Information on EC 6.3.2.23 - homoglutathione synthase

New: Word Map on EC 6.3.2.23
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Mark a special word or phrase in this record:
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...)


The expected taxonomic range for this enzyme is: Papilionoideae

EC NUMBER
COMMENTARY
6.3.2.23
-
RECOMMENDED NAME
GeneOntology No.
homoglutathione synthase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ATP + gamma-L-glutamyl-L-cysteine + beta-alanine = ADP + phosphate + gamma-L-glutamyl-L-cysteinyl-beta-alanine
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
peptide synthase reaction
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
homoglutathione biosynthesis
-
-
SYSTEMATIC NAME
IUBMB Comments
gamma-L-glutamyl-L-cysteine:beta-alanine ligase (ADP-forming)
Not identical with EC 6.3.2.3 glutathione synthase.
SYNONYMS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
beta-alanine specific hGSH synthetase
-
-
-
-
homoglutathione synthetase
-
-
-
-
synthetase, homoglutathione
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
113875-72-2
-
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
expressed in transgenic tobacco plants
-
-
Manually annotated by BRENDA team
ecotype MG-20, in nodulated plants x Mesorhizobium loti R7A
-
-
Manually annotated by BRENDA team
cv. Aragon x Sinorhizobium meliloti 102F78
-
-
Manually annotated by BRENDA team
ecotype Jemalong
-
-
Manually annotated by BRENDA team
no activity in Lupinus luteus
-
-
-
Manually annotated by BRENDA team
no activity in Vicia faba
-
-
-
Manually annotated by BRENDA team
no activity in Vigna radiata
-
-
-
Manually annotated by BRENDA team
cv. Contender x Rhizobium leguminosarum cv. phaseoli 3622
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
-
homoglutathione synthetase has evolved from glutathione synthetase, EC 6.3.2.3, by a single gene duplication event
metabolism
-
the response profile of GSH and hGSH in nonnodulated and nodulated plants to treatment with various hormones indicate that thiol homeostasis is independent of the nitrogen source of the plants
physiological function
-
differential regulation of mRNA levels, enzyme activity, and thiol contents by hormones, overview. Glutathione and homoglutathione play distinct roles in plant development and stress response
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + gamma-glutamylcysteine + gamma-aminobutyrate
ADP + phosphate + gamma-glutamylcysteinyl-4-aminobutyrate
show the reaction diagram
-
-
-
-
?
ATP + gamma-glutamylcysteine + glycine
ADP + phosphate + gamma-glutamylcysteinylglycine
show the reaction diagram
-
-
-
-
?
ATP + gamma-glutamylcysteine + glycine
ADP + phosphate + gamma-glutamylcysteinylglycine
show the reaction diagram
-
-
-
-
?
ATP + gamma-glutamylcysteine + glycine
ADP + phosphate + gamma-glutamylcysteinylglycine
show the reaction diagram
Q9XEB8
-
-
?
ATP + gamma-glutamylcysteine + glycine
ADP + phosphate + gamma-glutamylcysteinylglycine
show the reaction diagram
-
-
i.e. glutathione
?
ATP + gamma-L-glutamyl-L-cysteine + beta-alanine
ADP + phosphate + gamma-L-glutamyl-L-cysteinyl-beta-alanine
show the reaction diagram
-
-
-
?
ATP + gamma-L-glutamyl-L-cysteine + beta-alanine
ADP + phosphate + gamma-L-glutamyl-L-cysteinyl-beta-alanine
show the reaction diagram
-
-
-
-
?
ATP + gamma-L-glutamyl-L-cysteine + beta-alanine
ADP + phosphate + gamma-L-glutamyl-L-cysteinyl-beta-alanine
show the reaction diagram
-
-
-
?
ATP + gamma-L-glutamyl-L-cysteine + beta-alanine
ADP + phosphate + gamma-L-glutamyl-L-cysteinyl-beta-alanine
show the reaction diagram
-
-
-
?
ATP + gamma-L-glutamyl-L-cysteine + beta-alanine
ADP + phosphate + gamma-L-glutamyl-L-cysteinyl-beta-alanine
show the reaction diagram
-
-
-
?
