Takahashi Saki, Sakakibara Yoichi, Mishiro Emi, Kouriki Haruna, Nobe Rika, Kurogi Katsuhisa, Yasuda Shin, Liu Ming-Cheh, Suiko Masahito
Department of Biochemistry and Applied Biosciences, University of Miyazaki, 1-1, Gakuenkibanadai-Nishi, Miyazaki, Miyazaki 889-2192, Japan.
Biochem Biophys Res Commun. 2008 Oct 31;375(4):531-5. doi: 10.1016/j.bbrc.2008.08.051. Epub 2008 Aug 24.
By searching the GenBank database, we recently identified a novel mouse cytosolic sulfotransferase (SULT) cDNA (IMAGE Clone ID 679629) and a novel mouse SULT gene (LOC 215895). Sequence analysis revealed that both mouse SULTs belong to the cytosolic SULT3 gene family. The recombinant form of these two newly identified SULTs, designated SULT3A1 and SULT3A2, were expressed using the pGEX-4T-1 glutathione S-transferase fusion system and purified from transformed BL21 Escherichia coli cells. Both purified SULT3A1 and SULT3A2 exhibited strong amine N-sulfonating activities toward 1-naphthylamine among a variety of endogenous and xenobiotic compounds tested as substrates. Kinetic constants of the sulfation of 1-naphthylamine and 1-naphthol by these two enzymes were determined. Collectively, these results imply that these two amine-sulfonating SULT3s may play essential roles in the metabolism and detoxification of aromatic amine compounds in the body.
通过搜索GenBank数据库，我们最近鉴定出一种新的小鼠胞质磺基转移酶（SULT）cDNA（IMAGE克隆ID 679629）和一种新的小鼠SULT基因（LOC 215895）。序列分析表明，这两种小鼠SULT均属于胞质SULT3基因家族。这两种新鉴定的SULT的重组形式，命名为SULT3A1和SULT3A2，使用pGEX-4T-1谷胱甘肽S-转移酶融合系统进行表达，并从转化的BL21大肠杆菌细胞中纯化。在作为底物测试的多种内源性和外源性化合物中，纯化的SULT3A1和SULT3A2对1-萘胺均表现出强烈的胺N-磺化活性。测定了这两种酶对1-萘胺和1-萘酚硫酸化的动力学常数。总体而言，这些结果表明这两种胺磺化SULT3可能在体内芳香胺化合物的代谢和解毒中起重要作用。
