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Volumn 6, Issue , 2015, Pages

A highly selective biosynthetic pathway to non-natural C 50 carotenoids assembled from moderately selective enzymes

Author keywords

[No Author keywords available]

Indexed keywords

ASTAXANTHIN; CAROTENOID SYNTHASE; ENZYME VARIANT; GERANYLTRANSFERASE; SYNTHETASE; UNCLASSIFIED DRUG; BACTERIAL PROTEIN; CAROTENOID; CRTM PROTEIN, STAPHYLOCOCCUS AUREUS; ESCHERICHIA COLI PROTEIN; SQUALENE SYNTHASE; XANTHOPHYLL;

EID: 84937045641     PISSN: None     EISSN: 20411723     Source Type: Journal    
DOI: 10.1038/ncomms8534     Document Type: Article
Times cited : (58)

References (49)
  • 4
    • 62649122977 scopus 로고    scopus 로고
    • Synthetic metabolism: Engineering biology at the protein and pathway scales
    • Martin, C. H., Nielsen, D. R., Solomon, K. V., Prather, K. L. Synthetic metabolism: engineering biology at the protein and pathway scales. Chem. Biol. 16, 277-286 (2009).
    • (2009) Chem. Biol. , vol.16 , pp. 277-286
    • Martin, C.H.1    Nielsen, D.R.2    Solomon, K.V.3    Prather, K.L.4
  • 5
    • 79959252381 scopus 로고    scopus 로고
    • Constructing de novo biosynthetic pathways for chemical synthesis inside living cells
    • Weeks, A. M., Chang, M. C. Constructing de novo biosynthetic pathways for chemical synthesis inside living cells. Biochemistry 50, 5404-5418 (2011).
    • (2011) Biochemistry , vol.50 , pp. 5404-5418
    • Weeks, A.M.1    Chang, M.C.2
  • 6
    • 84861440312 scopus 로고    scopus 로고
    • Systems metabolic engineering of microorganisms for natural and non-natural chemicals
    • Lee, J. W. et al. Systems metabolic engineering of microorganisms for natural and non-natural chemicals. Nat. Chem. Biol. 8, 536-546 (2012).
    • (2012) Nat. Chem. Biol. , vol.8 , pp. 536-546
    • Lee, J.W.1
  • 7
    • 77950899704 scopus 로고    scopus 로고
    • Expanding metabolism for total biosynthesis of the nonnatural amino acid L-homoalanine
    • Zhang, K., Li, H., Cho, K. M., Liao, J. C. Expanding metabolism for total biosynthesis of the nonnatural amino acid L-homoalanine. Proc. Natl Acad. Sci. USA 107, 6234-6239 (2010).
    • (2010) Proc. Natl Acad. Sci. USA , vol.107 , pp. 6234-6239
    • Zhang, K.1    Li, H.2    Cho, K.M.3    Liao, J.C.4
  • 8
    • 65649123015 scopus 로고    scopus 로고
    • A novel semi-biosynthetic route for artemisinin production using engineered substrate-promiscuous P450(BM3)
    • Dietrich, J. A. et al. A novel semi-biosynthetic route for artemisinin production using engineered substrate-promiscuous P450(BM3). ACS Chem. Biol. 4, 261-267 (2009).
    • (2009) ACS Chem. Biol. , vol.4 , pp. 261-267
    • Dietrich, J.A.1
  • 9
    • 33645975530 scopus 로고    scopus 로고
    • Biosynthesis of novel carotenoid families based on unnatural carbon backbones: A model for diversification of natural product pathways
    • Tobias, A. V., Arnold, F. H. Biosynthesis of novel carotenoid families based on unnatural carbon backbones: a model for diversification of natural product pathways. Biochim. Biophys. Acta Mol. Cell Biol. Lipids 1761, 235-246 (2006).
    • (2006) Biochim. Biophys. Acta Mol. Cell Biol. Lipids , vol.1761 , pp. 235-246
    • Tobias, A.V.1    Arnold, F.H.2
  • 11
    • 84922067763 scopus 로고    scopus 로고
    • A microbial biomanufacturing platform for natural and semisynthetic opioids
    • Thodey, K., Galanie, S., Smolke, C. D. A microbial biomanufacturing platform for natural and semisynthetic opioids. Nat. Chem. Biol. 10, 837-844 (2014).
