메뉴 건너뛰기




Volumn 32, Issue 10, 2014, Pages 1011-1018

Enzyme clustering accelerates processing of intermediates through metabolic channeling

Author keywords

[No Author keywords available]

Indexed keywords

AGGLOMERATION; EFFICIENCY; ESCHERICHIA COLI; MAMMALS; METABOLISM; SIZE SEPARATION;

EID: 84917699113     PISSN: 10870156     EISSN: 15461696     Source Type: Journal    
DOI: 10.1038/nbt.3018     Document Type: Article
Times cited : (325)

References (55)
  • 1
    • 0037133537 scopus 로고    scopus 로고
    • Production and characterization of bifunctional enzymes. Substrate channeling in the aspartate pathway
    • James, C.L. & Viola, R.E. Production and characterization of bifunctional enzymes. Substrate channeling in the aspartate pathway. Biochemistry 41, 3726-3731 (2002).
    • (2002) Biochemistry , vol.41 , pp. 3726-3731
    • James, C.L.1    Viola, R.E.2
  • 2
    • 0025006579 scopus 로고
    • The tryptophan synthase bienzyme complex transfers indole between the alpha and beta sites via a 25-30 ANG long tunnel
    • Dunn, M.F. et al. The tryptophan synthase bienzyme complex transfers indole between the alpha and beta sites via a 25-30 ANG long tunnel. Biochemistry 29, 8598-8607 (1990).
    • (1990) Biochemistry , vol.29 , pp. 8598-8607
    • Dunn, M.F.1
  • 3
    • 0034919604 scopus 로고    scopus 로고
    • Channeling of substrates and intermediates in enzyme-catalyzed reactions
    • Huang, X., Holden, H.M. & Raushel, F.M. Channeling of substrates and intermediates in enzyme-catalyzed reactions. Annu. Rev. Biochem. 70, 149-180 (2001).
    • (2001) Annu. Rev. Biochem. , vol.70 , pp. 149-180
    • Huang, X.1    Holden, H.M.2    Raushel, F.M.3
  • 4
    • 0017411635 scopus 로고
    • On the role of organized multienzyme systems in cellular metabolism: A general synthesis
    • Welch, G.R. On the role of organized multienzyme systems in cellular metabolism: A general synthesis. Prog. Biophys. Mol. Biol. 32, 103-191 (1978).
    • (1978) Prog. Biophys. Mol. Biol. , vol.32 , pp. 103-191
    • Welch, G.R.1
  • 5
    • 84926009882 scopus 로고
    • Direct transfer of metabolites via enzyme-enzyme complexes: Evidence and physiological significance
    • Bernhard, S.A. & Srivastava, D.K. Direct transfer of metabolites via enzyme-enzyme complexes: evidence and physiological significance. NATO ASI Series 127, 143-163 (1987).
    • (1987) NATO ASI Series , vol.127 , pp. 143-163
    • Bernhard, S.A.1    Srivastava, D.K.2
  • 6
    • 0023061429 scopus 로고
    • Complexes of sequential metabolic enzymes
    • Srere, P.A. Complexes of sequential metabolic enzymes. Annu. Rev. Biochem. 56, 89-124 (1987).
    • (1987) Annu. Rev. Biochem. , vol.56 , pp. 89-124
    • Srere, P.A.1
  • 7
    • 77952050895 scopus 로고    scopus 로고
    • Channeling by proximity: The catalytic advantages of active site colocalization using Brownian dynamics
    • Bauler, P., Huber, G., Leyh, T. & McCammon, J.A. Channeling by proximity: the catalytic advantages of active site colocalization using Brownian dynamics. J. Phys. Chem. Lett. 1, 1332-1335 (2010).
    • (2010) J. Phys. Chem. Lett. , vol.1 , pp. 1332-1335
    • Bauler, P.1    Huber, G.2    Leyh, T.3    McCammon, J.A.4
  • 8
    • 68449088806 scopus 로고    scopus 로고
    • Synthetic protein scaffolds provide modular control over metabolic flux
    • Dueber, J.E. et al. Synthetic protein scaffolds provide modular control over metabolic flux. Nat. Biotechnol. 27, 753-759 (2009).
    • (2009) Nat. Biotechnol. , vol.27 , pp. 753-759
    • Dueber, J.E.1
  • 9
    • 84859780045 scopus 로고    scopus 로고
    • Spatial organization of enzymes for metabolic engineering
    • Lee, H., DeLoache, W.C. & Dueber, J.E. Spatial organization of enzymes for metabolic engineering. Metab. Eng. 14, 242-251 (2012).
