6.3.1.2: glutamine synthetase
This is an abbreviated version!
For detailed information about glutamine synthetase, go to the full flat file.
Word Map on EC 6.3.1.2
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6.3.1.2
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aminotransferase
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gg
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glial
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astrocyte
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nitrate
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bilirubin
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sulfoximine
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alt
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cerebral
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hepatocytes
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retina
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fibrillary
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cholesterol
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glutaminase
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albumin
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transaminase
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creatinine
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adenylylation
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triglyceride
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nodule
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astroglial
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bile
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neurotransmitter
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excitatory
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c-reactive
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uric
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no3
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neurotoxicity
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glutamatergic
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nitrogenase
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hyperammonemia
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excitotoxicity
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cirrhosis
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l-methionine
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anabaena
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periportal
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pii
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cholestasis
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gamma-gt
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photorespiratory
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n2-fixing
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pericentral
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gamma-glutamyltransferase
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photorespiration
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corpuscular
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adenylyltransferase
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drinker
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assimilatory
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remobilization
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drug development
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synthesis
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pharmacology
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diagnostics
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heterocysts
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medicine
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analysis
- 6.3.1.2
- aminotransferase
- gg
- glial
- astrocyte
- nitrate
- bilirubin
- sulfoximine
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alt
- cerebral
- hepatocytes
- retina
-
fibrillary
- cholesterol
- glutaminase
- albumin
- transaminase
- creatinine
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adenylylation
- triglyceride
- nodule
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astroglial
- bile
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neurotransmitter
-
excitatory
-
c-reactive
-
uric
- no3
-
neurotoxicity
-
glutamatergic
- nitrogenase
-
hyperammonemia
-
excitotoxicity
- cirrhosis
- l-methionine
- anabaena
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periportal
- pii
- cholestasis
- gamma-gt
-
photorespiratory
-
n2-fixing
-
pericentral
- gamma-glutamyltransferase
-
photorespiration
-
corpuscular
- adenylyltransferase
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drinker
-
assimilatory
-
remobilization
- drug development
- synthesis
- pharmacology
- diagnostics
- heterocysts
- medicine
- analysis
Reaction
Synonyms
AmGLN1, ATP glutamate-ammonia ligase, Chloroplast GS2, Clone lambda-GS28, Clone lambda-GS31, Clone lambda-GS8, Cytoplasmic GS3, Cytosolic GS1, gamma-glutamyl transferase, gamma-glutamyl:ammonia ligase, gamma-glutamylhydroxamate synthetase, Gln isozyme alpha, Gln isozyme beta, Gln isozyme gamma, Gln synthetase, GLN1,1, GLN1,2, GLN1,3, GLN1,4, GLN1-1, GLN1-2, Gln1;1, Gln1;2, Gln1;3, Gln1;4, Gln1;5, GLN2, GlnA, glnA-1, GlnA1, GlnA2, GlnA3, GlnA4, GlnN, GlnR, GluA, GLUL, Glutamate--ammonia ligase, glutamate-ammonia ligase, Glutamine synthetase, glutamine synthetase cytosolic isozyme 1, glutamine synthetase cytosolic isozyme 2, glutamine synthetase I, glutamine synthetase type II, glutamine synthetase type III, Glutamylhydroxamic synthetase, GS, GS type I, GS type-1, GS(1), GS-II, GS1, GS1 kinase, GS1-1, GS1-2, GS107, GS112, GS117, GS12, GS122, GS1a, GS1beta1, GS1gamma1, GS2, GS2a, GS3, GSI, GSII, GSIII, Isozyme delta, L-glutamate:ammonia ligase, L-glutamate:ammonia ligase (ADP-forming), L-Glutamine synthetase, LDBPK_060370, LdGS, MM_0964, MtGS, N47/N48, OsGLN1,1, OsGLN1,2, protein transacetylase, S2205/S2287, SSO0366, Synthetase, glutamine, TAase, type I glutamine synthetase, type III glutamine synthetase
ECTree
6.3.1.2 glutamine synthetaseAdvanced search results
results (
results (Activating Compound
Activating Compound on EC 6.3.1.2 - glutamine synthetase
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ACTIVATING COMPOUND 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
IMAGE
(R)-2-[3-(diethoxyphosphoryl)phenylamino]-3-hydroxypropionic acid
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(S)-2-[3-(diethoxyphosphoryl)phenylamino]-3-hydroxypropionic acid
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(S)-3-hydroxy-2-(3-methylsulfanylphenylamino)propionic acid
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2-oxoglutarate
activity increases 12fold in the presence of 10 mM 2-oxoglutarate alone and up to 18-fold in the presence of both 2-oxoglutarate and GlnK protein
GlnK
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PII regulator of nitrogen metabolism. In vivo, high GS activity after growth on nitrate is accompanied by presence of GlnK. In vitro, stimulation of activity up to 50%
