Zaruba M, Hilt D, Tennekoon G
Biochem Biophys Res Commun. 1985 Jun 14;129(2):522-9. doi: 10.1016/0006-291x(85)90183-4.
The mechanism of inhibition of rat brain cerebroside sulfotransferase (EC 2.8.2.11) by a series of triazine aromatic dyes was examined. These dyes are putative site-specific probes of the "dinucleotide fold". All of the dyes examined were competitive inhibitors of cerebroside sulfotransferase with respect to 3'-phosphoadenosine 5'-phosphosulfate (PAPS) binding. In addition, the binding of the dye, Congo Red, to the sulfotransferase was associated with a red shift in its absorption spectrum. Based on these results, it is suggested that rat brain cerebroside sulfotransferase contains a "dinucleotide fold" as a structural feature of the protein.
研究了一系列三嗪芳香族染料对大鼠脑硫苷脂硫酸转移酶（EC 2.8.2.11）的抑制机制。这些染料被认为是“二核苷酸折叠”的位点特异性探针。所有检测的染料都是硫苷脂硫酸转移酶相对于3'-磷酸腺苷5'-磷酸硫酸酯（PAPS）结合的竞争性抑制剂。此外，染料刚果红与硫酸转移酶的结合与其吸收光谱的红移有关。基于这些结果，提示大鼠脑硫苷脂硫酸转移酶含有“二核苷酸折叠”作为该蛋白质的结构特征。
