PURIFICATION OF AN ALLENE OXIDE SYNTHASE AND IDENTIFICATION OF THE ENZYME AS A CYTOCHROME-P-450

被引：234

作者：

SONG, WC ^{[1
]}

BRASH, AR ^{[1
]}

机构：

[1] VANDERBILT UNIV,MED CTR,SCH MED,DEPT PHARMACOL,NASHVILLE,TN 37232

来源：

SCIENCE | 1991年 / 253卷 / 5021期

关键词：

D O I：

10.1126/science.1876834

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

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.

引用

页码：781 / 784

页数：4

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