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GlnK1 protein
activity increases 12fold in the presence of 10 mM 2-oxoglutarate alone and up to 18-fold in the presence of both 2-oxoglutarate and GlnK protein
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GlnK2 protein
activity increases 12fold in the presence of 10 mM 2-oxoglutarate alone and up to 18-fold in the presence of both 2-oxoglutarate and GlnK protein
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glutamate
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in the presence of Mg2+ the activity increases with the concentration of the substrate
L-glutamate
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causes conformational changes similar to those produced by Cl-binding
MK801
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N-methyl-D-aspartate-type glutamate receptor antagonist, activates the enzyme and inhibits osteogenic differentiation of the rat bone marrow stem cells
NH4+
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in the presence of Mg2+ the activity increases with the concentration of the substrate
potassium arsenate
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activates the gamma-glutamylhydroxamate synthetase activity
protein GlnK1
GlnK1 and GlnK2 activate glutamine synthetase in vitro in the presence of 2-oxoglutarate. Enzyme activity increases 12fold in the presence of 10 mM 2-oxoglutarate alone and up to 18fold in the presence of both 2-oxoglutarate and one GlnK
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protein GlnK2
GlnK1 and GlnK2 activate glutamine synthetase in vitro in the presence of 2-oxoglutarate. Enzyme activity increases 12fold in the presence of 10 mM 2-oxoglutarate alone and up to 18fold in the presence of both 2-oxoglutarate and one GlnK
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resveratrol
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activity is increased by resveratrol at concentrations of 0.01 and 0.1 mM, 0.25 mM resveratrol does not affect activity
epicatechin
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0.03 mM completely prevents inactivation of glutamine synthetase by peroxynitrite
epicatechin
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0.03 mM completely prevents inactivation of glutamine synthetase by peroxynitrite
pinitol
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0.4 M results in maintenance of activity to 90% and 50% during heat treatment
trijodothyronine
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only when cultures are simultaneously treated with growth hormone and dexamethasone
trijodothyronine
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only when cultures are simultaneously treated with growth hormone and dexamethasone
trijodothyronine
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only when cultures are simultaneously treated with growth hormone and dexamethasone
trijodothyronine
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only when cultures are simultaneously treated with growth hormone and dexamethasone
additional information
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the level of glnA1 transcription is upregulated under nitrogen limitation conditions
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additional information
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glucose shows little tendency to protect the enzyme from loss of activity
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additional information
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dexamethasone increases transcription of the glutamine synthetase gene in astrocytes. The inductive effect of glucocorticoids is mediated by binding of the glucocorticoid receptor to a glucocorticoid response element in the regulatory region of the glutamine synthetase gene, and this effect is blocked by the proinflammatory cytokines interleukin 1beta and tumor necrosis factor-alpha. N-methyl-D-aspartate indces the enzyme, lipopolysaccharide and interferon-gamma inhibits the induction
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additional information
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glucocorticoids induce the enzyme transcription and translation in osteoblasts
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additional information
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glucocorticoids induce the enzyme transcription and translation in osteoblasts, cortisol and two synthetic compounds dexamethasone and prednisolone highly stimulate enzyme expression. No effects by aldosterone, estradiol, progesterone, dihydrotestosterone, or triiodothyronine. Treatment of MG-63 cells with MG-132, an inhibitor of proteasomal degradation, at 0.02 mM blocks the dexamethasone-induction of glutamine synthetase activity almost completely
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additional information
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glucose shows little tendency to protect the enzyme from loss of activity
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additional information
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the enzyme is not affected by dietary glutamine supplementation or by Mycobacterium bovis bacillus Calmette-Guerin infection, overview
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additional information
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the level of glnA1 transcription is upregulated under nitrogen limitation conditions
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additional information
transcription factor PpDof5 activates transcription of isozymes GS1a and GS1b, it is involved in enzyme expression regulation in the whole plant and during thr whole development and ia expressed itself with low levels of gene expression in green tissues and much higher levels in roots and lignified shoots, high levels in germinating seedlings, overview
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additional information
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transcription factor PpDof5 activates transcription of isozymes GS1a and GS1b, it is involved in enzyme expression regulation in the whole plant and during thr whole development and ia expressed itself with low levels of gene expression in green tissues and much higher levels in roots and lignified shoots, high levels in germinating seedlings, overview
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additional information
the level of glnA1 transcription is upregulated under nitrogen limitation conditions. GlnR is able to function as both an activator and repressor of transcription
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additional information
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the level of glnA1 transcription is upregulated under nitrogen limitation conditions. GlnR is able to function as both an activator and repressor of transcription
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