    • (2014) Nat. Chem. Biol. , vol.10 , pp. 837-844
    • Thodey, K.1    Galanie, S.2    Smolke, C.D.3
  • 12
    • 14844342448 scopus 로고    scopus 로고
    • Diversifying carotenoid biosynthetic pathways by directed evolution
    • Umeno, D., Tobias, A. V., Arnold, F. H. Diversifying carotenoid biosynthetic pathways by directed evolution. Microbiol. Mol. Biol. Rev. 69, 51-78 (2005).
    • (2005) Microbiol. Mol. Biol. Rev. , vol.69 , pp. 51-78
    • Umeno, D.1    Tobias, A.V.2    Arnold, F.H.3
  • 14
    • 53549085133 scopus 로고    scopus 로고
    • Evolutionary history of a specialized p450 propane monooxygenase
    • Fasan, R., Meharenna, Y. T., Snow, C. D., Poulos, T. L., Arnold, F. H. Evolutionary history of a specialized p450 propane monooxygenase. J. Mol. Biol. 383, 1069-1080 (2008).
    • (2008) J. Mol. Biol. , vol.383 , pp. 1069-1080
    • Fasan, R.1    Meharenna, Y.T.2    Snow, C.D.3    Poulos, T.L.4    Arnold, F.H.5
  • 15
    • 65249177164 scopus 로고    scopus 로고
    • Directed enzyme evolution: Climbing fitness peaks one amino acid at a time
    • Tracewell, C. A., Arnold, F. H. Directed enzyme evolution: climbing fitness peaks one amino acid at a time. Curr. Opin. Chem. Biol. 13, 3-9 (2009).
    • (2009) Curr. Opin. Chem. Biol. , vol.13 , pp. 3-9
    • Tracewell, C.A.1    Arnold, F.H.2
  • 16
    • 77953623874 scopus 로고    scopus 로고
    • Enzyme promiscuity: A mechanistic and evolutionary perspective
    • Khersonsky, O., Tawfik, D. S. Enzyme promiscuity: a mechanistic and evolutionary perspective. Annu. Rev. Biochem. 79, 471-505 (2010).
    • (2010) Annu. Rev. Biochem. , vol.79 , pp. 471-505
    • Khersonsky, O.1    Tawfik, D.S.2
  • 17
    • 84871755504 scopus 로고    scopus 로고
    • Diminishing returns and tradeoffs constrain the laboratory optimization of an enzyme
    • Tokuriki, N. et al. Diminishing returns and tradeoffs constrain the laboratory optimization of an enzyme. Nat. Commun. 3, 1257 (2012).
    • (2012) Nat. Commun. , vol.3 , pp. 1257
    • Tokuriki, N.1
  • 18
    • 73949094856 scopus 로고    scopus 로고
    • Metabolic engineering of Escherichia coli for the production of polylactic acid and its copolymers
    • Jung, Y. K., Kim, T. Y., Park, S. J., Lee, S. Y. Metabolic engineering of Escherichia coli for the production of polylactic acid and its copolymers. Biotechnol. Bioeng. 105, 161-171 (2010).
    • (2010) Biotechnol. Bioeng. , vol.105 , pp. 161-171
    • Jung, Y.K.1    Kim, T.Y.2    Park, S.J.3    Lee, S.Y.4
  • 19
    • 84869875863 scopus 로고    scopus 로고
    • Designing biological compartmentalization
    • Chen, A. H., Silver, P. A. Designing biological compartmentalization. Trends Cell Biol. 22, 662-670 (2012).
    • (2012) Trends Cell Biol , vol.22 , pp. 662-670
    • Chen, A.H.1    Silver, P.A.2
  • 20
    • 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
  • 21
    • 0033941389 scopus 로고    scopus 로고
    • Molecular breeding of carotenoid biosynthetic pathways
    • Schmidt-Dannert, C., Umeno, D., Arnold, F. H. Molecular breeding of carotenoid biosynthetic pathways. Nat. Biotechnol. 18, 750-753 (2000).
