Purification, characterization, and partial sequence of the glutathione-dependent formaldehyde dehydrogenase from Escherichia coli: a class III alcohol dehydrogenase

Biochemistry ◽  
1992 ◽  
Vol 31 (2) ◽  
pp. 475-481 ◽  
Author(s):  
William G. Gutheil ◽  
Barton Holmquist ◽  
Bert L. Vallee
Keyword(s):  
Escherichia Coli ◽  
Alcohol Dehydrogenase ◽  
Partial Sequence ◽  
Formaldehyde Dehydrogenase ◽  
Class Iii

Human class III alcohol dehydrogenase/glutathione-dependent formaldehyde dehydrogenase

1991 ◽  
Vol 10 (1) ◽  
pp. 69-73 ◽  
Author(s):  
Rudolf Kaiser ◽  
Barton Holmquist ◽  
Bert L. Vallee ◽  
Hans J�rnvall
Keyword(s):  
Alcohol Dehydrogenase ◽  
Formaldehyde Dehydrogenase ◽  
Class Iii ◽  
Human Class

Structure–function relationships in human Class III alcohol dehydrogenase (formaldehyde dehydrogenase)

2003 ◽  
Vol 143-144 ◽  
pp. 195-200 ◽  
Author(s):  
Paresh C. Sanghani ◽  
Howard Robinson ◽  
Riccardo Bennett-Lovsey ◽  
Thomas D. Hurley ◽  
W.F. Bosron
Keyword(s):  
Alcohol Dehydrogenase ◽  
Structure Function ◽  
Formaldehyde Dehydrogenase ◽  
Class Iii ◽  
Human Class

scholarly journals Plasmid-mediated formaldehyde resistance in Escherichia coli: characterization of resistance gene.

1996 ◽  
Vol 40 (10) ◽  
pp. 2276-2279 ◽  
Author(s):  
N Kümmerle ◽  
H H Feucht ◽  
P M Kaulfers
Keyword(s):  
Escherichia Coli ◽  
Resistance Gene ◽  
Resistant Strain ◽  
Resistance Mechanism ◽  
Resistance Mechanisms ◽  
Formaldehyde Dehydrogenase ◽  
Class Iii ◽  
Vitro Assay ◽  
Reading Frame

The formaldehyde resistance mechanisms in the formaldehyde-resistant strain Escherichia coli VU3695 were investigated. A large (4.6-kb) plasmid DNA fragment encompassing the formaldehyde resistance gene was sequenced. A single 1,107-bp open reading frame encoding a glutathione- and NAD-dependent formaldehyde dehydrogenase was identified and sequenced, and the enzyme was expressed in an in vitro assay and purified. Amino acid sequence homology studies showed 62.4 to 63.2% identity with class III alcohol dehydrogenases isolated from horse, human, and rat livers. We demonstrated that the resistance mechanism in the formaldehyde-resistant strain E. coli VU3695 and in other formaldehyde-resistant members of the family Enterobacteriaceae is based on the enzymatic degradation of formaldehyde by a formaldehyde dehydrogenase.

Immunocytochemical and biochemical demonstration of formaldhyde dehydrogenase (class III alcohol dehydrogenase) in the nucleus.

1992 ◽  
Vol 40 (12) ◽  
pp. 1865-1878 ◽  
Author(s):  
F J Iborra ◽  
J Renau-Piqueras ◽  
M Portoles ◽  
M D Boleda ◽  
C Guerri ◽  
...  
Keyword(s):  
Alcohol Dehydrogenase ◽  
Gold Particle ◽  
Cell Function ◽  
Particle Density ◽  
Rat Hepatocytes ◽  
Cell Types ◽  
Ethanol Metabolism ◽  
Significant Activity ◽  
Formaldehyde Dehydrogenase ◽  
Class Iii

Alcohol dehydrogenase (ADH), the major enzyme catalyzing the biological oxidation of ethanol in mammals, includes four classes with very different capacities for ethanol oxidation. Class III ADH is present in all the tissues and is well conserved throughout evolution. This enzyme has a low activity with ethanol, is specific for the glutathione-dependent oxidation of formaldehyde, and is therefore a formaldehyde dehydrogenase (FALDH). Until now there have been few and conflicting studies concerning its intracellular distribution, which is important for the understanding of its role in cell function. In the present work we used biochemical and immunocytochemical methods to assess the distribution of FALDH in rat hepatocytes and astroglial cells. With the glutathione-dependent formaldehyde dehydrogenase assay, we found the highest activity in the cytosol of hepatocytes and brain cells (12 and 2.6 mU/mg protein, respectively), but nuclei also exhibited significant activity (1.16 and 2.1 mU/mg protein, respectively). The immunocytochemical results showed the presence of FALDH binding sites in both the cytoplasm and the nucleus of the different cell types studied. Whereas no specific gold particle labeling was seen associated with any cytoplasmic component, in the nucleus the particles were found mainly over condensed chromatin and interchromatin regions. Finally, the gold particle density over both the nucleus and cytoplasm was greater in differentiated than in proliferating astrocytes in primary culture. In contrast, class I ADH, primarily responsible for ethanol metabolism, was found only in the cytoplasm of hepatocytes. We propose that one of the functions of FALDH is to protect cell structures, including DNA, from the toxic effects of endogenous formaldehyde, which is an intermediate in many metabolic process.

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