期刊
FEBS LETTERS
卷 470, 期 2, 页码 97-101出版社
ELSEVIER SCIENCE BV
DOI: 10.1016/S0014-5793(00)01299-0
关键词
phytosulfokine-alpha; tyrosine O-sulfation; tyrosylprotein sulfotransferase
An in vitro assay system to detect tyrosylprotein sulfotransferase (TPST) activity of higher plant cells was established, using synthetic oligopeptides based on the deduced amino acid sequence of a phytosulfokine-alpha (PSB-alpha) precursor, TPST activity nas found in microsomal membrane fractions of rice, asparagus and carrot cells and it was confirmed that acidic amino acid residues adjacent to the tyrosine residues of acceptor peptides were essential to the sulfation reaction. The asparagus TEST exhibited a broad pH optimum of 7.0-8.5, required manganese ions for maximal activity and appeared to be a membrane-bound protein localized in the Golgi apparatus. These enzymes should be defined as a new class of plant sulfotransferases that catalyze tyrosine O-sulfation of a PSK-alpha precursor and other unknown proteins. (C) 2000 Federation of European Biochemical Societies.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据