메뉴 건너뛰기




Volumn 20, Issue 9, 2011, Pages 1597-1606

Computational design and selections for an engineered, thermostable terpene synthase

Author keywords

Phage display; Protein engineering; Terpene synthases; Thermostability

Indexed keywords

SYNTHETASE; TOBACCO 5 EPI ARISTOLOCHENE SYNTHASE; UNCLASSIFIED DRUG;

EID: 84860389087     PISSN: 09618368     EISSN: 1469896X     Source Type: Journal    
DOI: 10.1002/pro.691     Document Type: Article
Times cited : (51)

References (48)
  • 2
    • 0021949079 scopus 로고
    • Monoterpene and sesquiterpene cyclases
    • Croteau R., Cane D.E. (1985) Monoterpene and sesquiterpene cyclases. Methods Enzymol 110:383-405.
    • (1985) Methods Enzymol , vol.110 , pp. 383-405
    • Croteau, R.1    Cane, D.E.2
  • 3
    • 0000558630 scopus 로고
    • Enzymatic formation of sesquiterpenes
    • Cane D.E. (1990) Enzymatic formation of sesquiterpenes. Chem Rev 90:1089-1103.
    • (1990) Chem Rev , vol.90 , pp. 1089-1103
    • Cane, D.E.1
  • 5
    • 0034620687 scopus 로고    scopus 로고
    • Demonstration of germacrene A as an intermediate in 5-Epi-aristolochene synthase catalysis
    • DOI 10.1021/ja993584h
    • Rising K.A., Starks C.M., Noel J.P., Chappell J. (2000) Demonstration of germacrene A as an intermediate in 5-epi-aristolochene synthase catalysis. J Am Chem Soc 122:1861-1866. (Pubitemid 30143886)
    • (2000) Journal of the American Chemical Society , vol.122 , Issue.9 , pp. 1861-1866
    • Rising, K.A.1    Starks, C.M.2    Noel, J.P.3    Chappell, J.4
  • 7
    • 0042432086 scopus 로고    scopus 로고
    • Directed evolution of industrial enzymes: An update
    • DOI 10.1016/S0958-1669(03)00099-5
    • Cherry J.R., Fidantsef A.L. (2003) Directed evolution of industrial enzymes: An update. Curr Opin Biotechnol 14:438-443. (Pubitemid 37011326)
    • (2003) Current Opinion in Biotechnology , vol.14 , Issue.4 , pp. 438-443
    • Cherry, J.R.1    Fidantsef, A.L.2
  • 8
    • 18244373419 scopus 로고    scopus 로고
    • Computational thermostabilization of an enzyme
    • DOI 10.1126/science.1107387
    • Korkegian A., Black M.E., Baker D., Stoddard B.L. (2005) Computational thermostabilization of an enzyme. Science 308:857-860. (Pubitemid 40629266)
    • (2005) Science , vol.308 , Issue.5723 , pp. 857-860
    • Korkegian, A.1    Black, M.E.2    Baker, D.3    Stoddard, B.L.4
  • 9
    • 35349015204 scopus 로고    scopus 로고
    • Selection of Horseradish Peroxidase Variants with Enhanced Enantioselectivity by Yeast Surface Display
    • DOI 10.1016/j.chembiol.2007.09.008, PII S1074552107003262
    • Lipovsek D., Antipov E., Armstrong K.A., Olsen M.J., Klibanov A.M., Tidor B., Wittrup K.D. (2007) Selection of horseradish peroxidase variants with enhanced enantioselectivity by yeast surface display. Chem Biol 14: 1176-1185. (Pubitemid 47599988)
    • (2007) Chemistry and Biology , vol.14 , Issue.10 , pp. 1176-1185
    • Lipovsek, D.1    Antipov, E.2    Armstrong, K.A.3    Olsen, M.J.4    Klibanov, A.M.5    Tidor, B.6    Wittrup, K.D.7
  • 10
    • 0029670577 scopus 로고    scopus 로고
    • Directed evolution of a para-nitrobenzyl esterase for aqueous-organic solvents
    • Moore J.C., Arnold F.H. (1996) Directed evolution of a para-nitrobenzyl esterase for aqueous-organic solvents. Nat Biotechnol 14:458-467.
