Oxylipins designate oxygenated unsaturated C18 fatty acids. Many filamentous fungi pathogens contain dioxygenases (DOX) in oxylipin biosynthesis with homology to human cyclooxygenases. They contain a DOX domain, which is often fused to a functional cytochrome P450 at the C-terminal end. A Tyr radical in the DOX domain initiates dioxygenation of linoleic acid by hydrogen abstraction with formation of 8-, 9-, or 10-hydroperoxy metabolites. The P450 domains can catalyze heterolytic cleavage of 8- and 10-hydroperoxides with oxidation of the heme thiolate iron for hydroxylation at C-5, C-7, C-9, or C-11 and for epoxidation of the 12Z double bond; thus displaying linoleate diol synthase (LDS) and epoxy alcohol synthase (EAS) activities. LSD activities are present in the rice blast pathogen Magnaporthe oryzae, Botrytis cinerea causing grey mold and the black scurf pathogen Rhizoctonia solani. 10R-DOX-EAS has been found in M. oryzae and Fusarium oxysporum. The P450 domains may also catalyze homolytic cleavage of 8- and 9-hydroperoxy fatty acids and dehydration to produce epoxides with an adjacent double bond, i.e., allene oxides, thus displaying 8- and 9-DOX-allene oxide synthases (AOS). F. oxysporum, F. graminearum, and R. solani express 9S-DOX-AOS and Zymoseptoria tritici 8S-and 9R-DOX-AOS. Homologues are present in endemic human-pathogenic fungi with extensive studies in Aspergillus fumigatus, A. flavus (also a plant pathogen) as well as the genetic model A. nidulans. 8R-and 10R-DOX appear to bind fatty acids “headfirst” in the active site, whereas 9S-DOX binds them “tail first” in analogy with cyclooxygenases. The biological relevance of 8R-DOX-5,8-LDS (also designated PpoA) was first discovered in relation to sporulation of A. nidulans and recently for development and programmed hyphal branching of A. fumigatus. Gene deletion DOX-AOS homologues in F. verticillioides, A. flavus, and A. nidulans alters, inter alia, mycotoxin production, sporulation, and gene expression.

Oxylipins 表示氧化的不饱和 C18 脂肪酸。许多丝状真菌病原体在氧化脂生物合成中含有与人类环氧合酶同源的双加氧酶 (DOX)。它们包含一个 DOX 结构域，该结构域通常在 C 末端与功能性细胞色素 P450 融合。DOX 结构域中的 Tyr 自由基通过夺氢引发亚油酸的双氧合，形成 8-、9-或 10-氢过氧代谢物。P450 结构域可以催化 8-和 10-氢过氧化物的异裂裂解，同时氧化硫醇血红素铁，在 C-5、C-7、C-9 或 C-11 上进行羟基化和 12Z 双键的环氧化；因此显示出亚油酸二醇合酶 (LDS) 和环氧醇合酶 (EAS) 的活性。LSD活性存在于稻瘟病病原体稻瘟病菌中，Botrytis cinerea引起灰霉病和黑色皮屑病原体立枯丝核菌。10R-DOX-EAS 已在M. oryzae和Fusarium oxysporum中发现。P450结构域还可以催化8-和9-氢过氧脂肪酸的均裂和脱水以产生具有相邻双键的环氧化物，即丙二烯氧化物，从而展示8-和9-DOX-丙二烯氧化物合酶(AOS)。F. oxysporum、F. graminearum和R. solani表达 9 S -DOX-AOS 和Zymoseptoria tritici 8 S -和 9 R -DOX-AOS。同源物存在于地方性人类病原真菌中，并在烟曲霉、黄曲霉（也是一种植物病原体）以及遗传模型构巢曲霉。8R-和 10R-DOX 似乎在活性位点“头先”结合脂肪酸，而 9S-DOX 与环氧合酶类似地“尾先”结合它们。8R-DOX-5,8-LDS（也称为 PpoA）的生物学相关性首次被发现与构巢曲霉的孢子形成有关，最近与烟曲霉的发育和程序化菌丝分枝有关。F. verticillioides、A. flavus和A. nidulans中的基因缺失 DOX-AOS 同源物尤其会改变霉菌毒素的产生、孢子形成和基因表达。