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  A glutathione-dependent formaldehyde-activating enzyme (Gfa) from Paracoccus denitrificans detected and purified via two- dimensional proton exchange NMR spectroscopy

Goenrich, M., Bartoschek, S., Hagemeier, C., Griesinger, C., & Vorholt, J. (2002). A glutathione-dependent formaldehyde-activating enzyme (Gfa) from Paracoccus denitrificans detected and purified via two- dimensional proton exchange NMR spectroscopy. Journal of Biological Chemistry, 277(5), 3069-3072. Retrieved from http://www.jbc.org/content/277/5/3069.full.pdf+html.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0012-F447-8 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0028-E0D3-C
Genre: Journal Article

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599694.pdf (Publisher version), 602KB
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Goenrich, M., Author
Bartoschek, S., Author
Hagemeier, C., Author
Griesinger, C.1, Author              
Vorholt, J., Author
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1Department of NMR Based Structural Biology, MPI for biophysical chemistry, Max Planck Society, ou_578567              

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 Abstract: The formation of S-hydroxymethylglutathione from formaldehyde and glutathione is a central reaction in the consumption of the cytotoxin formaldehyde in some methylotrophic bacteria as well as in many other organisms. We describe here the discovery of an enzyme from Paracoccus denitrificans that accelerates this spontaneous condensation reaction. The rates of S- hydroxymethylglutathione formation and cleavage were determined under equilibrium conditions via two-dimensional proton exchange NMR spectroscopy. The pseudo first order rate constants k(1)* were estimated from the temperature dependence of the reaction and the signal to noise ratio of the uncatalyzed reaction. At 303 K and pH 6.0 k(1)* was found to be 0.02 s(-1) for the spontaneous reaction. A 10-fold increase of the rate constant was observed upon addition of cell extract from P. denitrificans grown in the presence of methanol corresponding to a specific activity of 35 units mg(-1). Extracts of cells grown in the presence of succinate revealed a lower specific activity of 11 units mg(-1). The enzyme catalyzing the conversion of formaldehyde and glutathione was purified and named glutathione-dependent formaldehyde- activating enzyme (Gfa). The gene gfa is located directly upstream of the gene for glutathione-dependent formaldehyde dehydrogenase, which catalyzes the subsequent oxidation of S- hydroxymethylglutathione. Putative proteins with sequence identity to Gfa from P. denitrificans are present also in Rhodobacter sphaeroides, Sinorhizobium meliloti, and Mesorhizobium loti.

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Language(s): eng - English
 Dates: 2002-02-01
 Publication Status: Published in print
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 Rev. Method: Peer
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Title: Journal of Biological Chemistry
Source Genre: Journal
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Pages: - Volume / Issue: 277 (5) Sequence Number: - Start / End Page: 3069 - 3072 Identifier: -