National Changhua University of Education Institutional Repository : Item 987654321/16778

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NCUEIR > College of Science > Department of Biology > Periodical Articles > Item 987654321/16778

Please use this identifier to cite or link to this item: http://ir.ncue.edu.tw/ir/handle/987654321/16778

Title:	An Enzyme Possessing Both Glutathione-dependent Formaldehyde Dehydrogenase and S-nitrosoglutathione Reductase from Antrodia Camphorate
Authors:	Huang, Chih-Yu;Ken, Chuian-Fu;Wen, Lisa;Lin, Chi-Tsai
Contributors:	生物學系
Keywords:	Antrodia camphorata;Glutathione-dependent formaldehyde dehydrogenase (GFD or GSH-FDH);S-hydroxymethylglutathione (HMGSH);S-nitrosoglutathione (GSNO);S-nitrosoglutathione reductase (GSNOR)
Date:	2009-02
Issue Date:	2013-06-05T08:48:20Z
Publisher:	Elsevier
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:	Food Chemistry, 112(4): 795-802
Appears in Collections:	[Department of Biology] Periodical Articles

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