Steczko J, Axelrod B
Department of Biochemistry, Purdue University West Lafayette, Indiana 47906-1153.
Biochem Biophys Res Commun. 1992 Jul 31;186(2):686-9. doi: 10.1016/0006-291x(92)90801-q.
Lipoxygenases constitute a class of non-heme, non-sulfur iron dioxygenases acting upon lipids possessing a 1,4-cis-cis-pentadiene moiety. The iron is known to be essential for activity. A motif of six histidine residues has been found in all of the thirteen lipoxygenases, from both plant and animal sources, whose sequences have been reported. We had previously obtained mutant proteins in which each of the 6 conserved histidines of soybean lipoxygenase L-1 had been replaced and found that the mutants H499Q, H504Q (or H504S) and H690Q had no detectable enzymatic activity. We have now found that these inactive proteins contain no Fe, although they have the same electrophoretic mobility as wild-type L-1 under both denaturing and non-denaturing conditions and react with anti-L-1 antibodies.
脂氧合酶是一类非血红素、非硫的铁双加氧酶，作用于具有1,4-顺-顺-戊二烯部分的脂质。已知铁对酶活性至关重要。在已报道序列的所有13种来自植物和动物来源的脂氧合酶中，都发现了一个由六个组氨酸残基组成的基序。我们之前获得了大豆脂氧合酶L-1的6个保守组氨酸中的每一个都被替换的突变蛋白，发现突变体H499Q、H504Q（或H504S）和H690Q没有可检测到的酶活性。我们现在发现，这些无活性的蛋白质不含铁，尽管它们在变性和非变性条件下都具有与野生型L-1相同的电泳迁移率，并且能与抗L-1抗体反应。