    • (1996) Nat Biotechnol , vol.14 , pp. 458-467
    • Moore, J.C.1    Arnold, F.H.2
  • 11
    • 3843075198 scopus 로고    scopus 로고
    • Biphenyl dioxygenases: Functional versatilities and directed evolution
    • DOI 10.1128/JB.186.16.5189-5196.2004
    • Furukawa K., Suenaga H., Goto M. (2004) Biphenyl dioxygenases: Functional versatilities and directed evolution. J Bacteriol 186:5189-5196. (Pubitemid 39038121)
    • (2004) Journal of Bacteriology , vol.186 , Issue.16 , pp. 5189-5196
    • Furukawa, K.1    Suenaga, H.2    Goto, M.3
  • 12
    • 28844466075 scopus 로고    scopus 로고
    • High-throughput screening of enzyme libraries: Thiolactonases evolved by fluorescence-activated sorting of single cells in emulsion compartments
    • DOI 10.1016/j.chembiol.2005.09.012, PII S1074552105003042
    • Aharoni A., Amitai G., Bernath K., Magdassi S., Tawfik D.S. (2005) High-throughput screening of enzyme libraries: Thiolactonases evolved by fluorescence-activated sorting of single cells in emulsion compartments. Chem Biol 12:1281-1289. (Pubitemid 41779468)
    • (2005) Chemistry and Biology , vol.12 , Issue.12 , pp. 1281-1289
    • Aharoni, A.1    Amitai, G.2    Bernath, K.3    Magdassi, S.4    Tawfik, D.S.5
  • 14
    • 14844342448 scopus 로고    scopus 로고
    • Diversifying carotenoid biosynthetic pathways by directed evolution
    • DOI 10.1128/MMBR.69.1.51-78.2005
    • Umeno D., Tobias A.V., Arnold F.H. (2005) Diversifying carotenoid biosynthetic pathways by directed evolution. Microbiol Mol Biol Rev 69:51-78. (Pubitemid 40358067)
    • (2005) Microbiology and Molecular Biology Reviews , vol.69 , Issue.1 , pp. 51-78
    • Umeno, D.1    Tobias, A.V.2    Arnold, F.H.3
  • 15
    • 4644335310 scopus 로고    scopus 로고
    • Directed evolution as a method to create enantioselective cyclohexanone monooxygenases for catalysis in Baeyer-Villiger reactions
    • DOI 10.1002/anie.200460272
    • Reetz M.T., Brunner B., Schneider T., Schulz F., Clouthier C.M., Kayser M.M. (2004) Directed evolution as a method to create enantioselective cyclohexanone monooxygenases for catalysis in Baeyer-Villiger reactions. Angew Chem Int Ed Engl 43:4075-4078. (Pubitemid 39268851)
    • (2004) Angewandte Chemie - International Edition , vol.43 , Issue.31 , pp. 4075-4078
    • Reetz, M.T.1    Brunner, B.2    Schneider, T.3    Schulz, F.4    Clouthier, C.M.5    Kayser, M.M.6
  • 17
    • 0033610475 scopus 로고    scopus 로고
    • Directed evolution to investigate steric control of enzymatic oxidosqualene cyclization. An isoleucine-to-valine mutation in cycloartenol synthase allows lanosterol and parkeol biosynthesis [9]
    • DOI 10.1021/ja992589b
    • Hart E.A., Hua L., Darr L.B., Wilson W.K., Pang J., Matsuda S.P.T. (1999) Directed evolution to investigate steric control of enzymatic oxidosqualene cyclization. An isoleucine- to-valine mutation in cycloartenol synthase allows lanosterol and parkeol biosynthesis. J Am Chem Soc 121:9887-9888. (Pubitemid 29517434)
    • (1999) Journal of the American Chemical Society , vol.121 , Issue.42 , pp. 9887-9888
    • Hart, E.A.1    Hua, L.2    Darr, L.B.3    Wilson, W.K.4    Pang, J.5    Matsuda, S.P.T.6
  • 18
    • 8844224770 scopus 로고    scopus 로고
    • A single-vial analytical and quantitative gas chromatography-mass spectrometry assay for terpene synthases
    • DOI 10.1016/j.ab.2004.09.011, PII S000326970400733X
    • O'Maille P.E., Chappell J., Noel J.P. (2004) A single-vial analytical and quantitative gas chromatography-mass spectrometry assay for terpene synthases. Anal Biochem 335:210-217. (Pubitemid 39535185)
    • (2004) Analytical Biochemistry , vol.335 , Issue.2 , pp. 210-217
    • O'Maille, P.E.1    Chappell, J.2    Noel, J.P.3
  • 19
    • 33646178621 scopus 로고    scopus 로고
    • Designed divergent evolution of enzyme function
    • Yoshikuni Y., Ferrin T.E., Keasling J.D. (2006) Designed divergent evolution of enzyme function. Nature 440: 1078-1082.
