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Enzyme Nomenclature
Information on EC 6.3.1.2 - glutamine synthetase
for references in articles please use BRENDA:EC6.3.1.2
Word Map on EC 6.3.1.2
- 6.3.1.2
- astrocyte
- glial
- nitrate
- urea
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fibrillary
- lactate
- sulfoximine
- cerebral
- injury
- hepatocytes
- retina
- cortex
- glutaminase
- bilirubin
- nodule
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transaminase
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adenylylation
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astroglial
- creatinine
- triglyceride
- hippocampus
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neurotransmitter
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glucocorticoid
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neurotoxicity
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glutamatergic
- nitrogenase
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excitatory
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hyperammonemia
- gamma-gt
- pii
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excitotoxicity
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periportal
- encephalopathy
- anabaena
- l-methionine
- nh3
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perivenous
- cholestasis
- gamma-glutamyltransferase
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pericentral
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corpuscular
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photorespiratory
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photorespiration
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adenylyltransferase
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dodecamer
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carbohydrate-deficient
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n2-fixing
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drinker
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assimilatory
- heterocysts
- drug development
- pharmacology
- medicine
- analysis
- synthesis
- diagnostics
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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
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EC NUMBER 
COMMENTARY 
6.3.1.2
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RECOMMENDED NAME
GeneOntology No.
glutamine synthetase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ATP + L-glutamate + NH3 = ADP + phosphate + L-glutamine
ordered three-reactant system with the binding order: NH4+, L-Glu and ATP
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ATP + L-glutamate + NH3 = ADP + phosphate + L-glutamine
reaction mechanism
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ATP + L-glutamate + NH3 = ADP + phosphate + L-glutamine
reaction mechanism
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ATP + L-glutamate + NH3 = ADP + phosphate + L-glutamine
reaction mechanism and transition state analogue, overview
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ATP + L-glutamate + NH3 = ADP + phosphate + L-glutamine
reaction mechanism; reaction mechanism
ATP + L-glutamate + NH3 = ADP + phosphate + L-glutamine
reaction mechanism
ATP + L-glutamate + NH3 = ADP + phosphate + L-glutamine
reaction mechanism
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ATP + L-glutamate + NH3 = ADP + phosphate + L-glutamine
reaction mechanism
ATP + L-glutamate + NH3 = ADP + phosphate + L-glutamine
reaction mechanism
ATP + L-glutamate + NH3 = ADP + phosphate + L-glutamine
reaction mechanism
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ATP + L-glutamate + NH3 = ADP + phosphate + L-glutamine
reaction mechanism
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ATP + L-glutamate + NH3 = ADP + phosphate + L-glutamine
reaction mechanism
ATP + L-glutamate + NH3 = ADP + phosphate + L-glutamine
reaction mechanism
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ATP + L-glutamate + NH3 = ADP + phosphate + L-glutamine
random catalysis mechanism where the binding order of certain substrates is kinetically preferred by the enzyme
ATP + L-glutamate + NH3 = ADP + phosphate + L-glutamine
structure-function relationship and catalytic mechanism, overview
ATP + L-glutamate + NH3 = ADP + phosphate + L-glutamine
in the first step of catalysis, a tightly bound, activated intermediate, gamma-glutamyl phosphate, is formed when the terminal phosphate of ATP is transferred to the carboxylate side chain of the substrate glutamate. In the second step, an enzyme-bound ammonium ion is deprotonated, forming ammonia that attacks the carbonyl carbon of gamma-glutamyl phosphate to form a tetrahedral intermediate. The enzyme subsequently releases free phosphate and glutamine
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ATP + L-glutamate + NH3 = ADP + phosphate + L-glutamine
structure-function relationship and catalytic mechanism, overview
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ATP + L-glutamate + NH3 = ADP + phosphate + L-glutamine
in the first step of catalysis, a tightly bound, activated intermediate, gamma-glutamyl phosphate, is formed when the terminal phosphate of ATP is transferred to the carboxylate side chain of the substrate glutamate. In the second step, an enzyme-bound ammonium ion is deprotonated, forming ammonia that attacks the carbonyl carbon of gamma-glutamyl phosphate to form a tetrahedral intermediate. The enzyme subsequently releases free phosphate and glutamine
Mycobacterium tuberculosis ATCC 25618 / H37Rv
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ATP + L-glutamate + NH3 = ADP + phosphate + L-glutamine
reaction mechanism
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ATP + L-glutamate + NH3 = ADP + phosphate + L-glutamine
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Acid amide hydrolysis
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carboxylic
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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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.
