An engineered protease that cleaves specifically after sulfated tyrosine.-猫眼课题宝

一种工程蛋白酶，可特异性切割硫酸化酪氨酸。

DOI：

10.1002/anie.200800736

发表时间：

2008

期刊：

Angewandte Chemie (International ed. in English)

影响因子：

通讯作者：

中科院分区：

文献类型：

作者：

Varadarajan,Navin;Georgiou,George;Iverson,BrentL

Sulfated tyrosines are present in a wide array of proteins, such as G-protein-coupled receptors (GPCRs),[1] anticoagulation/coagulation factors,[2, 3] antibodies,[4] and bioactive peptides, such as phyllokinin, phytosulfokine, and cholecystokinin.[1] The post-translational addition of a sulfate group to tyrosine residues on peptides and proteins is catalyzed by membranebound tyrosylprotein sulfotransferases (TPSTs)[5] in the trans-Golgi network.[5] Sulfation occurs following protein translocation to the endoplasmic reticulum, and thus, there is spatial separation between the two common forms of post-translationally modified tyrosine residues, namely, phosphorylation in the cytosol, and sulfation in the extracellular space.[3]Although tyrosine-O-sulfation plays a critical role in protein–protein interactions, in cell function, and in certain disease states,[3] the elucidation of sulfation sites on proteins and peptides, and consequently the understanding of their function, is challenging.[1] There are no consensus sequences for tyrosine sulfation other than the presence of neighboring acidic residues. Furthermore, the sulfate group is hydrolyzed at low-pH conditions typically used for chemical analysis [6] and during analysis under positive/negative mode MS/MS.[7, 8]