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

Journal of the American Chemical Society
Sheng Peng, W A van der Donk

Abstract

Soybean lipoxygenase catalyzes the oxidation of arachidonic acid to 15S-HPETE. The reaction displays strong substrate inhibition with unlabeled substrate but no discernible substrate inhibition with arachidonic acid labeled with deuterium at C13, the site of hydrogen/deuterium atom abstraction. The unusual behavior is due primarily to a large kinetic isotope effect on Km,O2 as a result of the strong selection against deuterium in the abstraction step.

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Citations

Jul 16, 2013·Chemical Reviews·Katarzyna Swiderek, Piotr Paneth
Oct 31, 2008·Organic & Biomolecular Chemistry·Cyril JacquotWilfred A van der Donk
Sep 17, 2008·Bioorganic & Medicinal Chemistry Letters·Cyril JacquotWilfred A van der Donk
Sep 19, 2014·The Journal of Biological Chemistry·David B NeauMarcia E Newcomer
Nov 14, 2015·The Journal of Biological Chemistry·Yi Liu, Justine P Roth
Jul 30, 2020·Molecules : a Journal of Synthetic Chemistry and Natural Product Chemistry·Adam R Offenbacher, Theodore R Holman
Feb 6, 2017·Amino Acids·Tatyana V KorneenkoMikhail S Shchepinov
Sep 4, 2019·Biochemical and Biophysical Research Communications·Kaspar PõldemaaPriit Eek
Feb 3, 2006·The Journal of Physical Chemistry. a·Hironori KitaguchiShunichi Fukuzumi
Mar 12, 2011·Journal of Inorganic Biochemistry·Gang WuAh-lim Tsai

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