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CAS REGISTRY NUMBER
COMMENTARY
9023-70-5
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Azolla sp.
a genus of aquatic ferns, which harbors the cyanobacterium Anabaena azollae in specialized cavities formed in its leaves
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gene glnA1 or cg2429 encoding a GSI-beta-subtype enzyme GlnA1 as the functional enzyme form in the organism, gene glnA2 encodes a GSI-alpha-subtype
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nitrogen fixing bacterium, major supplier of fixed nitrogen to sugarcane
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nitrogen fixing bacterium, major supplier of fixed nitrogen to sugarcane
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gene GhGS; allotetraploid, strains 7235 and TM-1, gene GhGS, isozymes GS1 and GS2
UniProt
four highly homolgous GSI protein sequences GlnA1, GlnA2, GlnA3, and GlnA4
UniProt
two isoforms GSI and GSII encoded by the two genes glnA and glnB
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; two isoforms generated by alternative splicing, differences in molecular weights
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gene glula; gene glula, the paralogue has 3 alternative splice variants
UniProt
gene glulb; gene glulb, the paralogue has 3 alternative splice variants
F1QCV3
UniProt
gene glulc; gene glulc, the paralogue has 2 alternative splice variants
UniProt
wild-type and several single-tryptophan mutant forms; wild-type and site-directed mutants H4A, H4C, M8L, H12L, H12D
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wild-type and site-directed mutants H4A, H4C, M8L, H12L, H12D
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wild-type and site-directed mutants; wild-type and site-directed mutants H4A, H4C, M8L, H12L, H12D
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37498, 37561, 37568, 656201, 656584, 676918, 690626, 691521, 692129, 693624, 693789, 693959, 715144, 727277, 745832
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two transcripts arising from alternative splicing of the first intron, named GC2b-alpha and GS2b-beta
UniProt
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UniProt
four highly homolgous GSI protein sequences GlnA1, encoded by gene Rv2220, GlnA2, GlnA3, and GlnA4
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gene glnA1 or gene Rv2220 encoding isozyme GlnA1; gene glnA2 or gene Rv2222c encoding isozyme GlnA2
UniProt
four highly homolgous GSI protein sequences GlnA1, encoded by gene Rv2220, GlnA2, GlnA3, and GlnA4
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gene glnA1 or gene Rv2220 encoding isozyme GlnA1
UniProt
OsGS2; var. indica, drought-sensitive IR-64 cultivar and drought-tolerant Khitish cultivar, gene OsGS2
UniProt
var. indica, drought-sensitive IR-64 cultivar and drought-tolerant Khitish cultivar, gene OsGS1;2
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OsGS1;1; var. indica, drought-sensitive IR-64 cultivar and drought-tolerant Khitish cultivar, gene OsGS1;1
SwissProt
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two enzyme forms: low-activity form and high-activity form, depending on the concentration of combined nitrogen in the medium before harvest
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enzyme form GSI and GSIII encoded by the gene glnA and glnB; strain PCC 6803
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strains SA0 and SA1, SA1 carries a single amino acid mutation Y183C and is defective in ammonia assimilation below concentrations of 0.5 mM
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isozyme GS1a; cv. Cadenza, 10 genes from 4 subfamilies, from hexaploid wheat
UniProt
isozyme GS1b; cv. Cadenza, 10 genes from 4 subfamilies, from hexaploid wheat
UniProt
isozyme GS1c; cv. Cadenza, 10 genes from 4 subfamilies, from hexaploid wheat
UniProt
isozyme GS2a; cv. Cadenza, 10 genes from 4 subfamilies, from hexaploid wheat
UniProt
isozyme GS2b; cv. Cadenza, contains 10 genes from 4 subfamilies, from hexaploid wheat
UniProt
isozyme GS2c; cv. Cadenza, 10 genes from 4 subfamilies, from hexaploid wheat
UniProt
isozyme GSe1; cv. Cadenza, 10 genes from 4 subfamilies, from hexaploid wheat
UniProt
isozyme GSe2; cv. Cadenza, 10 genes from 4 subfamilies, from hexaploid wheat
UniProt
isozyme GSr1; cv. Cadenza, 10 genes from 4 subfamilies, from hexaploid wheat
UniProt
isozyme GSr2; cv. Cadenza, 10 genes from 4 subfamilies, from hexaploid wheat
UniProt
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
drug target
evolution
malfunction
metabolism
physiological function
