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Information on EC 6.3.1.2 - glutamine synthetase and Organism(s) Oryza sativa and UniProt Accession P14654
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6.3.1.2 glutamine synthetaseIUBMB Comments
Glutamine synthetase, which catalyses the incorporation of ammonium into glutamate, is a key enzyme of nitrogen metabolism found in all domains of life. Several types have been described, differing in their oligomeric structures and cofactor requirements.
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- 6.3.1.2
- aminotransferase
- gg
- glial
- astrocyte
- nitrate
- bilirubin
- sulfoximine
-
alt
- cerebral
- hepatocytes
- retina
-
fibrillary
- cholesterol
- glutaminase
- albumin
- transaminase
- creatinine
-
adenylylation
- triglyceride
- nodule
-
astroglial
- bile
-
neurotransmitter
-
excitatory
-
c-reactive
-
uric
- no3
-
neurotoxicity
-
glutamatergic
- nitrogenase
-
hyperammonemia
-
excitotoxicity
- cirrhosis
- l-methionine
- anabaena
-
periportal
- pii
- cholestasis
- gamma-gt
-
photorespiratory
-
n2-fixing
-
pericentral
- gamma-glutamyltransferase
-
photorespiration
-
corpuscular
- adenylyltransferase
-
drinker
-
assimilatory
-
remobilization
- drug development
- synthesis
- pharmacology
- diagnostics
- heterocysts
- medicine
- analysis
The taxonomic range for the selected organisms is: Oryza sativa
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Synonyms
glutamine synthetase, gamma-glutamyl transferase, gs-ii, gsiii, taase, glna1, glna2, gln1;2, gln synthetase, gs(1), 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Chloroplast GS2
-
-
-
-
Clone lambda-GS28
-
-
-
-
Clone lambda-GS31
-
-
-
-
Clone lambda-GS8
-
-
-
-
Cytoplasmic GS3
-
-
-
-
Cytosolic GS1
-
-
-
-
Gln isozyme alpha
-
-
-
-
Gln isozyme beta
-
-
-
-
Gln isozyme gamma
-
-
-
-
Glutamate--ammonia ligase
-
-
-
-
glutamate-ammonia ligase
-
-
-
-
Glutamine synthetase
Glutamylhydroxamic synthetase
-
-
-
-
GS
-
-
-
-
GS(1)
-
-
-
-
GS1
-
-
-
-
GS107
-
-
-
-
GS112
-
-
-
-
GS117
-
-
-
-
GS122
-
-
-
-
GS2
-
-
-
-
GSI
-
-
-
-
GSII
-
-
-
-
GSIII
-
-
-
-
Isozyme delta
-
-
-
-
L-Glutamine synthetase
-
-
-
-
N47/N48
-
-
-
-
S2205/S2287
-
-
-
-
Synthetase, glutamine
-
-
-
-
Glutamine synthetase
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
PATHWAY SOURCE
PATHWAYS
KEGG
-
-, -, -, -, -, -
SYSTEMATIC NAME
IUBMB Comments
L-glutamate:ammonia ligase (ADP-forming)
Glutamine synthetase, which catalyses the incorporation of ammonium into glutamate, is a key enzyme of nitrogen metabolism found in all domains of life. Several types have been described, differing in their oligomeric structures and cofactor requirements.
CAS REGISTRY NUMBER
COMMENTARY
9023-70-5
-
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
hydroxylamine + L-glutamine + ATP
L-gamma-glutamyl-hydroxamate + ammonia + ADP
gamma-glutamylhydroxamate synthetase activity
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
a two-step reaction with phosphorylation of L-glutamate by ATP to give gamma-glutamyl phosphate followed by addition of ammonia and release of phosphate resulting in L-glutamine, phosphate and ADP
-
-
?
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
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
structure-activity relationships and inhibitor design, overview
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
total GS, GS1 and GS2 activities in leaf, stem and root of rice in cultivars IR-64 and Khitish seedlings at various stages of water deprivation, overview
additional information
total GS, GS1 and GS2 activities in leaf, stem and root of rice in cultivars IR-64 and Khitish seedlings at various stages of water deprivation, overview
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
additional information
mRNA and protein contents of GS isoforms, overview
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
physiological function
-
rice mutant lacking OsGS1-1 exhibits severe retardation of shoot growth in the presence of ammonium compared with the wild-type. Overaccumulation of free ammonium in the leaf sheath and roots of the mutant indicates the importance of OsGS1-1 for ammonium assimilation in both organs. The mutant line displays an imbalance in levels of sugars, amino acids and metabolites in the tricarboxylic acid cycle, and overaccumulation of secondary metabolites, particularly in the roots under a continuous supply of ammonium. Presence of mutant-specific networks between tryptamine andother primary metabolites in the roots
physiological function
the enzyme catalyzes the ATP-dependent assimilation of ammonium into glutamate to yield glutamine, which is then used for the biosynthesis of essentially all nitrogenous compounds. Effect of water deprivation varies with variety, degree and duration of stress
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
gene GS1 transcript and polypeptide accumulate in leaf during drought, but GS1 activity is maintained at a constant level
total enzyme activity in stem of both the varieties is insensitive to drought
under drought stress, total GS activity in root and leaf decreases significantly in IR-64 seedlings in comparison to Khitish seedlings. The reduced GS activity in IR-64 leaf is mainly due to decrease in isozyme GS2 activity, which correlates with decrease in corresponding transcript and polypeptide contents
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Berlicki, L.
Inhibitors of glutamine synthetase and their potential application in medicine
Mini Rev. Med. Chem.
8
869-878
2008
Beta vulgaris, Bradyrhizobium japonicum, Chlorella sp., Columba sp., Escherichia coli, Ovis aries, Hordeum vulgare, Hordeum vulgare (P13564), Oryza sativa, Vigna radiata, Pisum sativum, Sorghum sp., Spinacia oleracea, Triticum aestivum, Zea mays, Senna obtusifolia, Rattus norvegicus (P09606), Salmonella enterica subsp. enterica serovar Typhimurium (P0A1P6), Bacillus subtilis (P12425), Homo sapiens (P15104), Mus musculus (P15105), Synechocystis sp. (P77961), Mycobacterium tuberculosis (P9WN39), Mycobacterium tuberculosis H37Rv (P9WN39)
Kusano, M.; Tabuchi, M.; Fukushima, A.; Funayama, K.; Diaz, C.; Kobayashi, M.; Hayashi, N.; Tsuchiya, Y.; Takahashi, H.; Kamata, A.; Yamaya, T.; Saito, K.
Metabolomics data reveal a crucial role of cytosolic glutamine synthetase 1;1 in coordinating metabolic balance in rice
Plant J.
66
456-466
2011
Oryza sativa
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