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，并且通过催化存在于多种细胞底物阵列中的硫酯键的裂解而发挥广泛的重要生物学功能。硫酯酶根据其序列保守性，三级和四级结构，活性位点构型和底物特异性分为25个家族。硫酯酶的最新结构和功能表征已导致我们对控制酶活性及其各自细胞作用的调节机制的认识发生了重大变化。硫酯酶调节的最终信条变化包括对通过低聚作用进行的ATP和GDP介导的调节的机理见解，新的关键调节区的作用以及对TE4家族成员内保守的四级结构的新见解。