Purification of formaldehyde and formate dehydrogenases from pea seeds by affinity chromatography and S-formylglutathione as the intermediate of formaldehyde metabolism

Uotila, Lasse; Koivusalo, Martti

doi:10.1016/0003-9861(79)90548-4

Cited by 83 publications

(60 citation statements)

References 32 publications

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“…Plant FALDHs have been isolated from pea seeds (Uotila and Koivusalo, 1979;Shafqat et al, 1996), Arabidopsis (Martínez et al, 1996), and maize (Zea mays; Wippermann et al, 1999). Their molecular and kinetic properties are remarkably similar to those found in the homolog enzymes from mammals, invertebrates, and microorganisms, providing evidence of the high degree of structural and functional conservation through evolution.…”

Section: Discussionmentioning

confidence: 92%

Enhanced Formaldehyde Detoxification by Overexpression of Glutathione-Dependent Formaldehyde Dehydrogenase from Arabidopsis

et al. 2003

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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 (sfa1⌬) by in vivo deletion of the SFA1 gene that codes for the endogenous FALDH. Overexpression of Arabidopsis FALDH in this mutant confers high resistance to formaldehyde added exogenously, which demonstrates the functional conservation of the enzyme through evolution and supports its essential role in formaldehyde metabolism. To investigate the role of the enzyme in plants, we have generated Arabidopsis transgenic lines with modified levels of FALDH. Plants overexpressing the enzyme show a 25% increase in their efficiency to take up exogenous formaldehyde, whereas plants with reduced levels of FALDH (due to either a cosuppression phenotype or to the expression of an antisense construct) show a marked slower rate and reduced ability for formaldehyde detoxification as compared with the wild-type Arabidopsis. These results show that the capacity to take up and detoxify high concentrations of formaldehyde is proportionally related to the FALDH activity in the plant, revealing the essential role of this enzyme in formaldehyde detoxification.

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Section: Discussionmentioning

confidence: 92%

Enhanced Formaldehyde Detoxification by Overexpression of Glutathione-Dependent Formaldehyde Dehydrogenase from Arabidopsis

et al. 2003

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“…FDH activity was visualized on non-denaturing polyacrylamide gels following the method of Uotila and Koivusalo (1979). The size and purity of the protein were assessed by running a sample on an sodium dodecyl-sulfatepolyacrylamide gel, and the purified protein was then incubated in darkness for 30 min at room temperature in the following solution: 100 mM sodium P-buffer, pH 7.0, 50 mM substrate, 0.8 mM NAD + , 0.03 mg mL 21 phenazine methosulfate, and 0.4 mg mL 21 NBT.…”

Section: Determination Of Fdh Enzyme Activitymentioning

confidence: 99%

A Formate Dehydrogenase Confers Tolerance to Aluminum and Low pH

et al. 2016

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Formate dehydrogenase (FDH) is involved in various higher plant abiotic stress responses. Here, we investigated the role of rice bean (Vigna umbellata) VuFDH in Al and low pH (H + ) tolerance. Screening of various potential substrates for the VuFDH protein demonstrated that it functions as a formate dehydrogenase. Quantitative reverse transcription-PCR and histochemical analysis showed that the expression of VuFDH is induced in rice bean root tips by Al or H + stresses. Fluorescence microscopic observation of VuFDH-GFP in transgenic Arabidopsis plants indicated that VuFDH is localized in the mitochondria. Accumulation of formate is induced by Al and H + stress in rice bean root tips, and exogenous application of formate increases internal formate content that results in the inhibition of root elongation and induction of VuFDH expression, suggesting that formate accumulation is involved in both H + -and Al-induced root growth inhibition. Over-expression of VuFDH in tobacco (Nicotiana tabacum) results in decreased sensitivity to Al and H + stress due to less production of formate in the transgenic tobacco lines under Al and H + stresses. Moreover, NtMATE and NtALS3 expression showed no changes versus wild type in these over-expression lines, suggesting that herein known Al-resistant mechanisms are not involved. Thus, the increased Al tolerance of VuFDH over-expression lines is likely attributable to their decreased Al-induced formate production. Taken together, our findings advance understanding of higher plant Al toxicity mechanisms, and suggest a possible new route toward the improvement of plant performance in acidic soils, where Al toxicity and H + stress coexist.

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“…Giese et al (1994) recently published a study on the characterization of the FDH of this species. The standard FDH assay does not discriminate between GSH-dependent and GSH-independent FDH (Uotila & Koivusalo, 1979, 1983. The apparent V max values (nkat mg −" protein) were 0.328 for E. aureum, 0.742 for F. benjamina and 0.543 for C. comosum.…”

Section: Enzymes Related To Formaldehyde Metabolismmentioning

confidence: 99%

Assimilation and metabolism of formaldehyde by leaves appear unlikely to be of value for indoor air purification

2000

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Uptake, translocation and metabolism of "%C-labelled formaldehyde in the leaves of Epipremnum aureum (Golden Potho) and Ficus benjamina (Weeping Fig) were investigated. Plants were exposed in light and dark to "%C-formaldehyde (500 µg m −$ ) in gas exposure chambers. The amount of "%C-incorporation into the soluble (waterextractable) and insoluble fractions of leaves, stem sections and roots was determined. The soluble "%C-activity was fractionated by ion exchange chromatography followed by thin-layer chromatography\autoradiography. Approximately 60-70% of the applied "%C-formaldehyde was recovered from the plants. In the light about five times more "%C-formaldehyde was assimilated than in the dark. The amount of "%C-label derived from "%C-formaldehyde, which was incorporated into acid-stable metabolites, was enhanced to an even larger extent in the light. The "%C-activity pattern closely resembled the general labelling spectrum of photosynthates, obtained after a "%CO # exposure. A substantial amount of labelled material, mostly sucrose, was translocated into the stems and roots. Our results suggest that in the light "%C enters the Calvin cycle after an enzymatic two-step oxidation process of "%C-formaldehyde to "%CO # . The activities of the respective enzymes, formaldehyde dehydrogenase and formate dehydrogenase, were determined. Among 27 ' leafy ' indoor decorative plants, a screening experiment revealed no outstanding species with regard to its capacity for metabolism of formaldehyde, and rate of uptake through stomata was too low to justify claims that plants contribute usefully to indoor air purification.

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Purification of formaldehyde and formate dehydrogenases from pea seeds by affinity chromatography and S-formylglutathione as the intermediate of formaldehyde metabolism

Cited by 83 publications

References 32 publications

Enhanced Formaldehyde Detoxification by Overexpression of Glutathione-Dependent Formaldehyde Dehydrogenase from Arabidopsis

Enhanced Formaldehyde Detoxification by Overexpression of Glutathione-Dependent Formaldehyde Dehydrogenase from Arabidopsis

A Formate Dehydrogenase Confers Tolerance to Aluminum and Low pH

Assimilation and metabolism of formaldehyde by leaves appear unlikely to be of value for indoor air purification

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