    • (2012) Metab. Eng. , vol.14 , pp. 242-251
    • Lee, H.1    Deloache, W.C.2    Dueber, J.E.3
  • 11
    • 0016363246 scopus 로고
    • Metabolic compartmentation: Symbiotic, organellar, multienzymic, and microenvironmental
    • Srere, P.A. & Mosbach, K. Metabolic compartmentation: Symbiotic, organellar, multienzymic, and microenvironmental. Annu. Rev. Microbiol. 28, 61-84 (1974).
    • (1974) Annu. Rev. Microbiol. , vol.28 , pp. 61-84
    • Srere, P.A.1    Mosbach, K.2
  • 12
    • 0019315396 scopus 로고
    • Characterization of the enzyme complex involving the folate-requiring enzymes of de novo purine biosynthesis
    • Smith, G.K., Mueller, W.T., Wasserman, G.F., Taylor, W.D. & Benkovic, S.J. Characterization of the enzyme complex involving the folate-requiring enzymes of de novo purine biosynthesis. Biochemistry 19, 4313-4321 (1980).
    • (1980) Biochemistry , vol.19 , pp. 4313-4321
    • Smith, G.K.1    Mueller, W.T.2    Wasserman, G.F.3    Taylor, W.D.4    Benkovic, S.J.5
  • 16
    • 14044251591 scopus 로고    scopus 로고
    • Assembly and regulation of a glycolytic enzyme complex on the human erythrocyte membrane
    • Campanella, M.E., Chu, H. & Low, P.S. Assembly and regulation of a glycolytic enzyme complex on the human erythrocyte membrane. Proc. Natl. Acad. Sci. USA 102, 2402-2407 (2005).
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 2402-2407
    • Campanella, M.E.1    Chu, H.2    Low, P.S.3
  • 17
    • 41749092312 scopus 로고    scopus 로고
    • Reversible compartmentalization of de novo purine biosynthetic complexes in living cells
    • An, S., Kumar, R., Sheets, E.D. & Benkovic, S.J. Reversible compartmentalization of de novo purine biosynthetic complexes in living cells. Science 320, 103-106 (2008).
    • (2008) Science , vol.320 , pp. 103-106
    • An, S.1    Kumar, R.2    Sheets, E.D.3    Benkovic, S.J.4
  • 18
    • 67649875630 scopus 로고    scopus 로고
    • Widespread reorganization of metabolic enzymes into reversible assemblies upon nutrient starvation
    • Narayanaswamy, R. et al. Widespread reorganization of metabolic enzymes into reversible assemblies upon nutrient starvation. Proc. Natl. Acad. Sci. USA 106, 10147-10152 (2009).
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 10147-10152
    • Narayanaswamy, R.1
  • 19
    • 84867817085 scopus 로고    scopus 로고
    • Mapping protein-protein proximity in the purinosome
    • Deng, Y. et al. Mapping protein-protein proximity in the purinosome. J. Biol. Chem. 287, 36201-36207 (2012).
    • (2012) J. Biol. Chem. , vol.287 , pp. 36201-36207
    • Deng, Y.1
  • 20
    • 84873701617 scopus 로고    scopus 로고
    • Hsp70/Hsp90 chaperone machinery is involved in the assembly of the purinosome
    • French, J.B. et al. Hsp70/Hsp90 chaperone machinery is involved in the assembly of the purinosome. Proc. Natl. Acad. Sci. USA 110, 2528-2533 (2013).
    • (2013) Proc. Natl. Acad. Sci. USA , vol.110 , pp. 2528-2533
    • French, J.B.1
  • 21
    • 77955593994 scopus 로고    scopus 로고
    • Microtubule-assisted mechanism for functional metabolic macromolecular complex formation
    • An, S., Deng, Y., Tomsho, J.W., Kyoung, M. & Benkovic, S.J. Microtubule-assisted mechanism for functional metabolic macromolecular complex formation. Proc. Natl. Acad. Sci. USA 107, 12872-12876 (2010).
    • (2010) Proc. Natl. Acad. Sci. USA , vol.107 , pp. 12872-12876
    • An, S.1    Deng, Y.2    Tomsho, J.W.3    Kyoung, M.4    Benkovic, S.J.5
  • 22
    • 84873560858 scopus 로고    scopus 로고
    • Transiently transfected purine biosynthetic enzymes form stress bodies
    • Zhao, A., et al. Transiently transfected purine biosynthetic enzymes form stress bodies. PLoS ONE 8, 2 (2013).
