文献类型：期刊文献

英文题名：Cloning and Characterization of Filamentous Fungal S-Nitrosoglutathione Reductase from Aspergillus nidulans

作者：Zhou, Yao[1];Zhou, Shengmin[1];Yu, Haijun[1];Li, Jingyi[1];Xia, Yang[1];Li, Baoyi[1];Wang, Xiaoli[1];Wang, Ping[1]

机构：[1]E China Univ Sci & Technol, Sch Biotechnol, Biomed Nanotechnol Ctr, State Key Lab Bioreactor Engn, Shanghai 200237, Peoples R China

年份：2016

卷号：26

期号：5

起止页码：928

外文期刊名：JOURNAL OF MICROBIOLOGY AND BIOTECHNOLOGY

收录：;WOS:【SCI-EXPANDED(收录号:WOS:000378761500014)】；

基金：This work was supported by the Major Programs of Ministry of Education of China, National Natural Science Foundation of China (21303050 and 31471659) and the National Special Fund for State Key Laboratory of Bioreactor Engineering (Grant No. 2060204).

语种：英文

外文关键词：S-Nitrosoglutathione reductase; nitrosation; denitrosation; nitric oxide; Aspergillus nidulans

摘要：S-Nitrosoglutathione reductase (GSNOR) metabolizes S-nitrosoglutathione (GSNO) and has been shown to play important roles in regulating cellular signaling and formulating host defense by modulating intracellular nitric oxide levels. The enzyme has been found in bacterial, yeast, mushroom, plant, and mammalian cells. However, to date, there is still no evidence of its occurrence in filamentous fungi. In this study, we cloned and investigated a GSNOR-like enzyme from the filamentous fungus Aspergillus nidulans. The enzyme occurred in native form as a homodimer and exhibited low thermal stability. GSNO was an ideal substrate for the enzyme. The apparent K-m and k(cat) values were 0.55 mM and 34,100 min(-1), respectively. Substrate binding sites and catalytic center amino acid residues based on those from known GSNORs were conserved in this enzyme, and the corresponding roles were verified using site-directed mutagenesis. Therefore, we demonstrated the presence of GSNOR in a filamentous fungus for the first time.