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Information on EC 6.3.2.3 - glutathione synthase and Organism(s) Arabidopsis thaliana

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EC Tree
     6 Ligases
         6.3 Forming carbon-nitrogen bonds
             6.3.2 Acid—amino-acid ligases (peptide synthases)
                6.3.2.3 glutathione synthase
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This record set is specific for:
Arabidopsis thaliana
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Word Map
The taxonomic range for the selected organisms is: Arabidopsis thaliana
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
glutathione synthetase, glutathione synthase, gsh synthetase, gshs, gsh-s, gsh synthase, tags2, gshii, gshs1, tags1, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Glutathione synthase
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Glutathione synthetase
Glutathione synthetase (tripeptide)
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GSH synthetase
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-
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GSHase
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-
-
GSS
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-
-
-
Phytochelatin synthetase
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-
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Synthetase, glutathione
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-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
carboxamide formation
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carboxylic acid-amide formation
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SYSTEMATIC NAME
IUBMB Comments
gamma-L-glutamyl-L-cysteine:glycine ligase (ADP-forming)
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CAS REGISTRY NUMBER
COMMENTARY hide
9023-62-5
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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
ATP + gamma-Glu-L-Cys + Gly
ADP + phosphate + glutathione
show the reaction diagram
ATP + gamma-L-glutamyl-L-cysteine + glycine
ADP + phosphate + glutathione
show the reaction diagram
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ATP + gamma-L-glutamyl-L-cysteine + glycine
ADP + phosphate + glutathione
show the reaction diagram
GSH homeostasis in plants is essential for cellular redox control and efficient responses to abiotic and biotic stress. Compartmentation of the GSH biosynthetic pathway is a unique feature of plants, restricting glutathione biosynthesis to the cytosol is sufficient for normal plant development, overview
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ADP
product inhibition
glutathione
product inhibition
phosphate
product inhibition
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.057 - 0.785
ATP
0.035 - 7.03
gamma-Glu-L-Cys
1.18 - 16.1
Gly
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.071 - 12.1
ATP
0.011 - 12.2
gamma-Glu-L-Cys
0.062 - 12.6
Gly
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.77 - 2.67
ADP
16.6 - 35.4
glutathione
25.1 - 69.1
phosphate
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
GSHB_ARATH
539
0
60271
Swiss-Prot
Chloroplast (Reliability: 1)
A0A7G2FAG1_ARATH
483
0
54387
TrEMBL
other Location (Reliability: 2)
A0A5S9Y7U7_ARATH
544
0
60793
TrEMBL
Chloroplast (Reliability: 1)
A0A178UD21_ARATH
539
0
60265
TrEMBL
Chloroplast (Reliability: 1)
Q0WUG4_ARATH
528
0
59211
TrEMBL
Chloroplast (Reliability: 1)
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
E148A
inactive enzyme
E148Q
inactive enzyme
E220A
decreased activity
E220Q
decreased activity
E371A
inactive enzyme
E371Q
decreased activity
E429A
E429Q
K313M
inactive enzyme
K367M
inactive enzyme
K456M
decreased activity
N150A
inactive enzyme
N150D
inactive enzyme
N376A
decreased activity
Q226A
decreased activity
Q226N
decreased activity
R132A
inactive enzyme
R132K
decreased activity
R274A
decreased activity
R274K
decreased activity
R454A
decreased activity
R454K
decreased activity
S153A
decreased activity
S155A
decreased activity
additional information
construction of gsh2 insertion mutants, the mutants have a seedling lethal phenotype in contrast to the embryo lethal phenotype of gamma-glutamate cysteine ligase, gsh1, EC 6.3.2.2, null mutants, overview. The mutants show hyperaccumulation of gamma-glutamylcysteine to levels 5000-fold that in the wild-type and 200fold wild-type levels of GSH, phenotype, overview. Complementation of gsh2 mutants with the cytosol-specific GSH2 give rise to phenotypically wild-type transgenic plants
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Ni2+ affinity chromatography and gel filtration
recombinant enzyme
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli strain C41(DE3)
gene gsh2, physical mapping and genotyping, expression analysis, overview
overexpression in an Escherichia coli expression system
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Jez, J.M.; Cahoon, R.E.
Kinetic mechanism of glutathione synthetase from Arabidopsis thaliana
J. Biol. Chem.
279
42726-42731
2004
Arabidopsis thaliana (P46416), Arabidopsis thaliana
Manually annotated by BRENDA team
Herrera, K.; Cahoon, R.E.; Kumaran, S.; Jez, J.
Reaction mechanism of glutathione synthetase from Arabidopsis thaliana: site-directed mutagenesis of active site residues
J. Biol. Chem.
282
17157-17165
2007
Arabidopsis thaliana (P46416), Arabidopsis thaliana
Manually annotated by BRENDA team
Pasternak, M.; Lim, B.; Wirtz, M.; Hell, R.; Cobbett, C.S.; Meyer, A.J.
Restricting glutathione biosynthesis to the cytosol is sufficient for normal plant development
Plant J.
53
999-1012
2008
Arabidopsis thaliana (P46416)
Manually annotated by BRENDA team