additional information
drug target
Q4CN04
since glutamine synthetase is the first metabolic enzyme involved in Trypanosoma cruzi evasion from the parasitophorous vacuole it is a potential target for designing anti-Trypanosoma cruzi drugs
drug target
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since glutamine synthetase is the first metabolic enzyme involved in Trypanosoma cruzi evasion from the parasitophorous vacuole it is a potential target for designing anti-Trypanosoma cruzi drugs
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evolution
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Unigene0016999 and Unigene0017002 belong to isozyme GSI, while Unigene0015608, Unigene0022741, and Unigene0002184 belong to isozyme GSII, and Unigene0002194 belongs to isozyme GSIII, sequence comparisons and phylogenetic tree, overview
evolution
two GS isoforms are encoded in the genome of higher plants: the cytosolic Gln synthetase isoform (GS1) and the chloroplastic Gln synthetase isoform (GS2). GS2 is encoded by a single gene (Gln-2), whereas GS1 is encoded by a multigene family, suggesting a complex role of GS1 with respect to plant N assimilation; two GS isoforms are encoded in the genome of higher plants: the cytosolic Gln synthetase isoform (GS1) and the chloroplastic Gln synthetase isoform (GS2). GS2 is encoded by a single gene (Gln-2), whereas GS1 is encoded by a multigene family, suggesting a complex role of GS1 with respect to plant N assimilation; two GS isoforms are encoded in the genome of higher plants: the cytosolic Gln synthetase isoform (GS1) and the chloroplastic Gln synthetase isoform (GS2). GS2 is encoded by a single gene (Gln-2), whereas GS1 is encoded by a multigene family, suggesting a complex role of GS1 with respect to plant N assimilation
evolution
glutamine synthetase (GS), a key enzyme in plant nitrogen metabolism, is encoded by a small family of highly homologous nuclear genes that produce cytosolic (GS1) and plastidic (GS2) isoforms. Compared to GS1, GS2 proteins have two extension peptides, one at the N- and the other at the C-terminus, which show a high degree of conservation among plant species
malfunction
OsGS1;2 homozygously inserted mutants show severe reduction in active tiller number and hence panicle number at harvest. The mutants show marked reductions in contents of glutamine, glutamate, asparagine and aspartate, but an increase in free ammonium ions compared to the wild-type
malfunction
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depletion of the enzyme in Hep-3B cells by transduction with two independent shRNAs reduces LC3-II formation. Conversely, exogenous enzyme overexpression increases autophagic activity in SK-Hep1 cells. Glutamine synthetase (GS) overexpression significantly increases sorafenib sensitivity in hepatocellular carcinoma cells
malfunction
a gln1-1:gln1-2 double mutant shows impairment of seed germination and seedling establishment, phenotype, overview; enzyme mutants, single mutant gln1-2 and gln1-1:gln1-2 double mutant, show impairment of seed germination and seedling establishment. The negative effect of Gln1-2 deficiency, causing slower seedling development in the mutants, is associated with reduced N remobilization from the cotyledons and can be fully alleviated by exogenous N supply. Phenotypes, overview
malfunction
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astrocytes enable the proliferation of GS-negative LN18 iRFP4 cells without Gln supplementation
malfunction
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the total capacity of the enzyme-mediated ligation of free ammonium and glutamate to form glutamine in the leaves of maize plants is not impaired upon severe magnesium starvation. The total GS-mediated primary or secondary assimilation of free NH4+ is not a limiting enzymatic reaction under Mg-deficiency and thus cannot be accountable for the observed restriction of plant growth and productivity in Mg-deficient maize, phenotype, overview
metabolism
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upon exposure to nitrogen limitation,GS activity increases significantly within 0.5 hrs and continues to increase significantly after 1 hr of nitrogen starvation to reach a final activity at 4 hrs that is approximately 2.5 fold greater than at zero hours. When an ammonium pulse is applied, GS activity decreases significantly within 1 hr of exposure to nitrogen excess
metabolism
