메뉴 건너뛰기




Volumn 3, Issue 6, 2014, Pages 380-386

Annexation of a high-activity enzyme in a synthetic three-enzyme complex greatly decreases the degree of substrate channeling

Author keywords

cell free synthetic biology; enzyme cascade; metabolon; rate limiting step; substrate channeling; synthetic enzyme complex

Indexed keywords

FRUCTOSE BISPHOSPHATASE; FRUCTOSE BISPHOSPHATE ALDOLASE; MULTIENZYME COMPLEX; TRIOSEPHOSPHATE ISOMERASE; BACTERIAL DNA; CELL CYCLE PROTEIN; COHESIN; NONHISTONE PROTEIN; RECOMBINANT PROTEIN; SYNTHETIC DNA;

EID: 84903161298     PISSN: None     EISSN: 21615063     Source Type: Journal    
DOI: 10.1021/sb4000993     Document Type: Article
Times cited : (45)

References (41)
  • 2
    • 33745454125 scopus 로고    scopus 로고
    • Synthetic biology: New engineering rules for an emerging discipline
    • Andrianantoandro, E., Basu, S., Karig, D. K., and Weiss, R. (2006) Synthetic biology: New engineering rules for an emerging discipline Mol. Syst. Biol. 2, 28
    • (2006) Mol. Syst. Biol. , vol.2 , pp. 28
    • Andrianantoandro, E.1    Basu, S.2    Karig, D.K.3    Weiss, R.4
  • 3
    • 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
    • (2013) Green Chem. , vol.15 , pp. 1708-1719
    • Rollin, J.A.1    Tam, T.K.2    Zhang, Y.-H.P.3
  • 4
    • 84876904385 scopus 로고    scopus 로고
    • Cell-free biosystems for biomanufacturing
    • (Zhong, J.-J. Ed.), Springer, Berlin Heidelberg
    • You, C. and Zhang, Y. H. P. (2013) Cell-free biosystems for biomanufacturing. In Adv. Biochem. Eng. Biotechnol. (Zhong, J.-J., Ed.), pp 89-119, Springer, Berlin Heidelberg.
    • (2013) Adv. Biochem. Eng. Biotechnol. , pp. 89-119
    • You, C.1    Zhang, Y.H.P.2
  • 5
    • 83255164998 scopus 로고    scopus 로고
    • Cell-free synthetic biology: Thinking outside the cell
    • Eric Hodgman, C. and Jewett, M. C. (2012) Cell-free synthetic biology: Thinking outside the cell Metab. Eng. 14, 261-269
    • (2012) Metab. Eng. , vol.14 , pp. 261-269
    • Eric Hodgman, C.1    Jewett, M.C.2
  • 7
    • 84867226844 scopus 로고    scopus 로고
    • Cell-free biology: Exploiting the interface between synthetic biology and synthetic chemistry
    • Harris, D. C. and Jewett, M. C. (2012) Cell-free biology: Exploiting the interface between synthetic biology and synthetic chemistry Curr. Opin. Biotechnol. 23, 672-678
    • (2012) Curr. Opin. Biotechnol. , vol.23 , pp. 672-678
    • Harris, D.C.1    Jewett, M.C.2
  • 9
    • 84856764807 scopus 로고    scopus 로고
    • Multi-enzyme systems: Bringing enzymes together in vitro
    • Schoffelen, S. and van Hest, J. C. M. (2012) Multi-enzyme systems: Bringing enzymes together in vitro Soft Matter 8, 1736-1746
    • (2012) Soft Matter , vol.8 , pp. 1736-1746
    • Schoffelen, S.1    Van Hest, J.C.M.2
  • 10
    • 79960216783 scopus 로고    scopus 로고
    • Substrate channeling and enzyme complexes for biotechnological applications
    • Zhang, Y. H. P. (2011) Substrate channeling and enzyme complexes for biotechnological applications Biotechnol. Adv. 29, 715-725
    • (2011) Biotechnol. Adv. , vol.29 , pp. 715-725
    • Zhang, Y.H.P.1
  • 12
    • 84859128218 scopus 로고    scopus 로고
    • Interenzyme substrate diffusion for an enzyme cascade organized on spatially addressable DNA nanostructures
    • Fu, J., Liu, M., Liu, Y., Woodbury, N. W., and Yan, H. (2012) Interenzyme substrate diffusion for an enzyme cascade organized on spatially addressable DNA nanostructures J. Am. Chem. Soc. 134, 5516-5519
    • (2012) J. Am. Chem. Soc. , vol.134 , pp. 5516-5519
    • Fu, J.1    Liu, M.2    Liu, Y.3    Woodbury, N.W.4    Yan, H.5
  • 13
    • 80053495138 scopus 로고    scopus 로고
    • DNA-mediated assembly of cytochrome P450 BM3 subdomains
