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Formaldehyde dehydrogenase homolog1

glutathione-dependent formaldehyde dehydrogenase
Top mentioned proteins: ACID, CAN, V1a, STEP, Alcohol Dehydrogenase
Papers on glutathione-dependent formaldehyde dehydrogenase
Four Components of the Conjugated Redox System in Organisms: Carbon, Nitrogen, Sulfur, Oxygen.
Ivanenko et al., Zug, Switzerland. In Biochemistry (mosc), Sep 2015
The central regulatory role in this redox system belongs to glutathione-dependent formaldehyde dehydrogenase, which controls FA binding with tetrahydrofolic acid, arginine methylation, and denitrosation of sulfhydryl groups.
Isolation and characterization of formaldehyde-degrading fungi and its formaldehyde metabolism.
Guo et al., Harbin, China. In Environ Sci Pollut Res Int, 2014
Quantitative real-time PCR analyses and enzyme activity analyses demonstrated that glutathione-dependent formaldehyde dehydrogenase (GDFADH) and formate dehydrogenase (FDH) pathway may play a functional role in enhancing formaldehyde-degrading capability in SGFA1.
Modulation of nitrosative stress via glutathione-dependent formaldehyde dehydrogenase and S-nitrosoglutathione reductase.
Lin et al., Taiwan. In Int J Mol Sci, 2013
Glutathione-dependent formaldehyde dehydrogenase (GFD) from Taiwanofungus camphorata plays important roles in formaldehyde detoxification and antioxidation.
Biostimulation by methanol enables the methylotrophic yeasts Hansenula polymorpha and Trichosporon sp. to reveal high formaldehyde biodegradation potential as well as to adapt to this toxic pollutant.
Heipieper et al., Kraków, Poland. In Appl Microbiol Biotechnol, 2013
Upon growth on either of the above substrates, the strains proved to produce the activity of glutathione-dependent formaldehyde dehydrogenase-the enzyme known to control the biooxidative step of Fd detoxification.
Analysis of Taiwan patents for the medicinal mushroom "Niu-Chang- Chih".
Yuan et al., Taiwan. In Recent Pat Food Nutr Agric, 2013
Newly identified functional proteins include a glutathione-dependent formaldehyde dehydrogenase (GFD), a glycoprotein named ACA1, and a laccase.
Glutathione-dependent formaldehyde dehydrogenase (ADH3) and low km mitochondrial aldehyde dehydrogenase (ALDH2). New evidence for differential expression in the rat retina in response to oxidative stress.
Pinazo-Durán et al., Valencia, Spain. In Free Radic Res, 2012
METHODS: To test proper mechanisms involved in removing peroxidic aldehydes from the retina, in an attempt to understand long-lasting changes induced by LPO, the oxidative and antioxidant enzymatic activities, as well as the retinal distribution and activity of glutathione-dependent formaldehyde dehydrogenase (ADH3) and low km mitochondrial aldehyde dehydrogenase (ALDH2), were studied and compared with induced LPO sites in the adult rat retina.
Function of S-nitrosoglutathione reductase (GSNOR) in plant development and under biotic/abiotic stress.
Corpas et al., Granada, Spain. In Plant Signal Behav, 2011
During the last decade, it was established that the class III alcohol dehydrogenase (ADH3) enzyme, also known as glutathione-dependent formaldehyde dehydrogenase (FALDH; EC,
Mammalian alcohol dehydrogenases--a comparative investigation at gene and protein levels.
Ostberg et al., Stockholm, Sweden. In Chem Biol Interact, 2011
ADH3, also denoted glutathione-dependent formaldehyde dehydrogenase and S-nitrosoglutathione reductase, is identified as the last gene in the ADH transcriptional order, but several pseudogenes for ADH3 have been traced at other chromosomes.
Immobilized formaldehyde-metabolizing enzymes from Hansenula polymorpha for removal and control of airborne formaldehyde.
Gonchar et al., Jerusalem, Israel. In J Biotechnol, 2011
The process was monitored by a specially constructed enzymatic amperometric biosensor based on FA oxidation by NAD+ and glutathione-dependent formaldehyde dehydrogenase from the recombinant H. polymorpha Tf 11-6 strain.
The plant ADH gene family.
Strommer, Guelph, Canada. In Plant J, 2011
The probable origins of the enzyme from a simple β-coil and eventual emergence from a glutathione-dependent formaldehyde dehydrogenase have been well described.
A novel role of catalase in detoxification of peroxynitrite in S. cerevisiae.
Ghosh et al., Calcutta, India. In Biochem Biophys Res Commun, 2009
Yeast flavohemoglobin (YHB) and glutathione-dependent formaldehyde dehydrogenase (GS-FDH) confers resistance against nitric oxide and related reactive nitrogen species.
Reagentless amperometric formaldehyde-selective biosensors based on the recombinant yeast formaldehyde dehydrogenase.
Gonchar et al., L'viv, Ukraine. In Talanta, 2008
Novel formaldehyde-selective amperometric biosensors were developed based on NAD(+)- and glutathione-dependent formaldehyde dehydrogenase isolated from a gene-engineered strain of the methylotrophic yeast Hansenula polymorpha.
A metabolic enzyme for S-nitrosothiol conserved from bacteria to humans.
Stamler et al., United States. In Nature, 2001
Here we have purified a single activity from Escherichia coli, Saccharomyces cerevisiae and mouse macrophages that metabolizes S-nitrosoglutathione (GSNO), and show that it is the glutathione-dependent formaldehyde dehydrogenase.
Site-directed mutagenesis and enzyme properties of mammalian alcohol dehydrogenases correlated with their tissue distribution.
Danielsson et al., Stockholm, Sweden. In Exs, 1993
It is possible to correlate the glutathione-dependent formaldehyde dehydrogenase activity of class III alcohol dehydrogenase with an arginine at position 115.
The alcohol dehydrogenase system.
Jörnvall, Stockholm, Sweden. In Exs, 1993
Other classes of this family include the class II protein, the glutathione-dependent formaldehyde dehydrogenase (the class III enzyme), the stomach-expressed class IV form, and the recently defined class V protein.
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