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Information on EC 6.3.1.2 - glutamine synthetase and Organism(s) Hordeum vulgare and UniProt Accession P13564
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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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Word Map
- 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: Hordeum vulgare
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
-
-
-
-
GS2
-
-
-
-
L-Glutamine synthetase
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ATP + L-glutamate + NH3 = ADP + phosphate + L-glutamine
reaction mechanism
ATP + L-glutamate + NH3 = ADP + phosphate + L-glutamine
reaction mechanism
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
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
senescence-specific downregulation of plastidic glutamine synthetase isozyme GS2, this is retarded by fertilisation of plants with nitrate or ammonium, but not urea, at the onset of leaf senescence, GS2 downregulation preceeds upregulation of lysine-ketoglutarate reductase and saccharopine dehydrogenase, overview
-
-
?
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, phopshate and ADP
-
-
?
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, phopshate and ADP
-
-
?
additional information
?
-
structure-activity relationship, overview
-
-
?
additional information
?
-
structure-activity relationship, 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 + NH3
ADP + phosphate + L-glutamine
senescence-specific downregulation of plastidic glutamine synthetase isozyme GS2, this is retarded by fertilisation of plants with nitrate or ammonium, but not urea, at the onset of leaf senescence, GS2 downregulation preceeds upregulation of lysine-ketoglutarate reductase and saccharopine dehydrogenase, overview
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
Mg2+
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
structure-activity relationships and inhibitor design, overview
-
additional information
structure-activity relationships and inhibitor design, overview
-
additional information
-
structure-activity relationships and inhibitor design, overview
-
additional information
structure-activity relationships and inhibitor design, overview
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
pinitol
-
0.4 M results in maintenance of activity to 90% and 50% during heat treatment
additional information
-
glucose shows little tendency to protect the enzyme from loss of activity
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
isozyme GS2 expression levels in response to nitrate and ammonium levels, overview
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
-
the rate-limiting step in photorespiration is the reassimilation of ammonia catalyzed by chloroplastic glutamine synthetase isozyme 2 (GS2). In plants, GS2 together with ferredoxin-dependent glutamate synthase (Fd-GOGAT) plays a major role in re-assimilation of ammonium liberated in mitochondria by the glycine decarboxylase, in the pathway known as glutamine synthetase/glutamate synthase (GS/GOGAT) cycle in chloroplasts. The product of this cycle, glutamate, is required for one of the peroxisomal transamination reactions
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). GLNA2_HORVU
434
0
47094
Swiss-Prot
other Location (Reliability: 2)
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
determination and photosynthetic responses of GS2 mutant of barley with reduced activity of chloroplastic glutamine synthetase, overview. The mutation of the enzyme not directly associated with conversion of light energy leads to significant modifications of structure and function of photosystems
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
40 - 55
-
activity decreases to 50% on heating at 40°C and to 10% or less on incubation at 55°C
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
myo-inositol (0.4 M) protects enzymatic activity during heat treatment, pinitol (0.4 M) results in maintenance of activity to 90% and 50% during heat treatment, glucose shows little tendency to protect the enzyme from loss of activity
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Jaindl, M.; Popp, M.
Cyclitols protect glutamine synthetase and malate dehydrogenase against heat induced deactivation and thermal denaturation
Biochem. Biophys. Res. Commun.
345
761-765
2006
Escherichia coli, Hordeum vulgare
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)
Schildhauer, J.; Wiedemuth, K.; Humbeck, K.
Supply of nitrogen can reverse senescence processes and affect expression of genes coding for plastidic glutamine synthetase and lysine-ketoglutarate reductase/saccharopine dehydrogenase
Plant Biol.
10 Suppl 1
76-84
2008
Hordeum vulgare (P13564), Hordeum vulgare, Arabidopsis thaliana (Q43127), Arabidopsis thaliana
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