Cloning and characterisation of S-formylglutathione hydrolase from Arabidopsis thaliana: a pathway for formaldehyde detoxification

Haslam, Richard P.; Rust, S. R.; Pallett, Ken; Cole, David J.; Coleman, J. O. D.

doi:10.1016/s0981-9428(02)01378-5

Cited by 37 publications

(26 citation statements)

References 21 publications

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“…These findings go some way to explaining the strong similarity in substrate specificity exhibited by these enzymes and further support the idea, already suggested by several authors, 1,[7][8][9] that the FGH enzyme is part of an universal detoxification pathway shared by a variety of organisms.…”

Section: Structural Comparisonsupporting

confidence: 89%

“…3 Subsequently, FGHs were characterized in several organisms such as Paracoccus denitrificans, 1 Saccharomyces cerevisiae, 4 Candida boidinii, 5 Escherichia coli, 6,7 and Arabidopsis thaliana. 8,9 Regardless of their source, all these enzymes showed remarkable conservation in their sequence and were characterized by the presence of a conserved cysteine residue (generally in position 59), a conserved sequence motif (GHSMGG) containing the catalytic serine, which together with an aspartate and a histidine residue completed a serine hydrolase catalytic triad. Moreover, the functional characterization of these enzymes showed that they were not strictly specific to glutathione thioesters, but also showed significant hydrolytic activity against xenobiotic carboxylic esters including methylumbelliferyl acetate.…”

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confidence: 99%

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Crystal structure of an S‐formylglutathione hydrolase from Pseudoalteromonas haloplanktis TAC125

et al. 2010

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S-formylglutathione hydrolases (FGHs) constitute a family of ubiquitous enzymes which play a key role in formaldehyde detoxification both in prokaryotes and eukaryotes, catalyzing the hydrolysis of S-formylglutathione to formic acid and glutathione. While a large number of functional studies have been reported on these enzymes, few structural studies have so far been carried out. In this article we report on the functional and structural characterization of PhEst, a FGH isolated from the psychrophilic bacterium Pseudoalteromonas haloplanktis. According to our functional studies, this enzyme is able to efficiently hydrolyze several thioester substrates with very small acyl moieties. By contrast, the enzyme shows no activity toward substrates with bulky acyl groups. These data are in line with structural studies which highlight for this enzyme a very narrow acyl-binding pocket in a typical alpha/beta-hydrolase fold. PhEst represents the first cold-adapted FGH structurally characterized to date; comparison with its mesophilic counterparts of known three-dimensional structure allowed to obtain useful insights into molecular determinants responsible for the ability of this psychrophilic enzyme to work at low temperature.

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Section: Structural Comparisonsupporting

confidence: 89%

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confidence: 99%

Crystal structure of an S‐formylglutathione hydrolase from Pseudoalteromonas haloplanktis TAC125

et al. 2010

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“…Furthermore, the combined introduction of FALDH mediated formaldehyde metabolic pathway in addition to the bacterial ribulose monophosphate pathway may result in which are more practically applicable to formaldehyde detoxification. The genes for S-formylglutathione hydrolase and formate dehydrogenase have been cloned from Arabidopsis (Haslam et al 2002;Olson et al 2000). The production of transformants overexpressing these genes is in progress.…”

Section: Discussionmentioning

confidence: 99%

Glutathione-dependent formaldehyde dehydrogenase from golden pothos (Epipremnum aureum) and the production of formaldehyde detoxifying plants