    • (2000) Nat. Biotechnol. , vol.18 , pp. 750-753
    • Schmidt-Dannert, C.1    Umeno, D.2    Arnold, F.H.3
  • 22
    • 0036901989 scopus 로고    scopus 로고
    • Combinatorial biosynthesis of carotenoids in a heterologous host: A powerful approach for the biosynthesis of novel structures
    • Sandmann, G. Combinatorial biosynthesis of carotenoids in a heterologous host: a powerful approach for the biosynthesis of novel structures. Chembiochem. 3, 629-635 (2002).
    • (2002) Chembiochem , vol.3 , pp. 629-635
    • Sandmann, G.1
  • 23
    • 0036882112 scopus 로고    scopus 로고
    • Evolution of the C30 carotenoid synthase CrtM for function in a C40 pathway
    • Umeno, D., Tobias, A. V., Arnold, F. H. Evolution of the C30 carotenoid synthase CrtM for function in a C40 pathway. J. Bacteriol. 184, 6690-6699 (2002).
    • (2002) J. Bacteriol. , vol.184 , pp. 6690-6699
    • Umeno, D.1    Tobias, A.V.2    Arnold, F.H.3
  • 24
    • 0037562074 scopus 로고    scopus 로고
    • Biosynthesis of structurally novel carotenoids in Escherichia coli
    • Lee, P. C., Momen, A. Z., Mijts, B. N., Schmidt-Dannert, C. Biosynthesis of structurally novel carotenoids in Escherichia coli. Chem. Biol. 10, 453-462 (2003).
    • (2003) Chem. Biol. , vol.10 , pp. 453-462
    • Lee, P.C.1    Momen, A.Z.2    Mijts, B.N.3    Schmidt-Dannert, C.4
  • 25
    • 5644246743 scopus 로고
    • Synthesen von Carotinoiden VI. Synthese eines Homologen des b-Carotins mit 15 konjugierten Doppelbindungen: Decapreno-b-carotin
    • Karrer, P., Eugster, C. H. Synthesen von Carotinoiden VI. Synthese eines Homologen des b-Carotins mit 15 konjugierten Doppelbindungen: Decapreno-b-carotin. Helv. Chim. Acta 34, 28-33 (1951).
    • (1951) Helv. Chim. Acta , vol.34 , pp. 28-33
    • Karrer, P.1    Eugster, C.H.2
  • 26
    • 84957289476 scopus 로고
    • Organization of carotenoid-phospholipid bilayer systems. Incorporation of zeaxanthin, astaxanthin, and their C50 homologues into dimyristoylphosphatidylcholine vesicles
    • Milon, A., Wolff, G., Ourisson, G., Nakatani, Y. Organization of carotenoid-phospholipid bilayer systems. Incorporation of zeaxanthin, astaxanthin, and their C50 homologues into dimyristoylphosphatidylcholine vesicles. Helv. Chim. Acta 69, 12-24 (1986).
    • (1986) Helv. Chim. Acta , vol.69 , pp. 12-24
    • Milon, A.1    Wolff, G.2    Ourisson, G.3    Nakatani, Y.4
  • 28
    • 84874192632 scopus 로고    scopus 로고
    • BCC Research Report #FOD025D
    • The Global Market for Carotenoids, BCC Research Report #FOD025D, http://www.bccresearch.com (2011).
    • (2011) The Global Market for Carotenoids
  • 29
    • 1342304132 scopus 로고    scopus 로고
    • Evolution of a pathway to novel long-chain carotenoids
    • Umeno, D., Arnold, F. H. Evolution of a pathway to novel long-chain carotenoids. J. Bacteriol. 186, 1531-1536 (2004).
    • (2004) J. Bacteriol. , vol.186 , pp. 1531-1536
    • Umeno, D.1    Arnold, F.H.2
  • 30
    • 0028817748 scopus 로고
    • Structure and functional analysis of a marine bacterial carotenoid biosynthesis gene cluster and astaxanthin biosynthetic pathway proposed at the gene level
    • Misawa, N. et al. Structure and functional analysis of a marine bacterial carotenoid biosynthesis gene cluster and astaxanthin biosynthetic pathway proposed at the gene level. J. Bacteriol. 177, 6575-6584 (1995).