    • (2006) Nature , vol.440 , pp. 1078-1082
    • Yoshikuni, Y.1    Ferrin, T.E.2    Keasling, J.D.3
  • 23
    • 0345304457 scopus 로고    scopus 로고
    • Computational Design and Characterization of a Monomeric Helical Dinuclear Metalloprotein
    • DOI 10.1016/j.jmb.2003.10.004
    • Calhoun J.R., Kono H., Lahr S., Wang W., DeGrado W.F., Saven J.G. (2003) Computational design and characterization of a monomeric helical dinuclear metalloprotein. J Mol Biol 334:1101-1115. (Pubitemid 37485692)
    • (2003) Journal of Molecular Biology , vol.334 , Issue.5 , pp. 1101-1115
    • Calhoun, J.R.1    Kono, H.2    Lahr, S.3    Wang, W.4    DeGrado, W.F.5    Saven, J.G.6
  • 24
    • 0035936702 scopus 로고    scopus 로고
    • Statistical theory for protein combinatorial libraries. Packing interactions, backbone flexibility, and the sequence variability of a main-chain structure
    • DOI 10.1006/jmbi.2000.4422
    • Kono H., Saven J.G. (2001) Statistical theory for protein combinatorial libraries. Packing interactions, backbone flexibility, and the sequence variability of a main-chain structure. J Mol Biol 306:607-628. (Pubitemid 33027726)
    • (2001) Journal of Molecular Biology , vol.306 , Issue.3 , pp. 607-628
    • Kono, H.1    Saven, J.G.2
  • 25
    • 0024554228 scopus 로고
    • The structural stability of a protein is an important determinant of its proteolytic susceptibility in Escherichia coli
    • Parsell D.A., Sauer R.T. (1989) The structural stability of a protein is an important determinant of its proteolytic susceptibility in Escherichia coli. J Biol Chem 264: 7590-7595. (Pubitemid 19119177)
    • (1989) Journal of Biological Chemistry , vol.264 , Issue.13 , pp. 7590-7595
    • Parsell, D.A.1    Sauer, R.T.2
  • 26
    • 0037468662 scopus 로고    scopus 로고
    • Selection based on the folding properties of proteins with ribosome display
    • DOI 10.1016/S0014-5793(03)00178-9
    • Matsuura T., Pluckthun A. (2003) Selection based on the folding properties of proteins with ribosome display. FEBS Lett 539:24-28. (Pubitemid 36351281)
    • (2003) FEBS Letters , vol.539 , Issue.1-3 , pp. 24-28
    • Matsuura, T.1    Pluckthun, A.2
  • 27
    • 0036970470 scopus 로고    scopus 로고
    • Quantifying beta-sheet stability by phage display
    • DOI 10.1016/S0022-2836(02)00738-6
    • Distefano M.D., Zhong A., Cochran A.G. (2002) Quantifying beta-sheet stability by phage display. J Mol Biol 322:179-188. (Pubitemid 36132677)
    • (2002) Journal of Molecular Biology , vol.322 , Issue.1 , pp. 179-188
    • Distefano, M.D.1    Zhong, A.2    Cochran, A.G.3
  • 28
    • 2342528494 scopus 로고    scopus 로고
    • Selection of stably folded proteins by phage-display with proteolysis
    • DOI 10.1111/j.1432-1033.2004.04074.x
    • Bai Y., Feng H. (2004) Selection of stably folded proteins by phage-display with proteolysis. Eur J Biochem 271: 1609-1614. (Pubitemid 38586293)
    • (2004) European Journal of Biochemistry , vol.271 , Issue.9 , pp. 1609-1614
    • Bai, Y.1    Feng, H.2
  • 29
    • 0036405903 scopus 로고    scopus 로고
    • Redesign of a four-helix bundle protein by phage display coupled with proteolysis and structural characterization by NMR and X-ray crystallography
    • DOI 10.1016/S0022-2836(02)00884-7
    • Chu R., Takei J., Knowlton J.R., Andrykovitch M., Pei W., Kajava A.V., Steinbach P.J., Ji X., Bai Y. (2002) Redesign of a four-helix bundle protein by phage display coupled with proteolysis and structural characterization by NMR and X-ray crystallography. J Mol Biol 323: 253-262. (Pubitemid 35283690)
    • (2002) Journal of Molecular Biology , vol.323 , Issue.2 , pp. 253-262
    • Chu, R.1    Takei, J.2    Knowlton, J.R.3    Andrykovitch, M.4    Pei, W.5    Kajava, A.V.6    Steinbach, P.J.7    Ji, X.8    Bai, Y.9
  • 30
    • 0033533503 scopus 로고    scopus 로고
    • Core-directed protein design. I. An experimental method for selecting stable proteins from combinatorial libraries
    • Finucane M.D., Tuna M., Lees J.H., Woolfson D.N. (1999) Core-directed protein design. I. An experimental method for selecting stable proteins from combinatorial libraries. Biochemistry 38:11604-11612.
