Tall Tuomas, Puigbò Pere
Department of Biology, University of Turku, 20500 Turku, Finland.
Nutrition and Health Unit, Eurecat Technology Center of Catalonia, 43204 Reus, Catalonia, Spain.
BioTech (Basel). 2022 Jul 26;11(3):28. doi: 10.3390/biotech11030028.
The 5-enolpyruvylshikimate 3-phosphate synthase (EPSPS) is the central enzyme of the shikimate pathway to synthesize the three aromatic amino acids in fungi, plants, and prokaryotes. This enzyme is the target of the herbicide glyphosate. In most plants and prokaryotes, the EPSPS protein is constituted by a single domain family, the EPSP synthase (PF00275) domain, whereas in fungi, the protein is formed by a multi-domain structure from combinations of 22 EPSPS-associated domains. The most common multi-domain EPSPS structure in fungi involves five EPSPS-associated domains of the shikimate pathway. In this article, we analyze 390 EPSPS proteins of fungi to determine the extent of the EPSPS-associated domains. Based on the current classification of the EPSPS protein, most fungal species are intrinsically sensitive to glyphosate. However, complex domain architectures may have multiple responses to the herbicide. Further empirical studies are needed to determine the effect of glyphosate on fungi, taking into account the diversity of multi-domain architectures of the EPSPS. This research opens the door to novel biotechnological applications for microbial degradation of glyphosate.
5-烯醇丙酮酰莽草酸-3-磷酸合酶（EPSPS）是真菌、植物和原核生物中合成三种芳香族氨基酸的莽草酸途径的关键酶。这种酶是除草剂草甘膦的作用靶点。在大多数植物和原核生物中，EPSPS蛋白由单个结构域家族即EPSP合酶（PF00275）结构域组成，而在真菌中，该蛋白由22个与EPSPS相关的结构域组合形成的多结构域结构构成。真菌中最常见的多结构域EPSPS结构涉及莽草酸途径的五个与EPSPS相关的结构域。在本文中，我们分析了390种真菌的EPSPS蛋白，以确定与EPSPS相关的结构域的范围。根据目前对EPSPS蛋白的分类，大多数真菌物种对草甘膦具有内在敏感性。然而，复杂的结构域架构可能对除草剂有多种反应。考虑到EPSPS多结构域架构的多样性，需要进一步的实证研究来确定草甘膦对真菌的影响。这项研究为草甘膦微生物降解的新型生物技术应用打开了大门。
