Fatty acid amide hydrolase (FAAH) is an enzyme that belongs to the amidase signature (AS) superfamily and is widely distributed in multicellular eukaryotes. FAAH hydrolyzes lipid signaling molecules – namely, N-acylethanolamines (NAEs) – which terminates their actions. Recently, the crystal structure of Arabidopsis thaliana FAAH was solved and key residues were identified for substrate-specific interactions. Here, focusing on residues surrounding the substrate-binding pocket, a comprehensive analysis of FAAH sequences from angiosperms reveals a distinctly different family of FAAH-like enzymes. We hypothesize that FAAH, in addition to its role in seedling development, also acts in an N-acyl amide communication axis to facilitate plant–microbe interactions and that structural diversity provides for the flexible use of a wide range of small lipophilic signaling molecules.

脂肪酸酰胺水解酶（FAAH）是一种属于酰胺酶签名（AS）超家族的酶，广泛分布于多细胞真核生物中。FAAH水解脂质信号分子-N-酰基乙醇胺（NAE）-终止其作用。最近，解决了拟南芥FAAH的晶体结构，并确定了关键残基用于底物特异性相互作用。在这里，着眼于底物结合袋周围的残基，对被子植物中FAAH序列的全面分析揭示了FAAH类酶的家族截然不同。我们假设FAAH，除了其在幼苗发育的作用，也作用在ñ-酰基酰胺通讯轴促进植物与微生物之间的相互作用，并且结构的多样性为灵活使用各种小的亲脂性信号分子提供了便利。