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presence of only one glutathione synthetase inactivation factor, 7A, encoded by open reading frame asl2329, gifA. Following addition of ammonium, expression of gifA is derepressed, leading to the synthesis of IF7A, and consequently, glutathione synthetase is inactivated. Upon ammonium removal, the glutathione synthetase activity returns to the initial level and IF7A becomes undetectable. Anabaena glutathione synthetase is not inactivated by Synechocystis IFs. In an Anabaena strain expressing a second inactivating factor, containing the amino-terminal part of IF17 from Synechocystis fused to IF7A, glutathione synthetase inactivation is more effective than that in the wild-ype and resembles that observed in Synechocystis
metabolism
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leaves of seedling grown in light for seven days contain about twofold higher glutamine synthetase activity than etiolated leaves. In both light and dark grown seedlings, total glutamine synthetase, isoforms GS1 and GS2 activities decline with plant age with more pronounced effect in leaves of etiolated seedlings. Isoform GS2 declines at a much faster rate than isoform GS1. Exposure of etiolated seedlings to light markedly enhances GS1 and GS2 activity, which is not affected by cycloheximide. Photosynthetic inhibitor dichlorophenyl dimethyl urea inhibits light dependent appearance of glutamine synthetase
metabolism
glutamine synthetase plays essential roles in nitrogen metabolism
metabolism
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the enzyme catalyzes the ATP-dependent synthesis of L-glutamine from glutamate and ammonia. GlnA1 is also involved in the synthesis of poly-L-glutamate/glutamine for the cell wall of pathogenic mycobacteria
metabolism
the glutamine synthetase/glutamate synthase cycle is considered as the major pathway for ammonium assimilation and regulation of nitrogen metabolism in higher plants
metabolism
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glutamine-starved GBM cells feed on astrocyte-derived glutamine. Only astrocytes demonstrate no net Gln consumption but rather, rapid Glu uptake, in line with the expression of excitatory amino acids transporters (EAAT) in this cell type. Under Gln starvation, Glu consumption is unaffected and paralleled by an equimolar net Gln efflux. The absence of Gln in the medium reduces intracellular Gln, but not Glu. Only 30-40% of both intracellular Glu and Gln are glucose-derived. Astrocytes maintain about 30% of the control level of intracellular Gln under Gln starvation, fitting with high enzyme expression. Astrocyte-derived Gln is the growth-supporting factor for Gln-starved glioblastoma cells
metabolism
glutamine synthetase is a key enzyme in plant nitrogen metabolism
metabolism
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presence of only one glutathione synthetase inactivation factor, 7A, encoded by open reading frame asl2329, gifA. Following addition of ammonium, expression of gifA is derepressed, leading to the synthesis of IF7A, and consequently, glutathione synthetase is inactivated. Upon ammonium removal, the glutathione synthetase activity returns to the initial level and IF7A becomes undetectable. Anabaena glutathione synthetase is not inactivated by Synechocystis IFs. In an Anabaena strain expressing a second inactivating factor, containing the amino-terminal part of IF17 from Synechocystis fused to IF7A, glutathione synthetase inactivation is more effective than that in the wild-ype and resembles that observed in Synechocystis
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metabolism
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glutamine synthetase plays essential roles in nitrogen metabolism
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metabolism
Mycobacterium tuberculosis ATCC 25618 / H37Rv
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the enzyme catalyzes the ATP-dependent synthesis of L-glutamine from glutamate and ammonia. GlnA1 is also involved in the synthesis of poly-L-glutamate/glutamine for the cell wall of pathogenic mycobacteria
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physiological function
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glutathione synthetase binds to transcription factor TnrA in its feedback-inhibited form, and also in its non-feedback-inhibited form, although less efficiently. TnrA forms either a stable soluble complex with GlnK in the absence of transmembrane ammonium transporter AmtB, or constitutively binds to glutathione synthetase in the absence of regulatuor GlnK. In vitro, the TnrA C-terminus is responsible for interactions with either glutathione synthetase or GlnK, and this region appears also to mediate proteolysis, suggesting that binding of GlnK or glutathione synthetase protects TnrA from degradation
