Enzymes
UniProtKB help_outline | 1,992 proteins |
Enzyme class help_outline |
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Reaction participants Show >> << Hide
- Name help_outline S-(hydroxymethyl)glutathione Identifier CHEBI:58758 Charge -1 Formula C11H18N3O7S InChIKeyhelp_outline PIUSLWSYOYFRFR-BQBZGAKWSA-M SMILEShelp_outline [NH3+][C@@H](CCC(=O)N[C@@H](CSCO)C(=O)NCC([O-])=O)C([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 3 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline glutathione Identifier CHEBI:57925 Charge -1 Formula C10H16N3O6S InChIKeyhelp_outline RWSXRVCMGQZWBV-WDSKDSINSA-M SMILEShelp_outline [NH3+][C@@H](CCC(=O)N[C@@H](CS)C(=O)NCC(=O)[O-])C(=O)[O-] 2D coordinates Mol file for the small molecule Search links Involved in 104 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline formaldehyde Identifier CHEBI:16842 (CAS: 50-00-0) help_outline Charge 0 Formula CH2O InChIKeyhelp_outline WSFSSNUMVMOOMR-UHFFFAOYSA-N SMILEShelp_outline [H]C([H])=O 2D coordinates Mol file for the small molecule Search links Involved in 141 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
RHEA:22488 | RHEA:22489 | RHEA:22490 | RHEA:22491 | |
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Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
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Publications
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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.H., Griesinger C., Vorholt J.A.
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 ac ... >> More
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. << Less
Comments
This reaction possibly occur spontaneously.