    • (2013) PLoS ONE , vol.8 , pp. 2
    • Zhao, A.1
  • 23
    • 0016844796 scopus 로고
    • Self-assembly of biological macromolecules
    • Perham, R.N. Self-assembly of biological macromolecules. Phyl. Trans. R. Soc. Lon. 272, 123-136 (1975).
    • (1975) Phyl. Trans. R. Soc. Lon. , vol.272 , pp. 123-136
    • Perham, R.N.1
  • 24
    • 2642644904 scopus 로고
    • Multienzyme complexes
    • Reed, L.J. Multienzyme complexes. Acc. Chem. Res. 7, 40-46 (1973).
    • (1973) Acc. Chem. Res. , vol.7 , pp. 40-46
    • Reed, L.J.1
  • 25
    • 31544450286 scopus 로고    scopus 로고
    • Construction of Escherichia coli K-12 in-frame, single-gen knockout mutants: The Keio collection
    • 2006.0008
    • Baba, T. et al. Construction of Escherichia coli K-12 in-frame, single-gen knockout mutants: the Keio collection. Mol. Syst. Biol. 2 2006.0008 (2006).
    • (2006) Mol. Syst. Biol. , vol.2
    • Baba, T.1
  • 26
    • 77952945226 scopus 로고    scopus 로고
    • Bacterial microcompartment organelles: Protein shell structure and evolution
    • Yeates, T.O., Crowley, C.S. & Tanaka, S. Bacterial microcompartment organelles: protein shell structure and evolution. Annu. Rev. Biophys. 39, 185-205 (2010).
    • (2010) Annu. Rev. Biophys. , vol.39 , pp. 185-205
    • Yeates, T.O.1    Crowley, C.S.2    Tanaka, S.3
  • 28
    • 77955102352 scopus 로고    scopus 로고
    • Quantifying E. Coli proteome and transcriptome with single-molecule sensitivity in single cells
    • Taniguchi, Y. et al. Quantifying E. coli proteome and transcriptome with single-molecule sensitivity in single cells. Science 329, 533-538 (2010).
    • (2010) Science , vol.329 , pp. 533-538
    • Taniguchi, Y.1
  • 30
    • 84876522835 scopus 로고    scopus 로고
    • BRENDA in 2013: Integrated reactions, kinetic data, enzyme function data, improved disease classification: New options and contents in BRENDA
    • Schomburg, I. et al. BRENDA in 2013: integrated reactions, kinetic data, enzyme function data, improved disease classification: new options and contents in BRENDA. Nucleic Acids Res. 41, D764-D772 (2013).
    • (2013) Nucleic Acids Res. , vol.41 , pp. D764-D772
    • Schomburg, I.1
  • 31
    • 0345062171 scopus 로고    scopus 로고
    • Molecular crowding and viscosity as determinants of translational diffusion of metabolites in subcellular organelles
    • García-Pérez, A.I. et al. Molecular crowding and viscosity as determinants of translational diffusion of metabolites in subcellular organelles. Arch. Biochem. Biophys. 362, 329-338 (1999).
    • (1999) Arch. Biochem. Biophys. , vol.362 , pp. 329-338
    • García-Pérez, A.I.1
  • 32
    • 77950863739 scopus 로고    scopus 로고
    • Use of modular, synthetic scaffolds for improved production of glucaric acid in engineered E. Coli
    • Moon, T.S., Dueber, J.E., Shiue, E. & Prather, K.L. Use of modular, synthetic scaffolds for improved production of glucaric acid in engineered E. coli. Metab. Eng. 12, 298-305 (2010).
    • (2010) Metab. Eng. , vol.12 , pp. 298-305
    • Moon, T.S.1    Dueber, J.E.2    Shiue, E.3    Prather, K.L.4
  • 33
    • 84870027847 scopus 로고    scopus 로고
    • Designing and using RNA scaffolds to assemble proteins in vivo
    • Delebecque, C.J., Silver, P.A. & Lindner, A.B. Designing and using RNA scaffolds to assemble proteins in vivo. Nat. Protoc. 7, 1797-1807 (2012).
    • (2012) Nat. Protoc. , vol.7 , pp. 1797-1807
    • Delebecque, C.J.1    Silver, P.A.2    Lindner, A.B.3
  • 34
    • 67649976463 scopus 로고    scopus 로고
    • Granules are liquid droplets that localize by controlled dissolution/condensation
    • Brangwynne, C. et al. Granules are liquid droplets that localize by controlled dissolution/condensation. Science 324, 1729-1732 (2009).
