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(i) Knapp, M. J.; Rickert, K.; Klinman, J. P. J. Am. Chem. Soc. 2002, 124, 3865-3874.
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(j) For isotope effect studies using labeled LA and human 15-LO, see: Lewis, E. R.; Johansen, E.; Holman, T. R. J. Am. Chem. Soc. 1999, 121, 1395-1396.
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0042459666
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note
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Such impurities could be either inhibitors in the unlabeled substrate or peroxide activators in the labeled substrate.
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14
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0042960743
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Ph.D. Thesis, University of Wisonsin-Madison
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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.
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Bencke Marti, K.M.1
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0034712662
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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.
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0037446632
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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.
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Ludwig, P.; Holzhutter, H. G.; Colosimo, A.; Silvestrini, M. C.; Schewe, T.; Rapoport, S. M. Eur. J. Biochem. 1987, 168, 325-337.
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0037072303
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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.
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26
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0042459665
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note
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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.
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27
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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.
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