"Enzymogenesis": classical liver alcohol dehydrogenase origin from the glutathione-dependent formaldehyde dehydrogenase line.
نویسندگان
چکیده
منابع مشابه
Function, Expression and Polymorphism of Human Alcohol Dehydrogenase 3/Glutathione- Dependent Formaldehyde Dehydrogenase
Alcohol dehydrogenase 3 (ADH3), identical to glutathione-dependent formaldehyde dehydrogenase, plays a vital role in the defense against formaldehyde through the activity for the spontaneously formed adduct between formaldehyde and glutathione, Shydroxymethylglutathione (HMGSH). ADH3 may also participate in the metabolism of S-nitrosylated glutathione, GSNO. To further investigate substrate enz...
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The results obtained led the authors to the suggestion that Reactions 2 and 4 are catalyzed by liver alcohol dehydrogenase but that Reaction 1 is due to an aldehyde dehydrogenase present in their liver preparation. Because of the inhomogeneity of the enzyme preparation employed, a reinvestigation of this problem with more highly purified enzyme was suggested. With the use of crystalline horse l...
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The ADH2 gene codes for the Arabidopsis glutathione-dependent formaldehyde dehydrogenase (FALDH), an enzyme involved in formaldehyde metabolism in eukaryotes. In the present work, we have investigated the potential role of FALDH in detoxification of exogenous formaldehyde. We have generated a yeast (Saccharomyces cerevisiae) mutant strain (sfa1Delta) by in vivo deletion of the SFA1 gene that co...
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In the course of studies of formaldehyde metabolism in yeast (I), an enzyme was found that catalyzed the oxidation of formaldehyde in the presence of glutathione and diphosphopyridine nucleotide. A similar enzyme was discovered independently by Strittmatter and Ball in liver (2). This paper describes the partial purification and some of the properties of yeast formaldehyde dehydrogenase. Some e...
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The quenching of liver alcohol dehydrogenase protein fluorescence at alkaline pH indicates two conformational states of the enzyme with a pK,, of 9.8 -t0.2, shifted to 10.6 f 0.2 in I&O. NAD’ and 2-p-toluidinonaphthalene-6-sulfonate, a fluorescent probe competitive with coenzyme, bind to the acid conformation of the enzyme. The pK,, of the proteinfluorescence quenching curve is shifted toward 7...
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ژورنال
عنوان ژورنال: Proceedings of the National Academy of Sciences
سال: 1992
ISSN: 0027-8424,1091-6490
DOI: 10.1073/pnas.89.19.9247