National Changhua University of Education Institutional Repository : Item 987654321/16778
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题名: An Enzyme Possessing Both Glutathione-dependent Formaldehyde Dehydrogenase and S-nitrosoglutathione Reductase from Antrodia Camphorate
作者: Huang, Chih-Yu;Ken, Chuian-Fu;Wen, Lisa;Lin, Chi-Tsai
贡献者: 生物學系
关键词: Antrodia camphorata;Glutathione-dependent formaldehyde dehydrogenase (GFD or GSH-FDH);S-hydroxymethylglutathione (HMGSH);S-nitrosoglutathione (GSNO);S-nitrosoglutathione reductase (GSNOR)
日期: 2009-02
上传时间: 2013-06-05T08:48:20Z
出版者: Elsevier
摘要: Glutathione-dependent formaldehyde dehydrogenase (GFD or GSH-FDH) plays important roles in formaldehyde detoxification and antioxidation. A gene encoding GFD from Antrodia camphorata was identified based on sequence homology. The deduced amino acid sequence of 378 amino acid residues is conserved among the reported GFDs. To characterise the Ac-GFD, the coding region was subcloned into a vector pET-20b(+) and transformed into Escherichia coli. The recombinant GFD was expressed and purified by Ni2+-nitrilotriacetic acid Sepharose. This purified enzyme showed a single band on a 10% SDS–PAGE. The enzyme retained 50% GFD activity after heating at 50 °C for 5 min. The enzyme is bifunctional. In addition to the GFD activity, it also functions as an effective S-nitrosoglutathione reductase (GSNOR) presumably to safeguard against nitrosative stress. The Km values for S-hydroxymethylglutathione and S-nitrosoglutathione were 1.20 and 0.28 mM, respectively.
關聯: Food Chemistry, 112(4): 795-802
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