Information on EC 4.4.1.22 - S-(hydroxymethyl)glutathione synthase

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The expected taxonomic range for this enzyme is: Paracoccus denitrificans

EC NUMBER
COMMENTARY hide
4.4.1.22
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RECOMMENDED NAME
GeneOntology No.
S-(hydroxymethyl)glutathione synthase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
S-(hydroxymethyl)glutathione = glutathione + formaldehyde
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
formaldehyde oxidation II (glutathione-dependent)
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Methane metabolism
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Microbial metabolism in diverse environments
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formaldehyde oxidation
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SYSTEMATIC NAME
IUBMB Comments
S-(hydroxymethyl)glutathione formaldehyde-lyase (glutathione-forming)
The enzyme from Paracoccus denitrificans accelerates the spontaneous reaction in which the adduct of formaldehyde and glutathione is formed, i.e. the substrate for EC 1.1.1.284, S-(hydroxymethyl)glutathione dehydrogenase, in the formaldehyde-detoxification pathway.
CAS REGISTRY NUMBER
COMMENTARY hide
425642-27-9
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
glutathione + formaldehyde
S-(hydroxymethyl)glutathione
show the reaction diagram
-
-
-
-
?
S-(hydroxymethyl)glutathione
glutathione + formaldehyde
show the reaction diagram
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
S-(hydroxymethyl)glutathione
glutathione + formaldehyde
show the reaction diagram
-
the enzyme accelerates the spontaneous reaction in which the adduct of formaldehyde and glutathione is formed, i.e. the substrate for EC 1.1.1.284, S-(hydroxymethyl)glutathione dehydrogenase, in the formaldehyde-detoxification pathway
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-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
21000
-
x * 21000, SDS-PAGE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
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x * 21000, SDS-PAGE
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
vapor diffusion method, crystallization of enzyme and enzyme in complex with glutathione
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Show AA Sequence (808 entries)
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