ATP + gamma-L-glutamyl-L-cysteine + beta-alanine
ADP + phosphate + gamma-L-glutamyl-L-cysteinyl-beta-alanine
show the reaction diagram
-
-
-
-
?
ATP + gamma-L-glutamyl-L-cysteine + beta-alanine
ADP + phosphate + gamma-L-glutamyl-L-cysteinyl-beta-alanine
show the reaction diagram
Q9XEB8
-
-
?
ATP + gamma-L-glutamyl-L-cysteine + beta-alanine
ADP + phosphate + gamma-L-glutamyl-L-cysteinyl-beta-alanine
show the reaction diagram
Q9FV27
-
-
-
?
ATP + gamma-L-glutamyl-L-cysteine + beta-alanine
ADP + phosphate + gamma-L-glutamyl-L-cysteinyl-beta-alanine
show the reaction diagram
Q9FV26
-
-
-
?
ATP + gamma-L-glutamyl-L-cysteine + beta-alanine
ADP + phosphate + gamma-L-glutamyl-L-cysteinyl-beta-alanine
show the reaction diagram
-
-
i.e. homoglutathione
?
ATP + gamma-L-glutamyl-L-cysteine + beta-alanine
ADP + phosphate + gamma-L-glutamyl-L-cysteinyl-beta-alanine
show the reaction diagram
-
-
i.e. homo-glutathione
-
?
ATP + gamma-L-glutamyl-L-cysteine + beta-alanine
ADP + phosphate + gamma-L-glutamyl-L-cysteinyl-beta-alanine
show the reaction diagram
-
-
i.e. homo-glutathione
-
?
ATP + gamma-L-glutamyl-L-cysteine + beta-alanine
ADP + phosphate + gamma-L-glutamyl-L-cysteinyl-beta-alanine
show the reaction diagram
-
deficiency on GSH and hGSH synthesis inhibits the formation of the root nodule
-
-
?
ATP + gamma-L-glutamyl-L-cysteine + beta-alanine
ADP + phosphate + gamma-L-glutamyl-L-cysteinyl-beta-alanine
show the reaction diagram
-
transgenic tobacco plants expressing homoglutathione synthase in the cytosol exhibit tolerance to acifluorfen but not to fomesafen, those expressing the enzyme in chloroplasts exhibit no enhanced tolerance to acifluorfen or fomesafen
-
-
?
ATP + gamma-L-glutamyl-L-cysteine + beta-alanine
?
show the reaction diagram
-
assay at pH 7.5, 25°C
-
-
?
ATP + gamma-L-glutamyl-L-cysteine + glycine
?
show the reaction diagram
-
assay at pH 7.5, 25°C
-
-
?
ATP + gamma-L-glutamyl-L-cysteine + L-serine
ADP + phosphate + gamma-L-glutamyl-L-cysteinyl-L-serine
show the reaction diagram
-
-
i.e. hydroxymethyl-glutathione
-
?
additional information
?
-
-
exposition of plants to drought results in down-regulation of homoglutathione synthetase
-
-
-
additional information
?
-
-
regulation of ascorbate and homoglutathione biosynthesis in common bean nodules under stress conditions and during aging, the homoglutathione synthetase expression and activity is not affected by stress. During senescence in the first stage ascorbate decreases by 60%, while homoglutathione and antioxidant activities remain fairly constant,whereas in the second stage ascorbate and homoglutathione, their redox states, and their associated enzyme activities significantly decrease, overview
-
-
-
additional information
?
-
-
hGSH synthetase found in plants is much more specific for beta-Ala, although it also accepts Gly as a substrate
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ATP + gamma-L-glutamyl-L-cysteine + beta-alanine
ADP + phosphate + gamma-L-glutamyl-L-cysteinyl-beta-alanine
show the reaction diagram
-
-
-
-
?
ATP + gamma-L-glutamyl-L-cysteine + beta-alanine
ADP + phosphate + gamma-L-glutamyl-L-cysteinyl-beta-alanine
show the reaction diagram
-
-
-
?
