Information on EC 1.8.1.16 - glutathione amide reductase

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The expected taxonomic range for this enzyme is: Marichromatium gracile

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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
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ORGANISM
UNIPROT
LITERATURE
2 glutathione amide + NAD+ = glutathione amide disulfide + NADH + H+
show the reaction diagram
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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].
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CAS REGISTRY NUMBER
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367279-42-3
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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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
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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
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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
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.097
glutathione amide disulfide
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pH 7.1, 25°C
6.9
glutathione disulfide
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pH 7.1, 25°C
0.0132
NADH
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pH 7.1, 25°C
1.98
NADPH
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pH 7.1, 25°C
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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, 25°C
146
glutathione disulfide
Marichromatium gracile
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pH 7.1, 25°C
186.8
NADH
Marichromatium gracile
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pH 7.1, 25°C
0.14
NADPH
Marichromatium gracile
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pH 7.1, 25°C
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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, 25°C
12001
21.2
glutathione disulfide
Marichromatium gracile
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pH 7.1, 25°C
973
14150
NADH
Marichromatium gracile
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pH 7.1, 25°C
8
0.07
NADPH
Marichromatium gracile
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pH 7.1, 25°C
5
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
49030
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2 * 49030, nanospray ionization mass spectrometry
98000
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gel filtration
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
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x * 49028, electrospray ionization mass spectrometry
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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 21°C 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
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
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Show AA Sequence (104 entries)
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LINKS TO OTHER DATABASES (specific for EC-Number 1.8.1.16)
ExplorEnz
ExPASy
KEGG
MetaCyc
SABIO-RK
NCBI: PubMed, Protein, Nucleotide, Structure, Genome, OMIM
IUBMB Enzyme Nomenclature
PROSITE Database of protein families and domains
SYSTERS
Protein Mutant Database
InterPro (database of protein families, domains and functional sites)