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Please use this identifier to cite or link to this item: http://ntour.ntou.edu.tw:8080/ir/handle/987654321/26994

Title: An enzyme possessing both glutathione-dependent formaldehyde dehydrogenase and S-nitrosoglutathione reductase from Antrodia camphorata
Authors: Chih-Yu Huang;Chuian-Fu Ken;Lisa Wen;Chi-Tsai Lin
Contributors: NTOU:Institute of Bioscience and Biotechnology
國立臺灣海洋大學:生物科技研究所
Keywords: Antrodia camphorata;Glutathione-dependent formaldehyde dehydrogenase (GFD or GSH-FDH);S-hydroxymethylglutathione (HMGSH);S-nitrosoglutathione (GSNO);S-nitrosoglutathione reductase (GSNOR)
Date: 2009-02-15
Issue Date: 2011-10-21T02:22:13Z
Publisher: Food Chemistry
Abstract: Abstract: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.
Relation: 112(4), pp.795–802
URI: http://ntour.ntou.edu.tw/handle/987654321/26994
Appears in Collections:[Department of Bioscience and Biotechnology ] Periodical Articles

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