    • (1999) Biochemistry , vol.38 , pp. 11604-11612
    • Finucane, M.D.1    Tuna, M.2    Lees, J.H.3    Woolfson, D.N.4
  • 31
    • 0031759422 scopus 로고    scopus 로고
    • Proteolytic selection for protein folding using filamentous bacteriophages
    • DOI 10.1016/S1359-0278(98)00044-3
    • Kristensen P., Winter G. (1998) Proteolytic selection for protein folding using filamentous bacteriophages. Fold Des 3:321-328. (Pubitemid 28494097)
    • (1998) Folding and Design , vol.3 , Issue.5 , pp. 321-328
    • Kristensen, P.1    Winter, G.2
  • 32
    • 0031729179 scopus 로고    scopus 로고
    • Selecting proteins with improved stability by a phage-based method
    • DOI 10.1038/nbt1098-955
    • Sieber V., Pluckthun A., Schmid F.X. (1998) Selecting proteins with improved stability by a phage-based method. Nat Biotechnol 16:955-960. (Pubitemid 28483625)
    • (1998) Nature Biotechnology , vol.16 , Issue.10 , pp. 955-960
    • Sieber, V.1    Pluckthun, A.2    Schmid, F.X.3
  • 33
    • 0030796451 scopus 로고    scopus 로고
    • Structural basis for cyclic terpene biosynthesis by tobacco 5-epi- aristolochene synthase
    • DOI 10.1126/science.277.5333.1815
    • Starks C.M., Back K., Chappell J., Noel J.P. (1997) Structural basis for cyclic terpene biosynthesis by tobacco 5- epi-aristolochene synthase. Science 277:1815-1820. (Pubitemid 27449192)
    • (1997) Science , vol.277 , Issue.5333 , pp. 1815-1820
    • Starks, C.M.1    Back, K.2    Chappell, J.3    Noel, J.P.4
  • 34
    • 0032053528 scopus 로고    scopus 로고
    • Crystal structure of calcium-independent subtilisin BPN' with restored thermal stability folded without the prodomain
    • DOI 10.1002/(SICI)1097-0134(19980401)31:1<21::AID-PROT3>3.0.CO;2-K
    • Almog O., Gallagher T., Tordova M., Hoskins J., Bryan P., Gilliland G.L. (1998) Crystal structure of calcium-independent subtilisin BPN' with restored thermal stability folded without the prodomain. Proteins 31:21-32. (Pubitemid 28180452)
    • (1998) Proteins: Structure, Function and Genetics , vol.31 , Issue.1 , pp. 21-32
    • Almog, O.1    Gallagher, T.2    Tordova, M.3    Hoskins, J.4    Bryan, P.5    Gilliland, G.L.6
  • 37
    • 0030751628 scopus 로고    scopus 로고
    • Pre-steady-state kinetic analysis of the trichodiene synthase reaction pathway
    • DOI 10.1021/bi963018o
    • Cane D.E., Chiu H.T. Liang P.H., Anderson K.S. (1997) Pre-steady-state kinetic analysis of the trichodiene synthase reaction pathway. Biochemistry 36:8332-8339. (Pubitemid 27297544)
    • (1997) Biochemistry , vol.36 , Issue.27 , pp. 8332-8339
    • Cane, D.E.1    Chiu, H.-T.2    Liang, P.-H.3    Anderson, K.S.4
  • 38
    • 0030752995 scopus 로고    scopus 로고
    • Pre-steady-state study of recombinant sesquiterpene cyclases
    • DOI 10.1021/bi963019g
    • Mathis J.R., Back K., Starks C., Noel J., Poulter C.D., Chappell J. (1997) Pre-steady-state study of recombinant sesquiterpene cyclases. Biochemistry 36: 8340-8348. (Pubitemid 27297545)
    • (1997) Biochemistry , vol.36 , Issue.27 , pp. 8340-8348
    • Mathis, J.R.1    Back, K.2    Starks, C.3    Noel, J.4    Poulter, C.D.5    Chappell, J.6
  • 39
    • 0019471750 scopus 로고
    • Prenyltransferase: Determination of the binding mechanism and individual kinetic constants for farnesylpyrophosphate synthetase by rapid quench and isotope partitioning experiments
    • DOI 10.1021/bi00510a027
