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Volumn 118, Issue 8, 1996, Pages

On the stereochemical course of human protein-farnesyl transferase

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EID: 5244300102     PISSN: 00027863     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (3)

References (48)
  • 3
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    • Casey, P. J. Science 1995, 268, 221-225
    • (1995) Science , vol.268 , pp. 221-225
    • Casey, P.J.1
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    • Tamanoi, F. TIBS 1993, 18, 349-353.
    • (1993) TIBS , vol.18 , pp. 349-353
    • Tamanoi, F.1
  • 10
    • 0028145239 scopus 로고
    • The first crystal structure of a prenyltransferase (avian FPP synthase), has only recently been reported: Tarshis, L. C.; Yan, M.; Poulter, C. D.; Sacchettim, J. C. Biochemistry 1994, 33, 10871-10877.
    • (1994) Biochemistry , vol.33 , pp. 10871-10877
    • Tarshis, L.C.1    Yan, M.2    Poulter, C.D.3    Sacchettim, J.C.4
  • 20
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    • note
    • 21
  • 23
    • 5244357265 scopus 로고    scopus 로고
    • note
    • The Boc-protected amino acid reagents were from Bachem, and all other synthetic reagents were from Aldrich unless otherwise noted. Solvents were from Aldrich, Fisher, or Curtin-Matheson and were used as received unless otherwise indicated. HPLC work was carried out using HPLC-grade solvents on a Waters system consisting of a U6K injector, two 501 pumps, and a 490E multiwavelength UV detector.
  • 26
    • 0014607241 scopus 로고
    • 2 is subject to a very large primary isotope effect: Goldman, I. M. J. Org. Chem. 1969, 34, 3289-3295.
    • (1969) J. Org. Chem. , vol.34 , pp. 3289-3295
    • Goldman, I.M.1
  • 31
    • 0027409747 scopus 로고
    • 1H-NMR studies on this deuterated famesylated N-benzoyldipeplide model system indicated that the signal for the C-1 farnesyl proton appeared as two doublets at 3.3 ppm (see also ref 42). The upfield shift of the C-1 signal seen with peptides 3 and 4 may be due to deshielding by the naphthyl ring of the dansyl group.
    • (1993) Bioorg. Med. Chem. Lett. , vol.3 , pp. 281-284
    • Gibbs, R.A.1    Mu, Y.Q.2    Wang, F.3
  • 43
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    • note
    • Note that if partial but significant racemization occurred during the PFTase reaction, then the diasteromeric excess of the biosynthetic 4 must he less than the 62% calculated for the synthetic sample of 3, since both are derived from the same sample of farnesyl chloride 14. In other words, this would mean that the minor negative peak in Figure 2c (at 2.807 ppm) would be larger than the minor negative peak in Figure 2b (at 2.825 ppm). Despite the significant noise level in Figure 2c, this does not appear to be the case, as such a peak would be more clearly visible above the noise. Thus, although we are only able to provide estimates of the diasteromeric excess of the biosynthetic farnesylated peptides, visual inspection of the spectra bolsters our confidence that the enzymatic transfer is accompanied by little if any racemization.


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