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Information on EC 6.3.2.2 - glutamate-cysteine ligase and Organism(s) Brassica juncea and UniProt Accession O23736
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6.3.2.2 glutamate-cysteine ligaseIUBMB Comments
Can use L-aminohexanoate in place of glutamate.
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Word Map
- 6.3.2.2
-
ganglion
- retinal
- nerve
- heme
-
plexiform
- fiber
- sulfoximine
- dismutase
-
coherence
-
tomography
-
buthionine
- s-transferase
- oxygenase-1
-
macular
-
erythroid
- quinone
-
neuroprotective
-
2-related
-
amacrine
-
cytoprotective
- gssg
-
nadph:quinone
- glaucoma
-
nf-e2-related
-
acuity
- transpeptidase
-
sd-oct
-
peripapillary
-
intravitreal
-
nrf2-mediated
-
nrf2-dependent
-
dentate
-
spectral-domain
-
nrf2-are
-
factor-erythroid
-
subgranular
-
glutathione-related
-
gsh-dependent
- phytochelatins
-
l-buthionine-s,r-sulfoximine
- tert-butylhydroquinone
-
oxidoreductase-1
-
ech-associated
-
kelch-like
-
nrf2-regulated
-
fovea
- biotechnology
- medicine
-
perimetry
- synthesis
-
gsh-depleting
- agriculture
- drug development
-
etdrs
- pharmacology
-
spectralis
The taxonomic range for the selected organisms is: Brassica juncea
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
gcl, gamma-glutamylcysteine synthetase, glutamate-cysteine ligase, gamma-gcs, glutamate cysteine ligase, gamma-glutamylcysteine ligase, gamma-ecs, glclc, gammagcs, gamma-gc, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Gamma-ECS
-
-
-
-
gamma-Glutamyl-L-cysteine synthetase
-
-
-
-
gamma-Glutamylcysteine synthetase
-
-
-
-
gamma-Glutamylcysteinyl-synthetase
-
-
-
-
GCS
-
-
-
-
Synthetase, gamma-glutamylcysteine
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
carboxylic acid amide formation
-
-
-
-
carboxamide formation
-
-
-
-
PATHWAY SOURCE
PATHWAYS
BRENDA
-
-, -, -, -
SYSTEMATIC NAME
IUBMB Comments
L-glutamate:L-cysteine gamma-ligase (ADP-forming)
Can use L-aminohexanoate in place of glutamate.
CAS REGISTRY NUMBER
COMMENTARY
9023-64-7
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + L-glutamate + L-cysteine
ADP + phosphate + gamma-L-glutamyl-L-cysteine
-
-
-
?
ATP + L-glutamate + L-cysteine
ADP + phosphate + gamma-L-glutamyl-L-cysteine
rate-limiting step in the biosynthesis of GSH. The regulatory mechanism is based on two intramolecular redox-sensitive disulfide bonds. Reduction of one disulfide bond allows a beta-hairpin motif to shield the active site of Brassica juncea GCL, thereby preventing the access of substrates. Reduction of the second disulfide bond reversibly controls dimer to monomer transition of the glutamate-cysteine ligase that is associated with a significant inactivation of the enzyme
-
-
?
ATP + L-glutamate + L-cysteine
ADP + phosphate + gamma-L-glutamyl-L-cysteine
redox regulation of the enzyme, a redox switch based on CC2-mediated homodimerization is unique to plant GCL enzymes, overview
-
-
?
additional information
?
-
the enzyme contains two intramolecular disulfide bridges, CC1 and CC2, which both strongly impact on GCL activity in vitro, cysteines of CC2 involved in the monomer-dimer transition in GCL. CC2 plays a role in GCL redox regulation, overview
-
-
?
additional information
?
-
-
the enzyme contains two intramolecular disulfide bridges, CC1 and CC2, which both strongly impact on GCL activity in vitro, cysteines of CC2 involved in the monomer-dimer transition in GCL. CC2 plays a role in GCL redox regulation, overview
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + L-glutamate + L-cysteine
ADP + phosphate + gamma-L-glutamyl-L-cysteine
rate-limiting step in the biosynthesis of GSH. The regulatory mechanism is based on two intramolecular redox-sensitive disulfide bonds. Reduction of one disulfide bond allows a beta-hairpin motif to shield the active site of Brassica juncea GCL, thereby preventing the access of substrates. Reduction of the second disulfide bond reversibly controls dimer to monomer transition of the glutamate-cysteine ligase that is associated with a significant inactivation of the enzyme
-
-
?
ATP + L-glutamate + L-cysteine
ADP + phosphate + gamma-L-glutamyl-L-cysteine
redox regulation of the enzyme, a redox switch based on CC2-mediated homodimerization is unique to plant GCL enzymes, overview
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). GSH1_BRAJU
514
0
57903
Swiss-Prot
Chloroplast (Reliability: 2)
PDB
SCOP
CATH
UNIPROT
ORGANISM
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
the enzyme contains two intramolecular disulfide bridges, CC1 and CC2, which both strongly impact on GCL activity in vitro, cysteines of CC2 involved in the monomer-dimer transition in GCL. Amino acids contributing to the homodimer interface in BjGCL are highly conserved among plant GCLs, but not in related proteobacterial GCLs
additional information
-
the enzyme contains two intramolecular disulfide bridges, CC1 and CC2, which both strongly impact on GCL activity in vitro, cysteines of CC2 involved in the monomer-dimer transition in GCL. Amino acids contributing to the homodimer interface in BjGCL are highly conserved among plant GCLs, but not in related proteobacterial GCLs
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor diffusion method, crystal structure at 2.1 A resolution
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C356A
the mutant shows reduced inhibition by DTT, but increased inhibition by glutathione
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Hothorn, M.; Wachter, A.; Gromes, R.; Stuwe, T.; Rausch, T.; Scheffzek, K.
Structural basis for the redox control of plant glutamate cysteine ligase
J. Biol. Chem.
281
27557-27565
2006
Brassica juncea (O23736), Brassica juncea
Gromes, R.; Hothorn, M.; Lenherr, E.D.; Rybin, V.; Scheffzek, K.; Rausch, T.
The redox switch of gamma-glutamylcysteine ligase via a reversible monomer-dimer transition is a mechanism unique to plants
Plant J.
54
1063-1075
2008
Agrobacterium tumefaciens, Xanthomonas campestris, Brassica juncea (O23736), Brassica juncea, Nicotiana tabacum (Q1W2L8), Nicotiana tabacum
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