    • (2009) Science , vol.324 , pp. 1729-1732
    • Brangwynne, C.1
  • 35
    • 0026505954 scopus 로고
    • Mutational analysis of carbamyl phosphate synthetase. Substitution of Glu84 1 leads to loss of functional coupling between the two catalytic domains of the synthetase subunit
    • Guillou, F., Liao, M., Garcia-Espana, A. & Lusty, C.J. Mutational analysis of carbamyl phosphate synthetase. Substitution of Glu84 1 leads to loss of functional coupling between the two catalytic domains of the synthetase subunit. Biochemistry 31, 1656-1664 (1992).
    • (1992) Biochemistry , vol.31 , pp. 1656-1664
    • Guillou, F.1    Liao, M.2    Garcia-Espana, A.3    Lusty, C.J.4
  • 36
    • 0024261193 scopus 로고
    • Site-directed mutagenesis of Escherichia coli ornithine transcarbamoylase: Role of arginine-57 in substrate binding and catalysis
    • Kuo, L.C., Miller, A.W., Lee, S. & Kozuma, C. Site-directed mutagenesis of Escherichia coli ornithine transcarbamoylase: role of arginine-57 in substrate binding and catalysis. Biochemistry 27, 8823-8832 (1988).
    • (1988) Biochemistry , vol.27 , pp. 8823-8832
    • Kuo, L.C.1    Miller, A.W.2    Lee, S.3    Kozuma, C.4
  • 37
    • 0010081536 scopus 로고
    • Production and crystallization of aspartate transcarbamylase
    • Shepherdson, M. & Pardee, A.B. Production and crystallization of aspartate transcarbamylase. J. Biol. Chem. 235, 3233-3237 (1960).
    • (1960) J. Biol. Chem. , vol.235 , pp. 3233-3237
    • Shepherdson, M.1    Pardee, A.B.2
  • 38
    • 0029065955 scopus 로고
    • Gene disruption in Escherichia coli: TcR and KmR cassettes with the option of Flp-catalyzed excision of the antibiotic-resistance determinant
    • Cherepanov, P.P. & Wackernagel, W. Gene disruption in Escherichia coli: TcR and KmR cassettes with the option of Flp-catalyzed excision of the antibiotic-resistance determinant. Gene 158, 9-14 (1995).
    • (1995) Gene , vol.158 , pp. 9-14
    • Cherepanov, P.P.1    Wackernagel, W.2
  • 39
    • 0034612342 scopus 로고    scopus 로고
    • One-step inactivation of chromasomal genes in Escherichia coli K-12 using PCR products
    • Datsenko, K.A. & Wanner, B.L. One-step inactivation of chromasomal genes in Escherichia coli K-12 using PCR products. Proc. Natl. Acad. Sci. 97, 6640-6645 (2000).
    • (2000) Proc. Natl. Acad. Sci. , vol.97 , pp. 6640-6645
    • Datsenko, K.A.1    Wanner, B.L.2
  • 40
    • 67349270900 scopus 로고    scopus 로고
    • Enzymatic assembly of DNA molecules up to several hundred kilobases
    • Gibson, D.G. et al. Enzymatic assembly of DNA molecules up to several hundred kilobases. Nat. Methods 6, 343-345 (2009).
    • (2009) Nat. Methods , vol.6 , pp. 343-345
    • Gibson, D.G.1
  • 41
    • 0014589126 scopus 로고
    • Compounds which serve as the sole source of carbon or nitrogen for Salmonella typhimurium LT-2
    • Gutnick, D., Calvo, J.M., Klopotowski, T. & Ames, B.N. Compounds which serve as the sole source of carbon or nitrogen for Salmonella typhimurium LT-2. J. Bacteriol. 100, 215-219 (1969).
    • (1969) J. Bacteriol. , vol.100 , pp. 215-219
    • Gutnick, D.1    Calvo, J.M.2    Klopotowski, T.3    Ames, B.N.4
  • 43
    • 80052069079 scopus 로고    scopus 로고
    • Proteomic characterization of pseudorabies virus extracellular virions
    • Kramer, T., Greco, T.M., Enquist, L.W. & Cristea, I.M. Proteomic characterization of pseudorabies virus extracellular virions. J. Virol. 85, 6427-6441 (2011).
    • (2011) J. Virol. , vol.85 , pp. 6427-6441
    • Kramer, T.1    Greco, T.M.2    Enquist, L.W.3    Cristea, I.M.4
  • 44
    • 34548183872 scopus 로고    scopus 로고
    • Protocol for micro-purification, enrichment, pre-fractionation and storage of peptides for proteomics using StageTips
    • Rappsilber, J., Mann, M. & Ishihama, Y. Protocol for micro-purification, enrichment, pre-fractionation and storage of peptides for proteomics using StageTips. Nat. Protoc. 2, 1896-1906 (2007).