physiological function
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the C-terminal domain peptide of nod26, a major intrinsic protein that constitutes the major protein component on the symbiosome membrane of N2-fixing soybean nodules, interacts with cytosolic glutamine synthetase GS1beta1. Recombinant soybean GS1beta1 binds the nod26 C-terminal domain with a 1:1 stoichiometry. GS1beta1 also binds to isolated symbiosome membranes, and this binding can be blocked by preincubation with the C-terminal peptide of nod26. In vivo the four cytosolic GS isoforms expressed in soybean nodules interact with full-length nod26
physiological function
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mice in which glutamine synthetase is selectively but completely eliminated from striated muscle are healthy and fertile. A 3-fold higher escape of ammonia reveals the absence of glutamine synthetase in muscle. After 20 h of fasting, glutamine synthetase-KO mice are not able to mount the 4fold increase in glutamine production across the hindquarter that is observed in control mice. Instead, muscle ammonia production is 5fold higher than in control mice. The fasting-induced metabolic changes are transient and return to fed levels at 36 h of fasting. Glucose consumption and lactate and ketone-body production are similar in glutamine synthetase-KO and control mice. Challenging glutamine synthetase-KO and control mice with intravenous ammonia in stepwise increments reveals that normal muscles can detoxify 2.5 mol ammonia/g muscle h in a muscle glutamine synthetase-dependent manner, with simultaneous accumulation of urea, whereas glutamine synthetase-KO mice respond with accumulation of glutamine and other amino acids, but not urea
physiological function
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study on glnA-1 mutant that produces reduced levels of glutamine synthetase. The mutant is able to grow in enriched 7H9 medium without glutamine supplementation.The glnA-1 strain contains no detectable poly-alpha-L-glutamine in the cell walls and shows marked sensitivity to different chemical and physical stresses such as lysozyme, SDS and sonication. The sensitivity of the mutant to antitubercular drugs, rifampicin and D-cycloserine, is also increased. The glnA-1 strain infects THP-1 cells with reduced efficiency and is also attenuated for growth in macrophages. A Mycobacterium smegmatis strain containing the Mycobacterium bovis glnA-1 gene survives longer in THP-1 cells than the wild-type strain and also produces cell wall-associated poly-alpha-L-glutamine. The mutant is not able to replicate in the organs of BALB/c mice and is cleared within 4-6 weeks of infection. Disruption of the glnA-1 gene adversely affects biofilm formation on polystyrene surfaces
physiological function
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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
hyperthermophilic archaea do not utilize glutamine synthetase predominantly for ammonia assimilation (the major pathway for ammonia assimilation is through glutamate dehydrogenase). The enzyme might play some role in ammonia assimilation under ammonia-starvation conditions
physiological function
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glutamine synthetase is the only human enzyme responsible for the de novo synthesis of glutamine, catalyzes the reaction of glutamate and ammonia. The enzyme influences sperm motility in mammals
physiological function
the enzyme glutamine synthetase plays an important role in the nitrogen metabolism of fish and in detoxifying ammonia, fish either decrease the production of ammonia, maintain/increase its excretion, or convert ammonia to less toxic products such as glutamine; the enzyme glutamine synthetase plays an important role in the nitrogen metabolism of fish and in detoxifying ammonia, fish either decrease the production of ammonia, maintain/increase its excretion, or convert ammonia to less toxic products such as glutamine; the enzyme glutamine synthetase plays an important role in the nitrogen metabolism of fish and in detoxifying ammonia, fish either decrease the production of ammonia, maintain/increase its excretion, or convert ammonia to less toxic products such as glutamine
physiological function
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glutamine synthetase plays a particularly important role in nitrogen metabolism and is the principal source of N for protein and nucleic acid synthesis
