4.4.1.22: S-(hydroxymethyl)glutathione synthase
This is an abbreviated version!
For detailed information about S-(hydroxymethyl)glutathione synthase, go to the full flat file.
Word Map on EC 4.4.1.22
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4.4.1.22
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1.2.1.1
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s-hydroxymethylglutathione
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nad+
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dehydrogenases
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gfa
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paracoccus
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methanol
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denitrificans
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methylotrophic
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boidinii
- 4.4.1.22
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1.2.1.1
- s-hydroxymethylglutathione
- nad+
- dehydrogenases
- gfa
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paracoccus
- methanol
- denitrificans
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methylotrophic
- boidinii
Reaction
Synonyms
EC 1.2.1.1, Gfa, glutathione-dependent formaldehyde-activating enzyme
ECTree
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General Information
General Information on EC 4.4.1.22 - S-(hydroxymethyl)glutathione synthase
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physiological function
additional information
GFA binds glutathione but does not directly catalyse S-hydroxymethylglutathione formation under standard conditions. Instead, it may be a glutathione carrier that acts to colocalise glutathione and formaldehyde in a cellular context
physiological function
the enzyme glutathione-dependent formaldehyde-activating enzyme (GFA) from Paracoccus denitrificans catalyzes S-hydroxymethylglutathione (HMG) formation from glutathione and formaldehyde. HMG may then be oxidised by an alcohol dehydrogenase to form S-formylglutathione, which is further metabolised by S-formylglutathione hydrolase to give formate, thus returning GSH to the cellular pool. Enzyme GFA binds glutathione but does not directly catalyse HMG formation under standard conditions. It is possible that GFA acts as a glutathione carrier that acts to co-localise glutathione and formaldehyde in a cellular context
GFA catalysis is proposed to proceed via a highly unusual mechanism involving translocation of this second zinc ion to another undefined site on the protein. HMG formation is then catalysed at this site before the zinc ion returns to the trigonal planar site after catalysis
additional information
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GFA catalysis is proposed to proceed via a highly unusual mechanism involving translocation of this second zinc ion to another undefined site on the protein. HMG formation is then catalysed at this site before the zinc ion returns to the trigonal planar site after catalysis