Department of Microbiology and Immunology, College of Physicians and Surgeons, Columbia University, New York, NY 10032, USA.
Microbiol Mol Biol Rev. 2011 Mar;75(1):192-212. doi: 10.1128/MMBR.00042-10.
Genomic studies have revealed the presence of Ser/Thr kinases and phosphatases in many bacterial species, although their physiological roles have largely been unclear. Here we review bacterial Ser/Thr kinases (eSTKs) that show homology in their catalytic domains to eukaryotic Ser/Thr kinases and their partner phosphatases (eSTPs) that are homologous to eukaryotic phosphatases. We first discuss insights into the enzymatic mechanism of eSTK activation derived from structural studies on both the ligand-binding and catalytic domains. We then turn our attention to the identified substrates of eSTKs and eSTPs for a number of species and to the implications of these findings for understanding their physiological roles in these organisms.
基因组研究揭示了许多细菌物种中存在丝氨酸/苏氨酸激酶和磷酸酶，尽管它们的生理作用在很大程度上还不清楚。在这里，我们回顾了在催化结构域与真核丝氨酸/苏氨酸激酶具有同源性的细菌丝氨酸/苏氨酸激酶（eSTK）及其与真核磷酸酶具有同源性的磷酸酶伴侣（eSTP）。我们首先讨论了结构研究对 eSTK 激活的酶促机制的深入了解，这些结构研究涉及配体结合和催化结构域。然后，我们将注意力转向一些物种中已鉴定的 eSTKs 和 eSTPs 的底物，以及这些发现对理解它们在这些生物体中的生理作用的意义。