    • (1995) J. Bacteriol. , vol.177 , pp. 6575-6584
    • Misawa, N.1
  • 31
    • 0037978128 scopus 로고    scopus 로고
    • A C35 carotenoid biosynthetic pathway
    • Umeno, D., Arnold, F. H. A C35 carotenoid biosynthetic pathway. Appl. Environ. Microbiol. 69, 3573-3579 (2003).
    • (2003) Appl. Environ. Microbiol. , vol.69 , pp. 3573-3579
    • Umeno, D.1    Arnold, F.H.2
  • 32
    • 27644564707 scopus 로고    scopus 로고
    • Characterization of b-carotene ketolases, CrtW, from marine bacteria by complementation analysis in Escherichia coli
    • Choi, S. K. et al. Characterization of b-carotene ketolases, CrtW, from marine bacteria by complementation analysis in Escherichia coli. Mar. Biotechnol. 7, 515-522 (2005).
    • (2005) Mar. Biotechnol. , vol.7 , pp. 515-522
    • Choi, S.K.1
  • 33
    • 33749872408 scopus 로고    scopus 로고
    • Characterization of bacterial b-carotene 3, 3'-hydroxylases, CrtZ, and P450 in astaxanthin biosynthetic pathway and adonirubin production by gene combination in Escherichia coli
    • Choi, S. K., Matsuda, S., Hoshino, T., Peng, X., Misawa, N. Characterization of bacterial b-carotene 3, 3'-hydroxylases, CrtZ, and P450 in astaxanthin biosynthetic pathway and adonirubin production by gene combination in Escherichia coli. Appl. Microbiol. Biotechnol. 72, 1238-1246 (2006).
    • (2006) Appl. Microbiol. Biotechnol. , vol.72 , pp. 1238-1246
    • Choi, S.K.1    Matsuda, S.2    Hoshino, T.3    Peng, X.4    Misawa, N.5
  • 34
    • 0029804201 scopus 로고    scopus 로고
    • A role of the amino acid residue located on the fifth position before the first aspartate-rich motif of farnesyl diphosphate synthase on determination of the final product
    • Ohnuma, S. et al. A role of the amino acid residue located on the fifth position before the first aspartate-rich motif of farnesyl diphosphate synthase on determination of the final product. J. Biol. Chem. 271, 30748-30754 (1996).
    • (1996) J. Biol. Chem. , vol.271 , pp. 30748-30754
    • Ohnuma, S.1
  • 35
    • 0033979844 scopus 로고    scopus 로고
    • Novel prenyltransferase gene encoding farnesylgeranyl diphosphate synthase from a hyperthermophilic archaeon Aeropyrum pernix. Molecularevolution with alteration in product specificity
    • Tachibana, A. et al. Novel prenyltransferase gene encoding farnesylgeranyl diphosphate synthase from a hyperthermophilic archaeon, Aeropyrum pernix. Molecularevolution with alteration in product specificity. Eur. J. Biochem. 267, 321-328 (2000).
    • (2000) Eur. J. Biochem. , vol.267 , pp. 321-328
    • Tachibana, A.1
  • 37
    • 0029807039 scopus 로고    scopus 로고
    • The carotenoid 7, 8-dihydro-c end group can be cyclized by the lycopene cyclases from the bacterium Erwinia uredovora and the higher plant Capsicum annuum
    • Takaichi, S. et al. The carotenoid 7, 8-dihydro-c end group can be cyclized by the lycopene cyclases from the bacterium Erwinia uredovora and the higher plant Capsicum annuum. Eur. J. Biochem. 241, 291-296 (1996).
    • (1996) Eur. J. Biochem. , vol.241 , pp. 291-296
    • Takaichi, S.1
  • 38
    • 11244281311 scopus 로고    scopus 로고
    • The'evolvability'of promiscuous protein functions
    • Aharoni, A. et al. The 'evolvability' of promiscuous protein functions. Nat. Genet. 37, 73-76 (2005).
    • (2005) Nat. Genet. , vol.37 , pp. 73-76
    • Aharoni, A.1
  • 39
    • 40949164743 scopus 로고    scopus 로고
    • Evolving biosynthetic tangos negotiate mechanistic landscapes
    • Austin, M. B., O'Maille, P. E., Noel, J. P. Evolving biosynthetic tangos negotiate mechanistic landscapes. Nat. Chem. Biol. 4, 217-222 (2008).
