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Volumn 279, Issue 5358, 1998, Pages 1958-1961

Redesigning enzyme topology by directed evolution

Author keywords

[No Author keywords available]

Indexed keywords

CHORISMATE MUTASE;

EID: 0032549781     PISSN: 00368075     EISSN: None     Source Type: Journal    
DOI: 10.1126/science.279.5358.1958     Document Type: Article
Times cited : (118)

References (33)
  • 10
    • 0027265713 scopus 로고
    • A. P. Brunet et al., Nature 364, 355 (1993).
    • (1993) Nature , vol.364 , pp. 355
    • Brunet, A.P.1
  • 16
    • 16044367245 scopus 로고    scopus 로고
    • C. J. Bult et al., Science 273, 1058 (1996).
    • (1996) Science , vol.273 , pp. 1058
    • Bult, C.J.1
  • 18
    • 0031035099 scopus 로고    scopus 로고
    • 4) because of the steeper temperature dependence of the uncatalyzed reaction.
    • (1997) Tetrahedron Lett. , vol.38 , pp. 1467
  • 21
    • 7144255201 scopus 로고    scopus 로고
    • note
    • f using the PCR with template pKMCMT-W and primers SEQT-S (5′-GTGAGCG-GATAACAATTTCACA-3′) and MJMA-N (5′-TCAG-CAATAAGCTTTTCSNNSNNSNNSNNSNNSNNC-TTAAGGATCTTATTGTCAATCTCATCAATCT- 3′) (N = A, C, G, or T; S = C or G). Cloning of this library of products into pKMCMT-NEG with restriction enzymes Nde I and Hind III gave library pKMCMT-LibA.
  • 23
    • 7144251548 scopus 로고    scopus 로고
    • note
    • The host strain for protein production was KA13, a CM-deficient E. coli with an isopropyl β-D-thiogalactopyranoside-inducible T7 RNA polymerase gene integrated into the chromosome.
  • 25
    • 0002498995 scopus 로고
    • S. E. Harding, A. J. Rowe, J. C. Horton, Eds. Royal Society of Chemistry, Cambridge, England
    • Sedimentation equilibrium runs were performed from 3000 to 17,000 revolutions per minute with 2, 10, and 30 μM protein concentrations in phosphate-buffered saline (PBS) at 20°C. Partial specific volumes and solvent densities were calculated with the program Sednterp [T. M. Laue, B. D. Shah, T. M. Ridgeway, S. L. Pelletier, in Analytical Ultracentrifugation in Biochemistry and Polymer Science, S. E. Harding, A. J. Rowe, J. C. Horton, Eds. (Royal Society of Chemistry, Cambridge, England, 1992), pp. 90-125] and data were analyzed by nonlinear least-squares fitting with the Origin software provided by Beckman.
    • (1992) Analytical Ultracentrifugation in Biochemistry and Polymer Science , pp. 90-125
    • Laue, T.M.1    Shah, B.D.2    Ridgeway, T.M.3    Pelletier, S.L.4
  • 29
    • 7144259428 scopus 로고    scopus 로고
    • Supplementary material
    • Supplementary material is available at www. sciencemag.org/feature/data/976438.shl.
  • 30
    • 7144228976 scopus 로고    scopus 로고
    • note
    • m were calculated from the initial rates.
  • 32
    • 7144254826 scopus 로고    scopus 로고
    • note
    • Removing six amino acids from the carboxyl terminus of MjCM increased its resistance to proteolytic cleavage without affecting the properties of the protein. Consequently, all detailed biochemical and biophysical characterizations of mMjCM were also carried out on a truncated derivative, which behaved identically to the full-length mMjCM in all aspects tested.
  • 33
    • 7144258198 scopus 로고    scopus 로고
    • note
    • We thank H. Lashuel and J. Kelly for analytical ultra-centrifugation studies. G.M. is the recipient of a Natural Sciences and Engineering Research Council of Canada 1967 Centennial Postgraduate Scholarship and an Eli Lilly Graduate Student Fellowship. Supported by the Skaggs Institute for Chemical Biology at The Scripps Research Institute.


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.