dc.contributor.author | Schilstra, M. | |
dc.contributor.author | Veldink, G.A. | |
dc.contributor.author | Verhagen, J. | |
dc.contributor.author | Vliegenthart, J.F.G. | |
dc.date.accessioned | 2008-11-27T09:03:21Z | |
dc.date.available | 2008-11-27T09:03:21Z | |
dc.date.issued | 1992 | |
dc.identifier.citation | Schilstra , M , Veldink , G A , Verhagen , J & Vliegenthart , J F G 1992 , ' Effect of lipid hydroperoxide on lipoxygenase kinetics ' , Biochemistry , vol. 31 , no. 33 , pp. 7692-7699 . https://doi.org/10.1021/bi00148a033 | |
dc.identifier.issn | 0006-2960 | |
dc.identifier.other | PURE: 90153 | |
dc.identifier.other | PURE UUID: 890e4073-dd69-47a9-b9e9-d7a1c5ebfc8d | |
dc.identifier.other | dspace: 2299/2651 | |
dc.identifier.other | Scopus: 0026793890 | |
dc.identifier.uri | http://hdl.handle.net/2299/2651 | |
dc.description | Original article can be found at: http://pubs.acs.org/journals/bichaw/index.html Copyright American Chemical Society DOI: 10.1021/bi00148a033 [Full text of this article is not available in the UHRA] | |
dc.description.abstract | In order to investigate the activation of lipoxygenase and to clarify the role of the oxygenation product hydroperoxide in this process, the effect of 13-hydroperoxylinoleic acid (P, 0-35 pM) on linoleic acid (S, 1-80 pM) oxygenation catalysis by 12 nM lipoxygenase-1 from soybean was studied at pH 10, 25 OC, and 240 pM 02 with rapid kinetic techniques. The following observations were made: (1) Iron(I1) and iron(II1) lipoxygenases are kinetically different: reactions started with the Fe(I1) enzyme form show a lag phase, whereas iron(II1) lipoxygenase induces an initial burst. (2) Oxidation of the enzyme alone is not sufficient to abolish the lag phase: at [SI > 50 pM, the initial burst in the iron(II1) lipoxygenase curves is still followed by a lag. The lag phase disappears completely only in the presence of micromolar quantities of P. (3) The approximate dissociation constants for S and P are 15 and 24 pM, respectively, 1 order of magnitude smaller than the corresponding values in the absence of oxygen. The observed kinetics are predicted by numerical integration of the rate equations of a model based on the single lipid binding site mechanism for the anaerobic lipoxygenase reaction [Ludwig et al. (1987) Eur. J. Biochem. 168,325- 337; Verhagen et al. (1978) Biochim. Biophys. Acta 529, 369-3791, A quasi-steady-state approximation of the model suggests that at high [S]/[P] the fraction of active iron(II1) lipoxygenase is small and that, therefore, a lag phase is intrinsic to the mechanism. | en |
dc.language.iso | eng | |
dc.relation.ispartof | Biochemistry | |
dc.title | Effect of lipid hydroperoxide on lipoxygenase kinetics | en |
dc.contributor.institution | School of Computer Science | |
dc.description.status | Peer reviewed | |
rioxxterms.versionofrecord | https://doi.org/10.1021/bi00148a033 | |
rioxxterms.type | Journal Article/Review | |
herts.preservation.rarelyaccessed | true | |