ATP + gamma-L-glutamyl-L-cysteine + beta-alanine
ADP + phosphate + gamma-L-glutamyl-L-cysteinyl-beta-alanine
show the reaction diagram
-
-
-
-
?
ATP + gamma-L-glutamyl-L-cysteine + beta-alanine
ADP + phosphate + gamma-L-glutamyl-L-cysteinyl-beta-alanine
show the reaction diagram
-
-
i.e. homoglutathione
?
ATP + gamma-L-glutamyl-L-cysteine + beta-alanine
ADP + phosphate + gamma-L-glutamyl-L-cysteinyl-beta-alanine
show the reaction diagram
-
-
i.e. homo-glutathione
-
?
ATP + gamma-L-glutamyl-L-cysteine + beta-alanine
ADP + phosphate + gamma-L-glutamyl-L-cysteinyl-beta-alanine
show the reaction diagram
-
deficiency on GSH and hGSH synthesis inhibits the formation of the root nodule
-
-
?
ATP + gamma-L-glutamyl-L-cysteine + beta-alanine
ADP + phosphate + gamma-L-glutamyl-L-cysteinyl-beta-alanine
show the reaction diagram
-
transgenic tobacco plants expressing homoglutathione synthase in the cytosol exhibit tolerance to acifluorfen but not to fomesafen, those expressing the enzyme in chloroplasts exhibit no enhanced tolerance to acifluorfen or fomesafen
-
-
?
ATP + gamma-L-glutamyl-L-cysteine + L-serine
ADP + phosphate + gamma-L-glutamyl-L-cysteinyl-L-serine
show the reaction diagram
-
-
-
-
?
additional information
?
-
-
exposition of plants to drought results in down-regulation of homoglutathione synthetase
-
-
-
additional information
?
-
-
regulation of ascorbate and homoglutathione biosynthesis in common bean nodules under stress conditions and during aging, the homoglutathione synthetase expression and activity is not affected by stress. During senescence in the first stage ascorbate decreases by 60%, while homoglutathione and antioxidant activities remain fairly constant,whereas in the second stage ascorbate and homoglutathione, their redox states, and their associated enzyme activities significantly decrease, overview
-
-
-
additional information
?
-
-
hGSH synthetase found in plants is much more specific for beta-Ala, although it also accepts Gly as a substrate
-
-
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
K+
-
stimulation
Mg2+
-
2-3 mM optimal; requirement
Mg2+
-
requirement
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
adenosine 5'-phosphosulfate
-
5 mM: 10-30% inhibition
ADP
-
5 mM: 70% inhibition
AMP
-
5 mM: 10-30% inhibition
cysteine
-
5 mM: 15% inhibition
glutathione
-
5 mM: 15% inhibition
additional information
-
methionine, homocysteine, S-adenosyl-methionine, serine, all 5 mM, are no inhibitors
-
additional information
-
the enzyme is not affected by jasmonate, Cd2+ and H2O2, overview
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
auxin
-
activates enzyme activity
additional information
-
no activation by cyctokinins and polyamines
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.023
ATP
-
-
0.33
beta-Alanine
-
-
1.34
beta-Alanine
-
-
1.9
beta-Alanine
-
-
3.39
beta-Alanine
-
wild-type enzyme
3.8
beta-Alanine
-
mutant L487A
8
beta-Alanine
-
mutant P488A
24.8
beta-Alanine
-
mutant L487A/P488A
8.3
gamma-aminobutyrate
-
-
0.073
gamma-glutamylcysteine
-
-
0.75
gamma-glutamylcysteine
-
-
0.044
gamma-L-glutamyl-L-cysteine
-
-
2.2
glycine
-
mutant L487A/P488A
5.1
glycine
-
mutant P488A
6.5
glycine
-
mutant L487A
98
glycine
-
-
104
glycine
-
-
additional information
additional information
-
glycine, value above 100 mM, wild-type enzyme
-
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
73.91
ATP
-
-
4
0.077
beta-Alanine
-
mutant L487A/P488A
494
0.211
beta-Alanine
-
mutant L487A
494
0.313
beta-Alanine
-
mutant P488A
494
0.708
beta-Alanine
-
wild-type enzyme
494
56.82
gamma-L-glutamyl-L-cysteine
-
-
4246
0.001
glycine
-
wild-type enzyme
72
0.046
glycine
-
mutant L487A
72
0.274
glycine
-
mutant P488A
72
0.95
glycine
-
mutant L487A/P488A
72
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.042
-
gamma-glutamylcysteine + beta-alanine
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
8 - 9
-
broad
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7 - 10
-
50% of maximal activity at pH 7 and pH 10
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