    • (2008) Nat. Chem. Biol. , vol.4 , pp. 217-222
    • Austin, M.B.1    O'Maille, P.E.2    Noel, J.P.3
  • 40
    • 80052135332 scopus 로고    scopus 로고
    • Regio-and stereoselectivity of P450-catalysed hydroxylation of steroids controlled by laboratory evolution
    • Kille, S., Zilly, F. E., Acevedo, J. P., Reetz, M. T. Regio-and stereoselectivity of P450-catalysed hydroxylation of steroids controlled by laboratory evolution. Nat. Chem. 3, 738-743 (2011).
    • (2011) Nat. Chem. , vol.3 , pp. 738-743
    • Kille, S.1    Zilly, F.E.2    Acevedo, J.P.3    Reetz, M.T.4
  • 41
    • 84865571240 scopus 로고    scopus 로고
    • Network context and selection in the evolution to enzyme specificity
    • Nam, H. et al. Network context and selection in the evolution to enzyme specificity. Science 337, 1101-1104 (2012).
    • (2012) Science , vol.337 , pp. 1101-1104
    • Nam, H.1
  • 42
    • 0042975166 scopus 로고    scopus 로고
    • Natural products-a simple model to explain chemical diversity
    • Firn, R. D., Jones, C. G. Natural products-a simple model to explain chemical diversity. Nat. Prod. Rep. 20, 382-391 (2003).
    • (2003) Nat. Prod. Rep. , vol.20 , pp. 382-391
    • Firn, R.D.1    Jones, C.G.2
  • 43
    • 0015980083 scopus 로고
    • On earlier states of the biochemical system
    • Ycas, M. On earlier states of the biochemical system. J. Theor. Biol. 44, 145-160 (1974).
    • (1974) J. Theor. Biol. , vol.44 , pp. 145-160
    • Ycas, M.1
  • 44
    • 0017272554 scopus 로고
    • Enzyme recruitment in evolution of new function
    • Jensen, R. A. Enzyme recruitment in evolution of new function. Annu. Rev. Microbiol. 30, 409-425 (1976).
    • (1976) Annu. Rev. Microbiol. , vol.30 , pp. 409-425
    • Jensen, R.A.1
  • 46
    • 0026678601 scopus 로고
    • Characterization of carotenoids in photosynthetic bacteria
    • Takaichi, S., Shimada, K. Characterization of carotenoids in photosynthetic bacteria. Methods Enzymol. 213, 374-385 (1992).
    • (1992) Methods Enzymol , vol.213 , pp. 374-385
    • Takaichi, S.1    Shimada, K.2
  • 47
    • 44349133924 scopus 로고    scopus 로고
    • Energy dissipation in the ground-state vibrational manifolds of b-carotene homologues: A sub-20-fs time-resolved transient grating spectro-scopic study
    • Fujiwara, M. et al. Energy dissipation in the ground-state vibrational manifolds of b-carotene homologues: a sub-20-fs time-resolved transient grating spectro-scopic study. Phys. Rev. B 77, 205118 (2008).
    • (2008) Phys. Rev. B , vol.77 , pp. 205118
    • Fujiwara, M.1
  • 48
    • 0026719459 scopus 로고
    • Carotenoid glycoside ester from Rhodococcus rhodochrous
    • Takaichi, S., Ishidsu, J. Carotenoid glycoside ester from Rhodococcus rhodochrous. Methods Enzymol. 213, 366-374 (1992).
    • (1992) Methods Enzymol , vol.213 , pp. 366-374
    • Takaichi, S.1    Ishidsu, J.2
  • 49
    • 0020482354 scopus 로고
    • Efficient enzymatic hydrolysis of polyprenyl pyrophosphates
    • Fujii, H., Koyama, T., Ogura, K. Efficient enzymatic hydrolysis of polyprenyl pyrophosphates. Biochim. Biophys. Acta 712, 716-718 (1982).
    • (1982) Biochim. Biophys. Acta , vol.712 , pp. 716-718
    • Fujii, H.1    Koyama, T.2    Ogura, K.3


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