PURIFICATION OF AN ALLENE OXIDE SYNTHASE AND IDENTIFICATION OF THE ENZYME AS A CYTOCHROME-P-450
PURIFICATION OF AN ALLENE OXIDE SYNTHASE AND IDENTIFICATION OF THE ENZYME AS A CYTOCHROME-P-450
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DOI：
10.1126/science.1876834
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发表时间：
1991-08-16
期刊：
影响因子：
56.9
通讯作者：
BRASH, AR
中科院分区：
文献类型：
--
作者：
SONG, WC;BRASH, AR
脂肪酸氢过氧化物(脂氧合酶产物)被一种在植物、珊瑚和海星卵母细胞中检测到的脱水酶代谢成丙二烯氧化物。丙二烯氧化物是更复杂产品的不稳定环氧化物前体，如植物生长激素茉莉酸。亚麻籽脱水酶特性分析表明，亚麻籽脱水酶是一种55kodalton的血红蛋白。该脱水酶的光谱特征表明它是一种细胞色素P-450。它以超过或等于每秒1000次成交量的惊人活动运行。这些结果建立了一种新的细胞色素P-450的催化活性，并说明了不同的加氧酶在脂肪酸代谢途径中的协同作用。
Fatty acid hydroperoxides (lipoxygenase products) are metabolized to allene oxides by a type of dehydrase that has been detected in plants, corals, and starfish oocytes. The allene oxides are unstable epoxide precursors of more complex products such as jasmonic acid, the plant growth hormone. Characterization of the dehydrase enzyme of flaxseed revealed that it is a 55-kilodalton hemoprotein. The spectral characteristics of this dehydrase revealed it to be a cytochrome P-450. It operates with the remarkable activity of greater-than-or-equal-to 1000 turnovers per second. The results establish a new catalytic activity for a cytochrome P-450 and illustrate the cooperation of different oxygenases in pathways of fatty acid metabolism.