Q9FV27
root nodules
Manually annotated by BRENDA team
-
hgshs expression is not upregulated after after treatment with the NO-donors sodium nitroprusside and nitrosoglutathione
Manually annotated by BRENDA team
-
nodulated plants
Manually annotated by BRENDA team
-
nodulated plants, mainly in starch grains within plastids
Manually annotated by BRENDA team
-
nonnodulated and nodulated plants
Manually annotated by BRENDA team
-
mainly in starch grains within chloroplasts
Manually annotated by BRENDA team
additional information
-
no activity in leaf
Manually annotated by BRENDA team
additional information
-
immunolocalization studies of thiol synthetases in leaves, roots, and nodules, overview
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
17% of enzyme activity in the leaf cells
Manually annotated by BRENDA team
-
of leaf chloroplasts and root plastids
Manually annotated by BRENDA team
-
of transgenic robacco
Manually annotated by BRENDA team
additional information
-
immunolocalization studies of thiol synthetases in leaves, roots, and nodules, overview
-
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
50000
-
SDS-PAGE
706219
85000
-
gel filtration
1185
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
-
x * 50000, about, recombinant tagged enzyme, SDS-PAGE
monomer
-
-
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
vapor diffusion method
-
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
40
-
20 h, 50 mM potassium phosphate buffer, pH 7.5: 15% remaining activity. 20 h, buffer plus 10% (v/v) glycerol: 30% remaining activity. 20 h, buffer with glycerol plus 1 mM dithiothreitol: 50% remaining activity. 20 h, buffer with glycerol and dithiothreitol plus 10 mg/ml bovine serum albumin: 85% remaining activity
1185
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, more than 1 mg enzyme/ml in potassium phosphate buffer, 30-50% glycerol, 1 mM dithiothreitol, stable for at least 4 months
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
mixed benzamidine-sepharose/Ni2+-NTA column, Superdex-200 FPLC column
-
recombinant N-terminally maltose binding protein- and His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity and immuno affinity chromatography
-
recombinant N-terminally maltose binding protein- and His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity and immuno affinity chromatography
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli BL21
-
recombinant expression of N-terminally maltose binding protein- and His-tagged enzyme in Escherichia coli strain BL21(DE3), subcloning in Escherichia coli strain DH5alpha
-
expression in Escherichia coli
-
recombinant expression of N-terminally maltose binding protein- and His-tagged enzyme in Escherichia coli strain BL21(DE3), subcloning in Escherichia coli strain DH5alpha
-
expression in Escherichia coli
C9VXR2
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
abscisic acid downregulates the enzyme in nonnodulated plants, salicylic acid downregulates the enzyme slightly in nodulated plants, jasmonic acid, and auxin downregulate the enzyme in roots, cytokinins and polyamines reduce the enzyme slightly in nodulated plants
-
abscisic acid upregulates the enzyme slightly in nodulated plants, salicylic acid upregulates the enzyme slightly in nonnodulated plants, indole-3-acetic acid induces the enzyme slightly in nodulated plants
-
increased expression in response to progressive drought stress
C9VXR2
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
L487A
-
improved catalytic efficiency using glcyine
L487A/P488A
-
conversion of substrate preference from beta-alanine to glycine
P488A
-
improved catalytic efficiency using glcyine
L534A
-
increased production of glutathione and reduced formation of homglutathione
L534A/P535A
-
as compared with L534A mutant, even further increased production of glutathione and further reduced formation of homglutathione
L534A/P535A
-
site-directed mutagenesis, the mutant shows properties similar to GSH synthetase, EC 6.3.2.3. A534 and A535 are conserved in glutathione synthetase