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Volumn 3, Issue 18, 2005, Pages 3388-3398

Synthesis of (6R)- And (6S)-5,10-dideazatetrahydrofolate oligo-γ-glutamates: Kinetics of multiple glutamate ligations catalyzed by folylpoly-γ-glutamate synthetase

Author keywords

[No Author keywords available]

Indexed keywords

ANTICANCER DRUGS; GLUTAMIC ACID; MICHAELIS-MENTEN KINETICS; STEADY-STATE KINETIC CONSTANTS;

EID: 26444508495     PISSN: 14770520     EISSN: None     Source Type: Journal    
DOI: 10.1039/b505907k     Document Type: Article
Times cited : (11)

References (55)
  • 2
    • 0000083882 scopus 로고
    • ed. R. L. Blakley and S. J. Benkovic, John Wiley & Sons, New York
    • J. J. McGuire, and J. K. Coward, in Folates and Pterins, ed. R. L. Blakley and S. J. Benkovic, John Wiley & Sons, New York, 1984, pp. 135-190.
    • (1984) Folates and Pterins , pp. 135-190
    • McGuire, J.J.1    Coward, J.K.2
  • 39
    • 0004262303 scopus 로고
    • Academic Press, New York
    • M. Dixon, and E. C. Webb, Enzymes (3rd edn), Academic Press, New York, 1979. Eqn (2) is valid under our assay conditions of fixed, saturating concentrations of ATP and glutamate.
    • (1979) Enzymes (3rd Edn)
    • Dixon, M.1    Webb, E.C.2
  • 44
    • 26444476548 scopus 로고    scopus 로고
    • note
    • Additional reducing agent was not included in these reactions, as early experiments with hFPGS expressed in E. coli indicated no measurable effect of the presence of reducing agent on enzyme activity or product distribution. However, the reactions that utilized enzyme expressed in E. coli had a final concentration of 4 mM 2-mercaptoethanol due to its presence in the enzyme storage buffer. In contrast, the reactions in which enzyme expressed in SF-9 insect cells had been used, the final concentration of 2-mercaptoethanol was 0.4 mM. Subsequently, it was determined that additional reducing agent (100 mM 2-mercaptoethanol or 5 mM dithiothreitol) increased the chain-length of the polyglutamate products produced only for the hFPGS expressed in SF-9 insect cells. This observation suggests that the addition of reducing agent to the assays shown in Fig. 3 would intensify the observed substrate inhibition.
  • 47
    • 26444529039 scopus 로고    scopus 로고
    • J. W. Tomsho, Ph.D. dissertation, University of Michigan, Ann Arbor, MI, 2005
    • J. W. Tomsho, Ph.D. dissertation, University of Michigan, Ann Arbor, MI, 2005.
  • 48
    • 0003518480 scopus 로고
    • John Wiley & Sons, New York
    • I. H. Segel, Enzyme Kinetics, John Wiley & Sons, New York, 1975.
    • (1975) Enzyme Kinetics
    • Segel, I.H.1
  • 54
    • 26444478676 scopus 로고
    • ed. H.-C. Curtius, S. Ghisla and N. Blau, Walter de Gruyter, Berlin
    • C. J. Barnett, and T. M. Wilson, in Chemistry and Biology of Pteridines 1989, ed. H.-C. Curtius, S. Ghisla and N. Blau, Walter de Gruyter, Berlin, 1990, pp. 102-105.
    • (1990) Chemistry and Biology of Pteridines 1989 , pp. 102-105
    • Barnett, C.J.1    Wilson, T.M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.