Information on EC 1.8.1.16 - glutathione amide reductase

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The expected taxonomic range for this enzyme is: Marichromatium gracile

EC NUMBER
COMMENTARY hide
1.8.1.16
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RECOMMENDED NAME
GeneOntology No.
glutathione amide reductase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
2 glutathione amide + NAD+ = glutathione amide disulfide + NADH + H+
show the reaction diagram
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-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
glutathione amide metabolism
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SYSTEMATIC NAME
IUBMB Comments
glutathione amide:NAD+ oxidoreductase
A dimeric flavoprotein (FAD). The enzyme restores glutathione amide disulfide, which is produced during the reduction of peroxide by EC 1.11.1.17 (glutathione amide-dependent peroxidase), back to glutathione amide (it catalyses the reaction in the opposite direction to that shown). The enzyme belongs to the family of flavoprotein disulfide oxidoreductases, but unlike other members of the family, which are specific for NADPH, it prefers NADH [1].
CAS REGISTRY NUMBER
COMMENTARY hide
367279-42-3
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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 amide disulfide + NADH + H+
2 glutathione amide + NAD+
show the reaction diagram
glutathione amide disulfide + NADPH + H+
2 glutathione amide + NADP+
show the reaction diagram
glutathione disulfide + NADH + H+
2 glutathione + NAD+
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
glutathione amide disulfide + NADH + H+
2 glutathione amide + NAD+
show the reaction diagram
glutathione amide disulfide + NADPH + H+
2 glutathione amide + NADP+
show the reaction diagram
glutathione disulfide + NADH + H+
2 glutathione + NAD+
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NAD+
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the enzyme forms a dimer, with each monomer consisting of a FAD domain, a Rossmann fold NADH binding domain, and an interface domain
NADH
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preferred cofactor
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.097
glutathione amide disulfide
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pH 7.1, 25C
6.9
glutathione disulfide
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pH 7.1, 25C
0.0132
NADH
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pH 7.1, 25C
1.98
NADPH
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pH 7.1, 25C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
249.7
glutathione amide disulfide
Marichromatium gracile
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pH 7.1, 25C
146
glutathione disulfide
Marichromatium gracile
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pH 7.1, 25C
186.8
NADH
Marichromatium gracile
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pH 7.1, 25C
0.14
NADPH
Marichromatium gracile
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pH 7.1, 25C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2574
glutathione amide disulfide
Marichromatium gracile
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pH 7.1, 25C
12001
21.2
glutathione disulfide
Marichromatium gracile
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pH 7.1, 25C
973
14150
NADH
Marichromatium gracile
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pH 7.1, 25C
8
0.07
NADPH
Marichromatium gracile
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pH 7.1, 25C
5
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
98000
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gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
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x * 49028, electrospray ionization mass spectrometry
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
crystal structure of the the enzyme both alone and in complex with NAD+ at 2.1 and 2.5 A resolution, respectively
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grown at 21C by the hanging-drop vapour-diffusion method using lithium sulfate as a precipitant in the presence of nickel ions. The crystals belong to space group P4(1), with unit-cell parameters a = b = 71.93, c = 223.85 A, alpha = beta = gamma = 90 and one dimer per asymmetric unit. A full set of X-ray diffraction data is collected to 2.1 A resolution with a completeness of 95.2%
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
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