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Information on EC 1.1.1.284 - S-(hydroxymethyl)glutathione dehydrogenase and Organism(s) Drosophila melanogaster

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EC Tree
IUBMB Comments
The substrate, S-(hydroxymethyl)glutathione, forms spontaneously from glutathione and formaldehyde; its rate of formation is increased in some bacteria by the presence of EC 4.4.1.22, S-(hydroxymethyl)glutathione synthase. This enzyme forms part of the pathway that detoxifies formaldehyde, since the product is hydrolysed by EC 3.1.2.12, S-formylglutathione hydrolase. The human enzyme belongs to the family of zinc-dependent alcohol dehydrogenases. Also specifically reduces S-nitrosylglutathione.
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This record set is specific for:
Drosophila melanogaster
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Word Map
The taxonomic range for the selected organisms is: Drosophila melanogaster
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
nitroreductase, gsnor, s-nitrosoglutathione reductase, gsno reductase, gsnor1, adh iii, gsno-r, alcohol dehydrogenase class iii, slgsnor, formic dehydrogenase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
alcohol dehydrogenase 3
-
-
Alcohol dehydrogenase SFA
-
-
-
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dehydrogenase, formaldehyde
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-
-
-
FALDH
-
-
-
-
FLD
-
-
-
-
formaldehyde dehydrogenase
formic dehydrogenase
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GD-FAlDH
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-
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GSNO reductase
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NAD-linked formaldehyde dehydrogenase
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-
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S-nitrosoglutathione reductase
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-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
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-
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redox reaction
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-
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reduction
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-
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SYSTEMATIC NAME
IUBMB Comments
S-(hydroxymethyl)glutathione:NAD+ oxidoreductase
The substrate, S-(hydroxymethyl)glutathione, forms spontaneously from glutathione and formaldehyde; its rate of formation is increased in some bacteria by the presence of EC 4.4.1.22, S-(hydroxymethyl)glutathione synthase. This enzyme forms part of the pathway that detoxifies formaldehyde, since the product is hydrolysed by EC 3.1.2.12, S-formylglutathione hydrolase. The human enzyme belongs to the family of zinc-dependent alcohol dehydrogenases. Also specifically reduces S-nitrosylglutathione.
CAS REGISTRY NUMBER
COMMENTARY hide
9028-84-6
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
formaldehyde + glutathione + NAD+
S-formylglutathione + NADH + H+
show the reaction diagram
formaldehyde + S-hydroxymethyl glutathione + NAD+
?
show the reaction diagram
-
-
-
-
?
S-nitrosoglutathione + NADH
? + NAD+
show the reaction diagram
-
-
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
S-nitrosoglutathione + NADH
? + NAD+
show the reaction diagram
-
-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.006
S-hydroxymethyl glutathione
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
16
S-hydroxymethyl glutathione
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-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
GSNOR is the sole alcohol dehydrogenase isozyme in vertebrate brains
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
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overexpression of the fdh in the central nervous system significantly increases GSNOR activity and induces visual pattern memory defects of Drosophila melanogaster. Overexpression of the fdh in the fan-shaped body induces memory defect, while overexpression in the mushroom body does not. The visual pattern memory defect can be rescued by co-expression with exogenous cGMP-dependent protein kinase
physiological function
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
ADHX_DROME
379
0
40389
Swiss-Prot
other Location (Reliability: 2)
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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overexpression of the fdh in the central nervous system significantly increases GSNOR activity and induces visual pattern memory defects of Drosophila melanogaster, Overexpression of fdh results in NO imbalance, thereby affecting the NO-cGMPPKG pathway and protein S-nitrosation and, ultimately, learning and memory function, regulation of protein S-nitrosation by fdh in transgenic flies, overview. elav-Gal4 driven pan-neuronal GSNOR and PKG co-expression flies restore normal memory performance completely
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
characterization of the DNA sequence of the gfd/odh genomic region containing the gene which encodes glutathione-dependent formaldehyde dehydrogenase
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overexpression of the fdh in the central nervous system of transgenic Drosophila melanogaster
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Fernandez, M.R.; Biosca, J.A.; Martinez, M.C.; Achkor, H.; Farres, J.; Pares, X.
Formaldehyde dehydrogenase from yeast and plant: implications for the general functional and structural significance of class III alcohol dehydrogenase
Adv. Exp. Med. Biol.
414
373-381
1997
Arabidopsis thaliana, Saccharomyces cerevisiae, Drosophila melanogaster, Escherichia coli, Homo sapiens, Pisum sativum, Rattus norvegicus
Manually annotated by BRENDA team
Luque, T.; Atrian, S.; Danielsson, O.; Jornvall, H.; Gonzalez-Duarte, R.
Structure of the Drosophila melanogaster glutathione-dependent formaldehyde dehydrogenase/octanol dehydrogenase gene (class III alcohol dehydrogenase). Evolutionary pathway of the alcohol dehydrogenase genes
Eur. J. Biochem.
225
985-993
1994
Drosophila melanogaster
Manually annotated by BRENDA team
Staab, C.A.; Hellgren, M.; Hoeoeg, J.O.
Medium- and short-chain dehydrogenase/reductase gene and protein families: Dual functions of alcohol dehydrogenase 3: implications with focus on formaldehyde dehydrogenase and S-nitrosoglutathione reductase activities
Cell. Mol. Life Sci.
65
3950-3960
2008
Arabidopsis thaliana, Branchiostoma lanceolatum, Ciona intestinalis, Drosophila melanogaster, Escherichia coli, Homo sapiens, Mus musculus
Manually annotated by BRENDA team
Hou, Q.; Jiang, H.; Zhang, X.; Guo, C.; Huang, B.; Wang, P.; Wang, T.; Wu, K.; Li, J.; Gong, Z.; Du, L.; Liu, Y.; Liu, L.; Chen, C.
Nitric oxide metabolism controlled by formaldehyde dehydrogenase (fdh, homolog of mammalian GSNOR) plays a crucial role in visual pattern memory in Drosophila
Nitric Oxide
24
17-24
2011
Drosophila melanogaster
Manually annotated by BRENDA team