编码小鼠硫嘌呤 S-甲基转移酶（TPMT）的 cDNA 的分子克隆及功能特性分析

Molecular cloning and functional characterization of the cDNA encoding the murine thiopurine S-methyltransferase (TPMT).

作者信息

Fessing M Y, Belkov V M, Krynetski E Y, Evans W E

机构信息

Department of Pharmaceutical Sciences, St. Jude Children's Research Hospital, Memphis, TN 38105, USA.

出版信息

FEBS Lett. 1998 Mar 13;424(3):143-5. doi: 10.1016/s0014-5793(98)00159-8.

DOI:10.1016/s0014-5793(98)00159-8

PMID:9539138

Abstract

Thiopurine S-methyltransferase (TPMT) is a cytosolic enzyme that catalyzes S-methylation of aromatic and heterocyclic sulfhydryl compounds, including anticancer and immunosuppressive thiopurines. Here we report the isolation and functional characterization of the murine TPMT cDNA. The screening of expressed sequence tags database led to isolation of a murine cDNA clone containing an uninterrupted ORF encoding the protein with an amino acid sequence that is 82% similar and 78% identical to the human TPMT. The expression product of the murine cDNA in rabbit reticulocyte and wheat germ lysate coupled transcription-translation systems showed TPMT enzymatic activity. We conclude that the isolated cDNA clone represents the murine TPMT cDNA.

摘要

硫嘌呤 S-甲基转移酶（TPMT）是一种胞质酶，可催化芳香族和杂环巯基化合物的 S-甲基化反应，其中包括抗癌和免疫抑制性硫嘌呤。在此，我们报告了小鼠 TPMT cDNA 的分离及功能特性。对表达序列标签数据库的筛选导致分离出一个小鼠 cDNA 克隆，该克隆包含一个不间断的开放阅读框，编码的蛋白质氨基酸序列与人类 TPMT 的相似性为 82%，同一性为 78%。小鼠 cDNA 在兔网织红细胞和麦胚裂解物偶联转录-翻译系统中的表达产物显示出 TPMT 酶活性。我们得出结论，分离出的 cDNA 克隆代表小鼠 TPMT cDNA。