    • Erkelenz, M., Kuo, C.-H., and Niemeyer, C. M. (2011) DNA-mediated assembly of cytochrome P450 BM3 subdomains J. Am. Chem. Soc. 133, 16111-16118
    • (2011) J. Am. Chem. Soc. , vol.133 , pp. 16111-16118
    • Erkelenz, M.1    Kuo, C.-H.2    Niemeyer, C.M.3
  • 14
    • 54849426838 scopus 로고    scopus 로고
    • DNA-directed assembly of artificial multienzyme complexes
    • Müller, J. and Niemeyer, C. M. (2008) DNA-directed assembly of artificial multienzyme complexes Biochem. Biophys. Res. Commun. 377, 62-67
    • (2008) Biochem. Biophys. Res. Commun. , vol.377 , pp. 62-67
    • Müller, J.1    Niemeyer, C.M.2
  • 16
    • 79960697001 scopus 로고    scopus 로고
    • Organization of intracellular reactions with rationally designed RNA assemblies
    • Delebecque, C. J., Lindner, A. B., Silver, P. A., and Aldaye, F. A. (2011) Organization of intracellular reactions with rationally designed RNA assemblies Science 333, 470-474
    • (2011) Science , vol.333 , pp. 470-474
    • Delebecque, C.J.1    Lindner, A.B.2    Silver, P.A.3    Aldaye, F.A.4
  • 17
    • 84874095104 scopus 로고    scopus 로고
    • Self-assembly of synthetic metabolons through synthetic protein scaffolds: One-step purification, co-immobilization, and substrate channeling
    • You, C. and Zhang, Y. H. P. (2013) Self-assembly of synthetic metabolons through synthetic protein scaffolds: One-step purification, co-immobilization, and substrate channeling ACS Synth. Biol. 2, 102-110
    • (2013) ACS Synth. Biol. , vol.2 , pp. 102-110
    • You, C.1    Zhang, Y.H.P.2
  • 19
    • 77955168936 scopus 로고    scopus 로고
    • Molecular assembly of P450 with ferredoxin and ferredoxin reductase by fusion to PCNA
    • Hirakawa, H. and Nagamune, T. (2010) Molecular assembly of P450 with ferredoxin and ferredoxin reductase by fusion to PCNA ChemBioChem 11, 1517-1520
    • (2010) ChemBioChem , vol.11 , pp. 1517-1520
    • Hirakawa, H.1    Nagamune, T.2
  • 20
    • 84979849095 scopus 로고    scopus 로고
    • Compartmentalization and metabolic channeling for multienzymatic biosynthesis: Practical strategies and modeling approaches
    • DOI: 10.1007/10-2013-221.
    • Jandt, U., You, C., Zhang, Y.-H. P., and Zeng, A. (2013) Compartmentalization and metabolic channeling for multienzymatic biosynthesis: Practical strategies and modeling approaches. In Adv. Biochem. Eng. Biotechnol. DOI: 10.1007/10-2013-221.
    • (2013) Adv. Biochem. Eng. Biotechnol.
    • Jandt, U.1    You, C.2    Zhang, Y.-H.P.3    Zeng, A.4
  • 21
    • 84869875863 scopus 로고    scopus 로고
    • Designing biological compartmentalization
    • Chen, A. H. and Silver, P. A. (2012) Designing biological compartmentalization Trends Cell Biol. 22, 662-670
    • (2012) Trends Cell Biol. , vol.22 , pp. 662-670
    • Chen, A.H.1    Silver, P.A.2
  • 22
    • 84880122011 scopus 로고    scopus 로고
    • Enzyme immobilisation in biocatalysis: Why, what, and how
    • Sheldon, R. A. and van Pelt, S. (2013) Enzyme immobilisation in biocatalysis: Why, what, and how Chem. Soc. Rev. 42, 6223-6235
    • (2013) Chem. Soc. Rev. , vol.42 , pp. 6223-6235
    • Sheldon, R.A.1    Van Pelt, S.2
  • 23
    • 13044268636 scopus 로고
    • Preparation of a soluble bifunctional enzyme by gene fusion
    • Bulow, L., Ljungcrantz, P., and Mosbach, K. (1985) Preparation of a soluble bifunctional enzyme by gene fusion Nat. Biotechnol. 3, 821-823
    • (1985) Nat. Biotechnol. , vol.3 , pp. 821-823
    • Bulow, L.1    Ljungcrantz, P.2    Mosbach, K.3
  • 25
    • 84865404296 scopus 로고    scopus 로고
    • Facilitated substrate channeling in a self-assembled trifunctional enzyme complex
    • You, C., Myung, S., and Zhang, Y. H. P. (2012) Facilitated substrate channeling in a self-assembled trifunctional enzyme complex Angew. Chem., Int. Ed. 51, 8787-8790
    • (2012) Angew. Chem., Int. Ed. , vol.51 , pp. 8787-8790
