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Volumn 125, Issue 30, 2003, Pages 8988-8989

An unusual isotope effect on substrate inhibition in the oxidation of arachidonic acid by lipoxygenase

Author keywords

[No Author keywords available]

Indexed keywords

ARACHIDONIC ACID; ISOTOPE; LIPOXYGENASE;

EID: 0041866686     PISSN: 00027863     EISSN: None     Source Type: Journal    
DOI: 10.1021/ja035977t     Document Type: Article
Times cited : (25)

References (27)
  • 13
    • 0042459666 scopus 로고    scopus 로고
    • note
    • Such impurities could be either inhibitors in the unlabeled substrate or peroxide activators in the labeled substrate.
  • 14
    • 0042960743 scopus 로고
    • Ph.D. Thesis, University of Wisonsin-Madison
    • 2O induced a change in the distribution of this enzyme form. The inhibition described here for SLO also involves a change in the distribution of the E-S• form.
    • (1987)
    • Bencke Marti, K.M.1
  • 16
    • 0034712662 scopus 로고    scopus 로고
    • These results argue against binding of arachidonic acid to an allosteric site as the major cause for substrate inhibition. Other experiments are required to rule out any allosteric inhibition by AA. For examples of such a type of inhibition of SLO, see ref 15 and: Mogul, R.; Johansen, E.; Holman, T. R. Biochemistry 2000, 39, 4801-4807. Ruddat, V. C.; Whitman, S.; Holman, T. R.; Bemasconi, C. F. Biochemistry 2003, 42, 4172-4178.
    • (2000) Biochemistry , vol.39 , pp. 4801-4807
    • Mogul, R.1    Johansen, E.2    Holman, T.R.3
  • 17
    • 0037446632 scopus 로고    scopus 로고
    • These results argue against binding of arachidonic acid to an allosteric site as the major cause for substrate inhibition. Other experiments are required to rule out any allosteric inhibition by AA. For examples of such a type of inhibition of SLO, see ref 15 and: Mogul, R.; Johansen, E.; Holman, T. R. Biochemistry 2000, 39, 4801-4807. Ruddat, V. C.; Whitman, S.; Holman, T. R.; Bemasconi, C. F. Biochemistry 2003, 42, 4172-4178.
    • (2003) Biochemistry , vol.42 , pp. 4172-4178
    • Ruddat, V.C.1    Whitman, S.2    Holman, T.R.3    Bemasconi, C.F.4
  • 21
    • 0037328843 scopus 로고    scopus 로고
    • For a discussion of hydrogen atom abstraction versus proton coupled electron transfer, see: Lehnert, N.; Solomon, E. I. J. Biol. Inorg. Chem. 2003, 8, 294-305.
    • (2003) J. Biol. Inorg. Chem. , vol.8 , pp. 294-305
    • Lehnert, N.1    Solomon, E.I.2
  • 25
    • 0037072303 scopus 로고    scopus 로고
    • Certain compounds are potent inhibitors of lipoxygenases by virtue of binding strongly to the ferrous enzyme. See: Moody, J. S.; Mamett, L. J. Biochemistry 2002, 41, 10297-10303.
    • (2002) Biochemistry , vol.41 , pp. 10297-10303
    • Moody, J.S.1    Mamett, L.J.2
  • 26
    • 0042459665 scopus 로고    scopus 로고
    • note
    • This observation suggests that (part of) substrate inhibition may also be initiated by dissociation of the peroxy radical from the ferrous enzyme. However, this would not explain the observed isotope effect on substrate inhibition.
  • 27
    • 0031587044 scopus 로고    scopus 로고
    • i = 1.5 mM). This inhibition is also relieved at higher levels of oxygen: Berry, H.; Debat, H.; Larretta-Garde, V. FEBS Lett. 1997, 408, 324-6.
    • (1997) FEBS Lett. , vol.408 , pp. 324-326
    • Berry, H.1    Debat, H.2    Larretta-Garde, V.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.