School of Chemistry and Astbury Centre for Structural Molecular Biology, University of Leeds, Leeds LS2 9JT, UK.
Biochem Soc Trans. 2013 Aug;41(4):1072-7. doi: 10.1042/BST20130071.
Phosphorylation is a ubiquitous protein post-translational modification, and the importance of phosphorylation of serine, threonine and tyrosine is well established. What is lesser known is that almost all heteroatom-containing amino acids can be phosphorylated and, among these, histidine, aspartate and cysteine have well established roles in bacterial signalling pathways. The first of these, phosphohistidine, is the most unusual in that it is labile under many conditions used to study proteins in vitro and can exist as two different isomers. In the present short review, we highlight the chemical challenges that this modification presents and the manner in which chemical synthesis has been used to identify and mimic the modification in proteins.
磷酸化是一种普遍存在的蛋白质翻译后修饰，丝氨酸、苏氨酸和酪氨酸的磷酸化的重要性已得到充分证实。但不为人知的是，几乎所有含杂原子的氨基酸都可以被磷酸化，其中组氨酸、天冬氨酸和半胱氨酸在细菌信号通路中具有明确的作用。其中，磷酸组氨酸是最不寻常的，因为它在许多用于体外研究蛋白质的条件下不稳定，并且可以以两种不同的异构体存在。在本次简短的综述中，我们重点介绍了这种修饰所带来的化学挑战，以及化学合成在鉴定和模拟蛋白质中的这种修饰方面的应用。