physiological function
glutamine synthetase catalyzes the synthesis of glutamine, providing nitrogen for the production of purines, pyrimidines, amino acids, and other compounds required in many pivotal cellular events. The enzyme is important in the development of the schistosome
physiological function
isozyme OsGS1;1 in the roots is unable to compensate for isozyme OsGS1;2 functions; isozyme OsGS1;2 is important in the primary assimilation of ammonium ions taken up by rice roots. Isozyme OsGS1;1 is unable to compensate for isozyme OsGS1;2 functions in 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. Gene OsGS1;1 expression is differently regulated by drought stresss in the two rice Oryza sativa varieties, effect of water deprivation varies with variety, degree and duration of stress
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; 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
physiological function
glutamine synthetase is a key enzyme for root nodule metabolism, and is a molecular target of nitric oxide in root nodules of Medicago truncatula and is regulated by tyrosine nitration. NO-mediated GS posttranslational inactivation is related to metabolite channeling to boost the nodule antioxidant defenses in response to NO; glutamine synthetase is a key enzyme for root nodule metabolism, and is a molecular target of nitric oxide in root nodules of Medicago truncatula and is regulated by tyrosine nitration. NO-mediated GS posttranslational inactivation is related to metabolite channeling to boost the nodule antioxidant defenses in response to NO
physiological function
Q4CN04
the enzyme is indispensable under excess ammonium conditions. It is required for the resistance of the organism to ammonium accumulation and evasion of the parasitophorous vacuole during host-cell infection. The enzyme contributes to the management of excess ammonium and uses it to form the amino acid glutamine. During its life cycle, the parasite invades mammalian host cells and transiently becomes enclosed in a tight vacuole, where it differentiates into the amastigote, an amino acid consumer stage. Amastigotes must escape from the vacuole into the host-cell cytoplasm to initiate intracellular replication. The inhibition of Trypanosoma cruzi glutamine synthetase aborts parasite evasion from the vacuole. The enzyme contributes to the control of ammonium produced by parasite metabolism, as ammonium increases the internal pH of the parasitophorous vacuole, making the enzymes for the Trypanosoma cruzi evasion process non-functional
physiological function
glutamine synthetase in nodule cytosol plays a major role in the assimilation of the ammonium produced by biological nitrogen fixation; glutamine synthetase in nodule cytosol plays a major role in the assimilation of the ammonium produced by biological nitrogen fixation
physiological function
glutamine synthetase is an important enzyme that catalyzes the conversion of L-glutamate into L-glutamine and ammonia in an energy dependent reaction with the simultaneous hydrolysis of ATP to ADP. In the cellular system, the enzyme plays an important role in nitrogen metabolism under ammonia-limiting conditions
physiological function
ammonium is incorporated into carbon skeletons by the sequential action of glutamine synthetase (GS) and glutamate synthase (GOGAT) in cyanobacteria. The activity of Synechocystis sp. PCC 6803 GS type I enzyme is controlled by protein-protein interactions with two intrinsically disordered inactivating factors (IFs): the 65-residue (IF7) and the 149-residue one (IF17), NMR sequence analysis and structure study, overview. The electrostatic-determined binding does not follow a kinetic two-state model, the binding is not diffusion-limited
physiological function
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the enzyme catalyzes the ATP-dependent synthesis of L-glutamine from glutamate and ammonia. GlnA1 is also involved in the synthesis of poly-L-glutamate/glutamine for the cell wall of pathogenic mycobacteria
physiological function
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glutamine synthetase-mediated autophagy explains the high sensitivity of beta-catenin-active hepatocellular carcinoma cells to sorafenib. beta-Catenin regulates the expression of glutamine synthetase and triggers a series of metabolic changes leading to induction of autophagy in hepatocellular carcinoma cells. Autophagy in beta-catenin-active Hep-3B and Hep-G2 cells is mediated by glutamine synthetase, as silencing of glutamine synthetase significantly reduced autophagic activity
physiological function
