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Information on EC 6.3.2.3 - glutathione synthase and Organism(s) Saccharomyces cerevisiae and UniProt Accession Q08220

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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:
Saccharomyces cerevisiae
UNIPROT: Q08220 not found.
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Word Map
The taxonomic range for the selected organisms is: Saccharomyces cerevisiae
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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-
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Glutathione synthetase
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-
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Glutathione synthetase (tripeptide)
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GSH synthetase
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-
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GSHase
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-
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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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-
additional information
enzyme belongs to the ATP-grasp enzyme superfamily
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
ATP + gamma-L-glutamyl-L-cysteine + glycine = ADP + phosphate + glutathione
show the reaction diagram
determination of reaction and substrate binding mechanisms, large conformational changes in the catalytic cycle
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-L-Glu-L-Cys + Gly
ADP + phosphate + glutathione
show the reaction diagram
ATP + gamma-Glu-2-aminobutyrate + hydroxylamine
ADP + phosphate + gamma-(alpha-aminomethyl)Glu-2-aminobutyryl-Gly
show the reaction diagram
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-
-
-
?
ATP + gamma-Glu-aminobutyrate + Gly
ADP + phosphate + ophthalmic acid
show the reaction diagram
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-
-
-
?
ATP + gamma-Glu-L-Cys + Gly
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-Glu-L-Cys + Gly
ADP + phosphate + glutathione
show the reaction diagram
final step in glutathione biosynthesis
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ir
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ATP
dependent on, binding structure
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
required, binding structure
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.083
ATP
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reaction with Glu-alpha-aminobutyrate + hydroxylamine
0.5
gamma-Glu-2-aminobutyrate
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-
0.8
Gly
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hydroxylamine
additional information
additional information
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
122000 - 123000
60000
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2 * 60000, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
homodimer, crystal structure
dimer
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2 * 60000, SDS-PAGE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystallization by vapour-diffusion hanging-drop method of the free enzyme or the enzyme liganded to substrate gamma-glutamylcysteine and non-hydrolyzable ATP-substrate-analogue AMP-PNP, 17 mg/ml enzyme in 10 mM Tris-HCl, pH 8.0, 150 mM NaCl, 1 mM DTT, plus equal volume of reservoir solution: for crystals of free enzyme with 1.97 M ammonium sulfate, 0.1 M Tris-HCl, pH 8.0, 2% PEG 400 at 22°C, or for the liganded enzyme with 3 mM AMP-PNP, 10 mM MgCl2, 3 mM gamma-glutamylcysteine against a well solution of 2.2 M ammonium sulfate, 0.1 M Tris-HCl, pH 8.0, 2% PEG 400, 5 mM TCEP, 40 mM MgCl2, at 22°C, X-ray diffraction structure determination and analysis at 2.3 A and 1.8 A, respectively
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
58
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relatively stable in presence of 25 mM glutathione
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Dennda, G.; Kula, M.R.
Purification and evaluation of the glutathione-synthesizing enzymes from Candida boidinii for cell-free synthesis of glutathione
J. Biotechnol.
4
143-158
1986
Brettanomyces abstinens, Saccharomyces cerevisiae, [Candida] boidinii, Pichia kudriavzevii, Cyberlindnera jadinii, Pichia membranifaciens, Ogataea angusta
-
Manually annotated by BRENDA team
Meister, A.
Glutathione synthesis
The Enzymes, 3rd Ed. (Boyer, P. D. , ed. )
10
671-697
1974
Saccharomyces cerevisiae, Escherichia coli, Homo sapiens, Pigeon
-
Manually annotated by BRENDA team
Mooz, E.D.; Meister, A.
Glutathione biosynthesis. I. gamma-Glutamylcysteine synthetase (hog liver). II. Glutathione (tripeptide) synthetase (yeast)
Methods Enzymol.
17B
483-495
1971
Saccharomyces cerevisiae
-
Manually annotated by BRENDA team
Gogos, A.; Shapiro, L.
Large conformational changes in the catalytic cycle of glutathione synthase
Structure
10
1669-1676
2002
Saccharomyces cerevisiae (Q08220), Saccharomyces cerevisiae
Manually annotated by BRENDA team