Tada¹,

Kidu²

2011

Plant Biotechnology

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Glutathione-dependent formaldehyde dehydrogenase (FALDH) is an enzyme involved in formaldehyde metabolism in eukaryotes. FALDH cDNA was cloned from golden pothos, which is reported to effectively purify gaseous formaldehyde from enclosed room atmosphere. FALDH cDNAs from Arabidopsis, rice and golden pothos were overexpressed in transgenic Arabidopsis, and the enzyme activity was compared to determine the one most suitable for the molecular breeding of formaldehyde-detoxifying plants. The transgenic lines exhibited modified levels of the FALDH transcript, i.e. 10-800% compared to the endogenous transcript, due to either an overexpression or a cosuppression phenotype. The enzyme activity in the crude leaf extract was not proportionate, but did correlate with the transcription levels with certain exceptions. The FALDHs from the three plant species indicated similar enzymatic activity on average. The capacity to detoxify exogenous formaldehyde in the transformants with the FALDHs was determined at the whole plant level. Plants overexpressing FALDH from the three plant species displayed up to a 40% increase in their efficiency to take up exogenous formaldehyde as compared with the wild-type plants. On the other hand, no difference in the survival rate was observed among the transformants and wild type plants on formaldehyde-containing agar medium. These results show the FALDH from golden pothos to be similarly or more effective for detoxifying formaldehyde in transgenic plants compared with Arabidopsis and rice, and that this cDNA is applicable to the molecular breeding of formaldehyde detoxifying plants.Key words: Formaldehyde dehydrogenase (FALDH), golden pothos (Epipremnum aureum), sick house.Plant Biotechnology 28, 373-378 (2011) DOI: 10.5511/plantbiotechnology.11.0620a Original PaperAbbreviations: FALDH, formaldehyde dehydrogenase; RACE, rapid amplification of cDNA ends; RT, Real-time quantitative reverse transcriptase This article can be found at

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“…FGH was first purified from human liver and characterized by Uotila & Koivusalo (1974), and later it was found to be identical to human esterase D (Eiberg & Mohr, 1986). The FGH gene has also been cloned from a higher plant, Arabidopsis thaliana (Haslam et al, 2002). Two bacterial and yeast FGHencoding genes from microbial sources, a methylotrophic bacterium, Paracoccus denitrificans (fghA) (Harms et al, 1996), and a budding yeast, Saccharomyces cerevisiae (YJL068C) (Degrassi et al, 1999), have been characterized.…”

Section: Introductionmentioning

confidence: 99%

Physiological role of S-formylglutathione hydrolase in C1 metabolism of the methylotrophic yeast Candida boidinii

et al. 2003

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The methylotrophic yeast Candida boidinii exhibits S-formylglutathione hydrolase activity (FGH, EC 3.1.2.12), which is involved in the glutathione-dependent formaldehyde oxidation pathway during growth on methanol as the sole carbon source. The structural gene, FGH1, was cloned from C. boidinii, and its predicted amino acid sequence showed more than 60 % similarity to those of FGHs from Paracoccus denitrificans and Saccharomyces cerevisiae, and human esterase D. FGH from C. boidinii contained a C-terminal tripeptide, SKL, which is a type I peroxisometargeting signal, and a bimodal distribution of FGH between peroxisomes and the cytosol was demonstrated. The FGH1 gene was disrupted in the C. boidinii genome by one-step gene disruption. The fgh1D strain was still able to grow on methanol as a carbon source under methanollimited chemostat conditions with low dilution rates (D<0?05 h "1 ), conditions under which a strain with disruption of the gene for formaldehyde dehydrogenase (another enzyme involved in the formaldehyde oxidation pathway) could not survive. These results suggested that FGH is not essential but necessary for optimal growth on methanol. This is believed to be the first report of detailed analyses of the FGH1 gene in a methylotrophic yeast strain.

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Cloning and characterisation of S-formylglutathione hydrolase from Arabidopsis thaliana: a pathway for formaldehyde detoxification

Cited by 37 publications

References 21 publications

Crystal structure of an S‐formylglutathione hydrolase from Pseudoalteromonas haloplanktis TAC125

Crystal structure of an S‐formylglutathione hydrolase from Pseudoalteromonas haloplanktis TAC125

Glutathione-dependent formaldehyde dehydrogenase from golden pothos (Epipremnum aureum) and the production of formaldehyde detoxifying plants

Physiological role of S-formylglutathione hydrolase in C1 metabolism of the methylotrophic yeast Candida boidinii

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