Gaffney B J
Chemistry Department, Johns Hopkins University, Baltimore, Maryland 21218-2685, USA.
Annu Rev Biophys Biomol Struct. 1996;25:431-59. doi: 10.1146/annurev.bb.25.060196.002243.
Lipoxygenases catalyze the formation of fatty acid hydroperoxides, products used in further biochemical reactions leading to normal and pathological cell functions. X-ray structure analysis and spectroscopy have been applied to elucidate the mechanism of lipoxygenases. Two X-ray structures of soybean lipoxygenase-1 reveal the side chains of three histidines and the COO- of the carboxy terminus as ligands to the catalytically important iron atom. The enzyme contains a novel three-turn pi-helix near the iron center. Spectroscopic studies, including electron magnetic resonance, X-ray absorption spectroscopy, infrared circular dichroism, and magnetic circular dichroism, have been applied to compare lipoxygenases from varied sources and with different substrate positional specificity.
脂氧合酶催化脂肪酸氢过氧化物的形成,这些产物用于进一步的生化反应,从而导致正常和病理细胞功能。X射线结构分析和光谱学已被应用于阐明脂氧合酶的作用机制。大豆脂氧合酶-1的两个X射线结构揭示了三个组氨酸的侧链以及羧基末端的COO-作为与催化重要铁原子的配体。该酶在铁中心附近含有一个新型的三圈π-螺旋。光谱学研究,包括电子磁共振、X射线吸收光谱、红外圆二色性和磁圆二色性,已被用于比较来自不同来源和具有不同底物位置特异性的脂氧合酶。