Information on EC 1.8.1.13 - bis-gamma-glutamylcystine reductase

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The expected taxonomic range for this enzyme is: Halobacterium salinarum

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EC NUMBER
COMMENTARY hide
1.8.1.13
-
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RECOMMENDED NAME
GeneOntology No.
bis-gamma-glutamylcystine reductase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
2 gamma-glutamylcysteine + NADP+ = bis-gamma-glutamylcystine + NADPH + H+
show the reaction diagram
highly specific; highly specific. Not identical with EC 1.8.1.7 glutathione-disulfide reductase or EC 1.8.1.14 CoA-disulfide reductase
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Glutathione metabolism
-
-
glutathione metabolism
-
-
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SYSTEMATIC NAME
IUBMB Comments
gamma-glutamylcysteine:NADP+ oxidoreductase
Contains FAD. The enzyme, which is found only in halobacteria, maintains the concentration of gamma-glutamylcysteine, the major low molecular weight thiol in halobacteria. Not identical with EC 1.8.1.7 (glutathione-disulfide reductase) or EC 1.8.1.14 (CoA-disulfide reductase).
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CAS REGISTRY NUMBER
COMMENTARY hide
117056-54-9
-
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
enzyme is a member of the pyridine nucleotide disulfide oxidoreductase family
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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
5,5'-dithiobis(2-nitrobenzoic acid) + NADPH
4-nitrobenzenethiol + NADP+
show the reaction diagram
-
-
-
-
?
bis-gamma-glutamylcystine + NADPH + H+
2 gamma-glutamylcysteine + NADP+
show the reaction diagram
additional information
?
-
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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
bis-gamma-glutamylcystine + NADPH + H+
2 gamma-glutamylcysteine + NADP+
show the reaction diagram
-
-
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADH
-
less effective than NADPH
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
AsO2-
-
25 mM arsenite, relative activity 46%
Cu2+
-
relative activity less than 5%
Hg2+
-
relative activity less than 5%
Zn2+
-
relative activity less than 44%
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.81 - 1.1
bis-gamma-glutamylcystine
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
54
bis-gamma-glutamylcystine
Halobacterium salinarum
Q9HSN0
pH 6.7, temperature not specified in the publication
28.3
FAD
Halobacterium salinarum
-
-
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
49
bis-gamma-glutamylcystine
Halobacterium salinarum
Q9HSN0
pH 6.7, temperature not specified in the publication
15665
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.3 - 8.2
-
about half-maximal activity at pH 6.3 and 8.2
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
61000
-
2 * 61000, SDS-PAGE
122000
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
-
2 * 61000, SDS-PAGE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
60
-
retains full activity after incubation in high-and intermediate-ionic-strength buffers, inactivated after incubation in low-ionic strength buffers
80
-
inactivation in buffers of each of the 3 ionic strengths, low-ionic, intermediate-ionic and high-ionic
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
high-ionic-strength buffer above 2 M stabilizes during purification and storage
-
high-ionic-strength buffer above 3.5 M increases thermal stability
-
low-ionic-strength buffer below 1.0 M leads to rapid denaturation
-
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
20°C, stable to prolonged storage at room temperature in high-ionic-strength buffer above 3.5 M
-
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
both native enzyme and recombinant enzyme, from inclusion bodies
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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LINKS TO OTHER DATABASES (specific for EC-Number 1.8.1.13)
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)