    • You, C.1    Myung, S.2    Zhang, Y.H.P.3
  • 27
    • 84876019828 scopus 로고    scopus 로고
    • Non-complexed four cascade enzyme mixture: Simple purification and synergetic co-stabilization
    • Myung, S. and Zhang, Y. H. P. (2013) Non-complexed four cascade enzyme mixture: Simple purification and synergetic co-stabilization PLoS One 8, e61500
    • (2013) PLoS One , vol.8 , pp. 61500
    • Myung, S.1    Zhang, Y.H.P.2
  • 28
    • 84879386272 scopus 로고    scopus 로고
    • Construction of a multifunctional enzyme complex via the strain-promoted azide-alkyne cycloaddition
    • Schoffelen, S., Beekwilder, J., Debets, M. F., Bosch, D., and Hest, J. C. M. v. (2013) Construction of a multifunctional enzyme complex via the strain-promoted azide-alkyne cycloaddition Bioconjugate Chem. 24, 987-996
    • (2013) Bioconjugate Chem. , vol.24 , pp. 987-996
    • Schoffelen, S.1    Beekwilder, J.2    Debets, M.F.3    Bosch, D.4    Hest, J.C.M.5
  • 29
    • 55849139751 scopus 로고    scopus 로고
    • High-yield hydrogen production from starch and water by a synthetic enzymatic pathway
    • Zhang, Y.-H. P., Evans, B. R., Mielenz, J. R., Hopkins, R. C., and Adams, M. W. W. (2007) High-yield hydrogen production from starch and water by a synthetic enzymatic pathway PLoS One 2, e456
    • (2007) PLoS One , vol.2 , pp. 456
    • Zhang, Y.-H.P.1    Evans, B.R.2    Mielenz, J.R.3    Hopkins, R.C.4    Adams, M.W.W.5
  • 31
    • 61349097193 scopus 로고    scopus 로고
    • Spontaneous high-yield production of hydrogen from cellulosic materials and water catalyzed by enzyme cocktails
    • Ye, X., Wang, Y., Hopkins, R. C., Adams, M. W. W., Evans, B. R., Mielenz, J. R., and Zhang, Y.-H. P. (2009) Spontaneous high-yield production of hydrogen from cellulosic materials and water catalyzed by enzyme cocktails ChemSusChem 2, 149-152
    • (2009) ChemSusChem , vol.2 , pp. 149-152
    • Ye, X.1    Wang, Y.2    Hopkins, R.C.3    Adams, M.W.W.4    Evans, B.R.5    Mielenz, J.R.6    Zhang, Y.-H.P.7
  • 32
    • 0035717165 scopus 로고    scopus 로고
    • Molecular cloning, expression, purification, and characterization of fructose-1,6-bisphosphate aldolase from Thermus aquaticus
    • DOI 10.1006/prep.2000.1380
    • Sauvé, V. and Sygusch, J. (2001) Molecular cloning, expression, purification, and characterization of fructose-1,6-bisphosphate aldolase from Thermus aquaticus Protein Expression Purif. 21, 293-302 (Pubitemid 34166075)
    • (2001) Protein Expression and Purification , vol.21 , Issue.2 , pp. 293-302
    • Sauve, V.1    Sygusch, J.2
  • 33
    • 78049440008 scopus 로고    scopus 로고
    • Characterization of a dockerin-based affinity tag: Application for purification of a broad variety of target proteins
    • Demishtein, A., Karpol, A., Barak, Y., Lamed, R., and Bayer, E. A. (2010) Characterization of a dockerin-based affinity tag: Application for purification of a broad variety of target proteins J. Mol. Recognit. 23, 525-535
    • (2010) J. Mol. Recognit. , vol.23 , pp. 525-535
    • Demishtein, A.1    Karpol, A.2    Barak, Y.3    Lamed, R.4    Bayer, E.A.5
  • 34
    • 33644633124 scopus 로고    scopus 로고
    • A Transition from Cellulose Swelling to Cellulose Dissolution by o -Phosphoric Acid: Evidence from Enzymatic Hydrolysis and Supramolecular Structure
    • Zhang, Y. H. P., Cui, J., Lynd, L. R., and Kuang, L. R. (2006) A Transition from Cellulose Swelling to Cellulose Dissolution by o -Phosphoric Acid: Evidence from Enzymatic Hydrolysis and Supramolecular Structure Biomacromolecules 7, 644-648
    • (2006) Biomacromolecules , vol.7 , pp. 644-648
    • Zhang, Y.H.P.1    Cui, J.2    Lynd, L.R.3    Kuang, L.R.4
  • 35
    • 37349114555 scopus 로고    scopus 로고
    • Quantitative determination of cellulose accessibility to cellulase based on adsorption of a nonhydrolytic fusion protein containing CBM and GFP with its applications
