ArticlePlant molecular biology1997
Maize glutathione-dependent formaldehyde dehydrogenase cDNA: a novel plant gene of detoxification.
Article in Plant molecular biology, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
10 citing papers in PubMed, 38 citations in OpenAlex.
- Article
- Conservation of ethanol fermentation and its regulation in land plants.Journal of experimental botany · 2019Article
- Isolation, sequencing, and heterologous expression of the Paecilomyces variotii gene encoding S-hydroxymethylglutathione dehydrogenase (fldA).Applied microbiology and biotechnology · 2015Article
- Article
- S-Nitrosoglutathione reductase (GSNOR) mediates the biosynthesis of jasmonic acid and ethylene induced by feeding of the insect herbivore Manduca sexta and is important for jasmonate-elicited responses in Nicotiana attenuata.Journal of experimental botany · 2011Article
- Function of S-nitrosoglutathione reductase (GSNOR) in plant development and under biotic/abiotic stress.Plant signaling & behavior · 2011Review
- Redox regulation of the NPR1-TGA1 system of Arabidopsis thaliana by nitric oxide.The Plant cell · 2010Article
- The molecular basis of shoot responses of maize seedlings to Trichoderma harzianum T22 inoculation of the root: a proteomic approach.Plant physiology · 2008Article
- Proteomic identification of S-nitrosylated proteins in Arabidopsis.Plant physiology · 2005Article
- Elevated atmospheric COThe New phytologist · 2002Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
We have previously shown that intact plants and cultured plant cells can metabolize and detoxify formaldehyde through the action of a glutathione-dependent formaldehyde dehydrogenase (FDH), followed by C-1 metabolism of the initial metabolite (formic acid). The cloning and heterologous expression of a cDNA for the glutathione-dependent formaldehyde dehydrogenase from Zea mays L. is now described. The functional expression of the maize cDNA in Escherichia coli proved that the cloned enzyme catalyses the NAD(+)- and glutathione (GSH)-dependent oxidation of formaldehyde. The deduced amino acid sequence of 41 kDa was on average 65% identical with class III alcohol dehydrogenase from animals and less than 60% identical with conventional plant alcohol dehydrogenases (ADH) utilizing ethanol. Genomic analysis suggested the existence of a single gene for this cDNA. Phylogenetic analysis supports the convergent evolution of ethanol-consuming ADHs in animals and plants from formaldehyde-detoxifying ancestors. The high structural conservation of present-day glutathione-dependent FDH in microorganisms, plants and animals is consistent with a universal importance of these detoxifying enzymes.
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Registered trials
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