Information on EC 1.8.1.13 - bis-gamma-glutamylcystine reductase

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Select one or more organisms in this record:
Show additional data
Do not include text mining results
Include (text mining) results (more...)
Include results (AMENDA + additional results, but less precise; more...)
Please login to have access to the AMENDA and FRENDA data


The expected taxonomic range for this enzyme is: Halobacterium salinarum

top print hide
EC NUMBER
COMMENTARY hide
1.8.1.13
-
top print hide
RECOMMENDED NAME
GeneOntology No.
bis-gamma-glutamylcystine reductase
top print hide
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
-
-
-
top print hide
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
top print hide
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Glutathione metabolism
-
-
glutathione metabolism
-
-
top print hide
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).
top
top print hide
CAS REGISTRY NUMBER
COMMENTARY hide
117056-54-9
-
top print hide
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
top print hide
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
enzyme is a member of the pyridine nucleotide disulfide oxidoreductase family
top print hide
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
?
-
top print hide
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
-
-
-
-
?
top print hide
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADH
-
less effective than NADPH
top print hide
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%
top print hide
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.81 - 1.1
bis-gamma-glutamylcystine
top print hide
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
-
-
top print hide
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
top print hide
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
top print hide
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
top print hide
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.3 - 8.2
-
about half-maximal activity at pH 6.3 and 8.2
top print hide
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
top print hide
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
61000
-
2 * 61000, SDS-PAGE
122000
top print hide
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
-
2 * 61000, SDS-PAGE
top print hide
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
top print hide
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
-
top print hide
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
20�C, stable to prolonged storage at room temperature in high-ionic-strength buffer above 3.5 M
-
top print hide
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
both native enzyme and recombinant enzyme, from inclusion bodies
top print hide
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
top
top
top
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)