specific roles of the individual GS1 isogenes with respect to nitrogen remobilization, early seedling vigour, and final seed productivity. Isozyme Gln1-2 plays an important role in N remobilization for both seedling establishment and seed production in Arabidopsis thaliana; specific roles of the individual GS1 isogenes with respect to nitrogen remobilization, early seedling vigour, and final seed productivity. Isozymes Gln1-1 and Gln1-2 play specific roles in seed germination and seedling establishment in Arabidopsis thaliana
physiological function
glutamine synthetase catalyzes the formation of glutamine from glutamate in the presence of NH4+, ATP, and metal cations. The reaction is the rate-limiting step in the control of N-assimilation and N-recycling during growth and development of plants
physiological function
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the enzyme catalyses the ATP-dependent condensation of ammonium and L-glutamate, thus forming L-glutamine, ADP, phosphate and a proton. The enzyme is highly expressed and essential for the growth of the bacteria both in vitro and in vivo. The Mycobacterium tuberculosis enzyme plays an important role in cell wall biosynthesis, specifically via the production of a poly-L-glutamate-glutamine component found exclusively in pathogenic mycobacteria. Extracellular Mycobacterium tuberculosis enzyme may also affect pH modulation in phagosomes and consequently prevent phagosome-lysosome fusion
physiological function
Gln synthetase catalyzes the assimilation of ammonium into Gln and constitutes as such a central component of the N assimilatory pathway in plants. GS2 is the predominant GS isoform in leaves of vegetatively growing plants. In shoots, both GS1 and GS2 contribute to ammonium assimilation into Gln; Gln synthetase catalyzes the assimilation of ammonium into Gln and constitutes as such a central component of the N assimilatory pathway in plants. In shoots, both GS1 and GS2 contribute to ammonium assimilation into Gln; Gln synthetase catalyzes the assimilation of ammonium into Gln and constitutes as such a central component of the N assimilatory pathway in plants. In shoots, both GS1 and GS2 contribute to ammonium assimilation into Gln; Gln synthetase catalyzes the assimilation of ammonium into Gln and constitutes as such a central component of the N assimilatory pathway in plants. In shoots, both GS1 and GS2 contribute to ammonium assimilation into Gln. Isozyme Gln-1;2 is essential for ammonium assimilation and amino acid synthesis. Gln-1;2 is the main isozyme contributing to shoot GS1 activity in vegetative growth stages and can be up-regulated to relieve ammonium toxicity
physiological function
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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
physiological function
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glutamine synthetase is one of the key enzymes in nitrogen assimilation, ligating-free ammonium to glutamate to form glutamine and it is therefore crucial for plant growth and productivity
physiological function
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glutamine synthetase is an important enzyme that catalyzes the conversion of L-glutamate into L-glutamine and ammonia in an energy dependent reaction with the simultaneous hydrolysis of ATP to ADP. In the cellular system, the enzyme plays an important role in nitrogen metabolism under ammonia-limiting conditions
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physiological function
Mycobacterium tuberculosis ATCC 25618 / H37Rv
-
the enzyme catalyses the ATP-dependent condensation of ammonium and L-glutamate, thus forming L-glutamine, ADP, phosphate and a proton. The enzyme is highly expressed and essential for the growth of the bacteria both in vitro and in vivo. The Mycobacterium tuberculosis enzyme plays an important role in cell wall biosynthesis, specifically via the production of a poly-L-glutamate-glutamine component found exclusively in pathogenic mycobacteria. Extracellular Mycobacterium tuberculosis enzyme may also affect pH modulation in phagosomes and consequently prevent phagosome-lysosome fusion; the enzyme catalyzes the ATP-dependent synthesis of L-glutamine from glutamate and ammonia. GlnA1 is also involved in the synthesis of poly-L-glutamate/glutamine for the cell wall of pathogenic mycobacteria
-
physiological function
-
glutamine synthetase plays a particularly important role in nitrogen metabolism and is the principal source of N for protein and nucleic acid synthesis
-
physiological function
-
