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
-
1.2.1.1
- s-hydroxymethylglutathione
- nad+
- dehydrogenases
- gfa
-
paracoccus
- methanol
- denitrificans
-
methylotrophic
- boidinii
Reaction
Synonyms
EC 1.2.1.1, Gfa, glutathione-dependent formaldehyde-activating enzyme
ECTree
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Metals Ions
Metals Ions on EC 4.4.1.22 - S-(hydroxymethyl)glutathione synthase
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Zn
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the enzyme has a new fold with two zinc-sulfur centers, one that is structural (zinc tetracoordinated) and one catalytic (zinc apparently tricoordinated). In the complex of enzyme with glutathione, the catalytic zinc is displaced due to disulfide bond formation of glutathione with one of the zinc-coordinating cysteines
Zn2+
required, the GFA domain contains two zinc binding sites, one zinc ion is coordinated by four cysteinyl thiols (C31, C33, C99 and C102) in a tetrahedral geometry, whereas the other zinc ion is coordinated by three cysteinyl thiols (C52, C54 and C57) in a trigonal planar geometry. GSH binding induces translocation of the second zinc ion. Manual model building of the catalytic zinc site