issue.12 , pp. 1453-1462
    • Van der Klei, I.J.1    Yurimoto, H.2    Sakai, Y.3    Veenhuis, M.4
  • 63
    • 0028676232 scopus 로고
    • New heterologous modules for classical or PCR-based gene disruptions in Saccharomyces cerevisiae
    • Wach A., Brachat A., Pöhlmann R., and Philippsen P. New heterologous modules for classical or PCR-based gene disruptions in Saccharomyces cerevisiae. Yeast 10 13 (1994) 1793-1808
    • (1994) Yeast , vol.10 , Issue.13 , pp. 1793-1808
    • Wach, A.1    Brachat, A.2    Pöhlmann, R.3    Philippsen, P.4
  • 65
    • 5444226007 scopus 로고    scopus 로고
    • Reliable high-throughput screening with Pichia pastoris by limiting yeast cell death phenomena
    • Weis R., Luiten R., Skranc W., Schwab H., Wubbolts M., and Glieder A. Reliable high-throughput screening with Pichia pastoris by limiting yeast cell death phenomena. FEMS Yeast Res. 5 2 (2004) 179-189
    • (2004) FEMS Yeast Res. , vol.5 , Issue.2 , pp. 179-189
    • Weis, R.1    Luiten, R.2    Skranc, W.3    Schwab, H.4    Wubbolts, M.5    Glieder, A.6
  • 67
    • 1842472920 scopus 로고    scopus 로고
    • Alcohol dehydrogenases that catalyse methyl formate synthesis participate in formaldehyde detoxification in the methylotrophic yeast Candida boidinii
    • Yurimoto H., Lee B., Yasuda F., Sakai Y., and Kato N. Alcohol dehydrogenases that catalyse methyl formate synthesis participate in formaldehyde detoxification in the methylotrophic yeast Candida boidinii. Yeast 21 (2004) 341-350
    • (2004) Yeast , vol.21 , pp. 341-350
    • Yurimoto, H.1    Lee, B.2    Yasuda, F.3    Sakai, Y.4    Kato, N.5
  • 68
    • 60849096352 scopus 로고    scopus 로고
    • Introduction of an NADH regeneration system into Klebsiella oxytoca leads to an enhanced oxidative and reductive metabolism of glycerol
    • Zhang Y., Huang Z., Du C., Li Y., and Cao Z. Introduction of an NADH regeneration system into Klebsiella oxytoca leads to an enhanced oxidative and reductive metabolism of glycerol. Metab. Eng. 11 (2009) 101-106
    • (2009) Metab. Eng. , vol.11 , pp. 101-106
    • Zhang, Y.1    Huang, Z.2    Du, C.3    Li, Y.4    Cao, Z.5
  • 69
    • 29244477223 scopus 로고    scopus 로고
    • A recombinant ketoreductase tool-box: assessing the substrate selectivity and stereoselectivity toward the reduction of β-ketoesters
    • Zhu D., Mukherjee C., Rozzell J.D., Kambourakis S., and Hua L. A recombinant ketoreductase tool-box: assessing the substrate selectivity and stereoselectivity toward the reduction of β-ketoesters. Tetrahedron 62 (2006) 901-905
    • (2006) Tetrahedron , vol.62 , pp. 901-905
    • Zhu, D.1    Mukherjee, C.2    Rozzell, J.D.3    Kambourakis, S.4    Hua, L.5


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