Institute for Glycomics, Griffith University, Southport, Queensland 4222, Australia.
School of Chemistry and Molecular Biosciences, Institute for Molecular Bioscience, Australian Infectious Diseases Research Centre, University of Queensland, Brisbane, Queensland 4072, Australia.
Prog Lipid Res. 2020 Jul;79:101036. doi: 10.1016/j.plipres.2020.101036. Epub 2020 May 19.
Thioesterases are present in all living cells and perform a wide range of important biological functions by catalysing the cleavage of thioester bonds present in a diverse array of cellular substrates. Thioesterases are organised into 25 families based on their sequence conservation, tertiary and quaternary structure, active site configuration, and substrate specificity. Recent structural and functional characterisation of thioesterases has led to significant changes in our understanding of the regulatory mechanisms that govern enzyme activity and their respective cellular roles. The resulting dogma changes in thioesterase regulation include mechanistic insights into ATP and GDP-mediated regulation by oligomerisation, the role of new key regulatory regions, and new insights into a conserved quaternary structure within TE4 family members. Here we provide a current and comparative snapshot of our understanding of thioesterase structure, function, and regulation across the different thioesterase families.
硫酯酶存在于所有活细胞中，通过催化各种细胞底物中硫酯键的断裂，发挥广泛的重要生物学功能。根据序列保守性、三级和四级结构、活性位点构型和底物特异性，硫酯酶被组织成 25 个家族。最近对硫酯酶的结构和功能特征的研究，使我们对调节酶活性的调控机制及其各自的细胞作用有了重大的认识。由此导致的硫酯酶调控的教条变化包括：通过寡聚化实现 ATP 和 GDP 介导的调节的机制见解、新的关键调节区域的作用，以及对 TE4 家族成员中保守的四级结构的新见解。在这里，我们提供了对不同硫酯酶家族的硫酯酶结构、功能和调控的当前和比较性的快照。