    • (2007) Nat. Protoc. , vol.2 , pp. 1896-1906
    • Rappsilber, J.1    Mann, M.2    Ishihama, Y.3
  • 45
    • 84879574177 scopus 로고    scopus 로고
    • The functional interaction landscape of the human histone deacetylase family
    • Joshi, P. et al. The functional interaction landscape of the human histone deacetylase family. Mol. Sys. Biol. 9, 672 (2013).
    • (2013) Mol. Sys. Biol. , vol.9 , pp. 672
    • Joshi, P.1
  • 46
    • 77951072181 scopus 로고    scopus 로고
    • Metabolomic analysis via reversed-phase ion-pairing liquid chromotography coupled to a stand alone orbitrap mass spectrometer
    • Lu, W. et al. Metabolomic analysis via reversed-phase ion-pairing liquid chromotography coupled to a stand alone orbitrap mass spectrometer. Anal. Chem. 82, 3212-3221 (2010).
    • (2010) Anal. Chem. , vol.82 , pp. 3212-3221
    • Lu, W.1
  • 47
    • 0010081536 scopus 로고
    • Product and crystallization of aspartate transcarbamylase
    • Shepherdson, M. & Pardee, A. Product and crystallization of aspartate transcarbamylase. J. Biol. Chem. 235, 3233-3237 (1960).
    • (1960) J. Biol. Chem. , vol.235 , pp. 3233-3237
    • Shepherdson, M.1    Pardee, A.2
  • 48
    • 0014622121 scopus 로고
    • Modified methods for the determination of carbamoyl aspartate
    • Prescott, L.M. & Jones, M.E. Modified methods for the determination of carbamoyl aspartate. Anal. Biochem. 32, 408-419 (1969).
    • (1969) Anal. Biochem. , vol.32 , pp. 408-419
    • Prescott, L.M.1    Jones, M.E.2
  • 49
    • 0001425337 scopus 로고
    • The enzymology of control by feedback inhibition
    • Gerhart, J.C. & Pardee, A.B. The enzymology of control by feedback inhibition. J. Biol. Chem. 237, 891-896 (1962).
    • (1962) J. Biol. Chem. , vol.237 , pp. 891-896
    • Gerhart, J.C.1    Pardee, A.B.2
  • 50
    • 84881475919 scopus 로고    scopus 로고
    • Pyrimidine homeostasis is accomplished by directed overflow metabolism
    • Reaves, M.L., Young, B.D., Hosios, A.M., Xu, Y.-F. & Rabinowitz, J. Pyrimidine homeostasis is accomplished by directed overflow metabolism. Nature 500, 237-241 (2013).
    • (2013) Nature , vol.500 , pp. 237-241
    • Reaves, M.L.1    Young, B.D.2    Hosios, A.M.3    Xu, Y.-F.4    Rabinowitz, J.5
  • 52
    • 26844569776 scopus 로고    scopus 로고
    • Aggregation as bacterial inclusion bodies does not imply inactivation of enzymes and fluorescent proteins
    • García-Fruitós, E. et al. Aggregation as bacterial inclusion bodies does not imply inactivation of enzymes and fluorescent proteins. Microb. Cell Fact. 4, 27 (2005).
    • (2005) Microb. Cell Fact. , vol.4 , pp. 27
    • García-Fruitós, E.1
  • 53
    • 0345062171 scopus 로고    scopus 로고
    • Molecular crowding and viscosity as determinants of translational diffusion of metabolites in subcellular organelles
    • García-Pérez, A.I. et al. Molecular crowding and viscosity as determinants of translational diffusion of metabolites in subcellular organelles. Arch. Biochem. Biophys. 362, 329-338 (1999).
    • (1999) Arch. Biochem. Biophys. , vol.362 , pp. 329-338
    • García-Pérez, A.I.1
  • 55
    • 77649270954 scopus 로고    scopus 로고
    • Size and shape of protein molecules at the nanometer level determined by sedimentation, gel filtration, and electron microscopy
    • Erickson, H.P. Size and shape of protein molecules at the nanometer level determined by sedimentation, gel filtration, and electron microscopy. Biol. Proced. Online 11, 32-51 (2009).
    • (2009) Biol. Proced. Online , vol.11 , pp. 32-51
    • Erickson, H.P.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.