Polidori Nakia, Babin Peter, Daniel Bastian, Gruber Karl
Institute of Molecular Biosciences, University of Graz, Graz, Austria.
Dipartimento di Scienze della Vita e Biologia dei Sistemi, Università di Torino, Torino, Italy.
Proteins. 2025 Jun;93(6):1181-1188. doi: 10.1002/prot.26800. Epub 2025 Jan 22.
The Old Yellow Enzyme from Ferrovum sp. JA12 (FOYE) displays an unusual thermal stability for an enzyme isolated from a mesophilic organism. We determined the crystal structure of this enzyme and performed bioinformatic characterization to get insights into its thermal stability. The enzyme displays a tetrameric quaternary structure; however, unlike the other tetrameric homologs, it clusters in a separate phylogenetic group and possesses unique interactions that stabilize this oligomeric state. The thermal stability of this enzyme is mainly due to an unusually high number of intramolecular hydrogen bonds. Finally, this study provides a general analysis of the forces driving the oligomerization in Old Yellow Enzymes.
来自嗜铁菌属JA12菌株的老黄色酶（FOYE）对于一种从中温生物中分离出的酶而言，展现出不同寻常的热稳定性。我们测定了这种酶的晶体结构，并进行了生物信息学表征，以深入了解其热稳定性。该酶呈现出四聚体四级结构；然而，与其他四聚体同源物不同的是，它聚集在一个单独的系统发育组中，并具有稳定这种寡聚状态的独特相互作用。这种酶的热稳定性主要归因于分子内氢键数量异常之多。最后，本研究对驱动老黄色酶寡聚化的作用力进行了全面分析。