    • DOI 10.1021/la7025686
    • Hong, J., Ye, X., and Zhang, Y.-H. P. (2007) Quantitative determination of cellulose accessibility to cellulase based on adsorption of a nonhydrolytic fusion protein containing CBM and GFP with its applications Langmuir 23, 12535-12540 (Pubitemid 350284536)
    • (2007) Langmuir , vol.23 , Issue.25 , pp. 12535-12540
    • Hong, J.1    Ye, X.2    Zhang, Y.-H.P.3
  • 36
    • 40449093567 scopus 로고    scopus 로고
    • Functional asymmetry in cohesin binding belies inherent symmetry of the dockerin module: Insight into cellulosome assembly revealed by systematic mutagenesis
    • DOI 10.1042/BJ20071193
    • Karpol, A., Barak, Y., Lamed, R., Shoham, Y., and Bayer, E. A. (2008) Functional asymmetry in cohesin binding belies inherent symmetry of the dockerin module: Insight into cellulosome assembly revealed by systematic mutagenesis Biochem. J. 410, 331-338 (Pubitemid 351346191)
    • (2008) Biochemical Journal , vol.410 , Issue.2 , pp. 331-338
    • Karpol, A.1    Barak, Y.2    Lamed, R.3    Shoham, Y.4    Bayer, E.A.5
  • 37
    • 33644633124 scopus 로고    scopus 로고
    • A transition from cellulose swelling to cellulose dissolution by o-phosphoric acid: Evidence from enzymatic hydrolysis and supramolecular structure
    • Zhang, Y.-H. P., Cui, J., Lynd, L. R., and Kuang, L. R. (2006) A transition from cellulose swelling to cellulose dissolution by o-phosphoric acid: Evidence from enzymatic hydrolysis and supramolecular structure Biomacromolecules 7, 644-648
    • (2006) Biomacromolecules , vol.7 , pp. 644-648
    • Zhang, Y.-H.P.1    Cui, J.2    Lynd, L.R.3    Kuang, L.R.4
  • 38
    • 84863115482 scopus 로고    scopus 로고
    • Simple cloning via direct transformation of PCR product (DNA multimer) to Escherichia coli and Bacillus subtilis
    • You, C., Zhang, X.-Z., and Zhang, Y.-H. P. (2012) Simple cloning via direct transformation of PCR product (DNA multimer) to Escherichia coli and Bacillus subtilis Appl. Environ. Microbiol. 78, 1593-1595
    • (2012) Appl. Environ. Microbiol. , vol.78 , pp. 1593-1595
    • You, C.1    Zhang, X.-Z.2    Zhang, Y.-H.P.3
  • 39
    • 79951647068 scopus 로고    scopus 로고
    • Biohydrogenation from biomass sugar mediated by in vitro synthetic enzymatic pathways
    • Wang, Y., Huang, W., Sathitsuksanoh, N., Zhu, Z., and Zhang, Y.-H. P. (2011) Biohydrogenation from biomass sugar mediated by in vitro synthetic enzymatic pathways Chem. Biol. 18, 372-380
    • (2011) Chem. Biol. , vol.18 , pp. 372-380
    • Wang, Y.1    Huang, W.2    Sathitsuksanoh, N.3    Zhu, Z.4    Zhang, Y.-H.P.5
  • 40
    • 78149491924 scopus 로고    scopus 로고
    • Fructose-1,6-bisphosphatase from a hyper-thermophilic bacterium Thermotoga maritima: Characterization, metabolite stability, and its implications
    • Myung, S., Wang, Y. R., and Zhang, Y.-H. P. (2010) Fructose-1,6- bisphosphatase from a hyper-thermophilic bacterium Thermotoga maritima: Characterization, metabolite stability, and its implications Proc. Biochem. 45, 1882-1887
    • (2010) Proc. Biochem. , vol.45 , pp. 1882-1887
    • Myung, S.1    Wang, Y.R.2    Zhang, Y.-H.P.3
  • 41
    • 79951645821 scopus 로고    scopus 로고
    • Ultra-stable phosphoglucose isomerase through immobilization of cellulose-binding module-tagged thermophilic enzyme on low-cost high-capacity cellulosic adsorbent
    • Myung, S., Zhang, X.-Z., and Zhang, Y.-H. P. (2011) Ultra-stable phosphoglucose isomerase through immobilization of cellulose-binding module-tagged thermophilic enzyme on low-cost high-capacity cellulosic adsorbent Biotechnol. Prog. 27, 969-975
    • (2011) Biotechnol. Prog. , vol.27 , pp. 969
    • Myung, S.1    Zhang, X.-Z.2    Zhang, Y.-H.P.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.