    • Laskovics F.M., Poulter C.D. (1981) Prenyltransferase; determination of the binding mechanism and individual kinetic constants for farnesylpyrophosphate synthetase by rapid quench and isotope partitioning experiments. Biochemistry 20:1893-1901. (Pubitemid 11127070)
    • (1981) Biochemistry , vol.20 , Issue.7 , pp. 1893-1901
    • Laskovics, F.M.1    Poulter, C.D.2
  • 40
    • 0031576989 scopus 로고    scopus 로고
    • Prediction of protein side-chain rotamers from a backbone-dependent rotamer library: A new homology modeling tool
    • DOI 10.1006/jmbi.1997.0926
    • Bower M.J., Cohen F.E., Dunbrack R.L. (1997) Prediction of protein side-chain rotamers from a backbone-dependent rotamer library: A new homology modeling tool. J Mol Biol 267:1268-1282. (Pubitemid 27192637)
    • (1997) Journal of Molecular Biology , vol.267 , Issue.5 , pp. 1268-1282
    • Bower, M.J.1    Cohen, F.E.2    Dunbrack Jr., R.L.3
  • 42
    • 0037325329 scopus 로고    scopus 로고
    • EF-Tu binding peptides identified, dissected, and affinity optimized by phage display
    • DOI 10.1016/S1074-5521(03)00025-5
    • Murase K., Morrison K.L., Tam P.Y., Stafford R.L., Jurnak F., Weiss G.A. (2003) EF-Tu binding peptides identified, dissected, and affinity optimized by phage display. Chem Biol 10:161-168. (Pubitemid 36250974)
    • (2003) Chemistry and Biology , vol.10 , Issue.2 , pp. 161-168
    • Murase, K.1    Morrison, K.L.2    Tam, P.Y.3    Stafford, R.L.4    Jurnak, F.5    Weiss, G.A.6
  • 44
    • 0023613953 scopus 로고
    • Rapid and efficient site-specific mutagenesis without phenotypic selection
    • Kunkel T.A., Roberts J.D., Zakour R.A. (1987) Rapid and efficient site-specific mutagenesis without phenotypic selection. Methods Enzymol 154:367-382.
    • (1987) Methods Enzymol , vol.154 , pp. 367-382
    • Kunkel, T.A.1    Roberts, J.D.2    Zakour, R.A.3
  • 46
    • 33646145081 scopus 로고    scopus 로고
    • Biosynthetic potential of sesquiterpene synthases: Alternative products of tobacco 5-epi-aristolochene synthase
    • O'Maille P.E., Chappell J., Noel J.P. (2006) Biosynthetic potential of sesquiterpene synthases: Alternative products of tobacco 5-epi-aristolochene synthase. Arch Biochem Biophys 448:73-82.
    • (2006) Arch Biochem Biophys , vol.448 , pp. 73-82
    • O'Maille, P.E.1    Chappell, J.2    Noel, J.P.3
  • 47
    • 0029822194 scopus 로고    scopus 로고
    • Purification of overproduced Escherichia coli RNA polymerase sigma factors by solubilizing inclusion bodies and refolding from Sarkosyl
    • Burgess R.R. (1996) Purification of overproduced Escherichia coli RNA polymerase sigma factors by solubilizing inclusion bodies and refolding from Sarkosyl. Methods Enzymol 273:145-149.
    • (1996) Methods Enzymol , vol.273 , pp. 145-149
    • Burgess, R.R.1
  • 48
    • 0001836628 scopus 로고    scopus 로고
    • Cyclization enzymes in the biosynthesis of monoterpenes, sesquiterpenes, and diterpenes
    • Leeper FJ, Vederas JC, Ed Springer-Verlag, Berlin
    • Davis E.M., Croteau R, Cyclization enzymes in the biosynthesis of monoterpenes, sesquiterpenes, and diterpenes In: Leeper FJ, Vederas JC, Ed (2000) Topics in Current Chemistry: Biosynthesis: Aromatic Polyketides, Isoprenoids, Alkaloids. Springer-Verlag, Berlin, vol. 209, pp 53-95.
    • (2000) Topics in Current Chemistry: Biosynthesis: Aromatic Polyketides, Isoprenoids, Alkaloids , vol.209 , pp. 53-95
    • Davis, E.M.1    Croteau, R.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.