hyperthermophilic archaea do not utilize glutamine synthetase predominantly for ammonia assimilation (the major pathway for ammonia assimilation is through glutamate dehydrogenase). The enzyme might play some role in ammonia assimilation under ammonia-starvation conditions
-
physiological function
-
the enzyme is indispensable under excess ammonium conditions. It is required for the resistance of the organism to ammonium accumulation and evasion of the parasitophorous vacuole during host-cell infection. The enzyme contributes to the management of excess ammonium and uses it to form the amino acid glutamine. During its life cycle, the parasite invades mammalian host cells and transiently becomes enclosed in a tight vacuole, where it differentiates into the amastigote, an amino acid consumer stage. Amastigotes must escape from the vacuole into the host-cell cytoplasm to initiate intracellular replication. The inhibition of Trypanosoma cruzi glutamine synthetase aborts parasite evasion from the vacuole. The enzyme contributes to the control of ammonium produced by parasite metabolism, as ammonium increases the internal pH of the parasitophorous vacuole, making the enzymes for the Trypanosoma cruzi evasion process non-functional
-
additional information
the Bacillus subtilis enzyme undergoes dramatic intersubunit conformational alterations during formation of the transition state. Structure-function relationship, overview
additional information
the enzyme sequence contains a classic beta-grasp domain and a catalytic domain of glutamine synthetase
additional information
-
the enzyme sequence contains a classic beta-grasp domain and a catalytic domain of glutamine synthetase
additional information
Val161 in GS1beta1 is the key residue responsible for the heat stability
additional information
Val161 in GS1beta1 is the key residue responsible for the heat stability
additional information
structure-function relationships of wild-type and mutant enzymes, ligand molecular docking, homology structure modeling using the crystal structure of the enzyme from Bacillus subtilis, PDB ID 4LNF, as a template, overview
additional information
-
structure-function relationships of wild-type and mutant enzymes, ligand molecular docking, homology structure modeling using the crystal structure of the enzyme from Bacillus subtilis, PDB ID 4LNF, as a template, overview
additional information
-
enzyme structure-activity relationship, overview
additional information
the C-terminal extension peptide of plastid-located glutamine synthetase from Medicago truncatula is crucial for enzyme activity but needless for protein import into the plastids. The C-terminal extension peptide does not affect the solubility or the stability of the protein but likely the interaction of the enzyme with its substrates. The first 49 amino acids of the N-terminus are predicted to be the transit peptide, the sorting signal for targeting nucleus-encoded proteins to the plastids, which is cleaved during the import
additional information
-
the Bacillus subtilis enzyme undergoes dramatic intersubunit conformational alterations during formation of the transition state. Structure-function relationship, overview
-
additional information
-
structure-function relationships of wild-type and mutant enzymes, ligand molecular docking, homology structure modeling using the crystal structure of the enzyme from Bacillus subtilis, PDB ID 4LNF, as a template, overview
-
additional information
Mycobacterium tuberculosis ATCC 25618 / H37Rv
-
enzyme structure-activity relationship, overview
-
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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 + 3-aminopentanedioate + hydroxylamine
ADP + phosphate + gamma-glutamylhydroxamate
the enzyme is more selective for L-glutamate (alpha-glutamate) than 3-aminopentanedioate (beta-glutamate) as a substrate
-
-
?
ATP + L-Glu + methylamine
ADP + phosphate + L-Gln + ?
-
7% of the activity with NH4+, at pH 8.0, activated with 30 mM Mg2+
-
-
?
ATP + L-glutamate + hydroxylamine
ADP + phosphate + gamma-L-glutamyl hydroxamate + NH3
-
in presence of Mn2+
-
-
?
ATP + L-glutamate + hydroxylamine
ADP + phosphate + L-gamma-glutamylhydroxamate
-
photometric determination of GS activity based on formation of an L-gamma-glutamylhydroxamate ferric chloride complex using hydroxylamine instead of ammonia
-
-
?
L-Gln + hydroxylamine + ADP
L-gamma-glutamylhydroxamate + NH4+ + ?
-
-
-
?
L-glutamine + hydroxylamine + ADP
gamma-glutamylhydroxamate + NH3 + ?
-
partial reverse reaction
-
-
?
TTP + L-Glu + NH4+
TDP + phosphate + L-Gln
-
10% of the activity relative to ATP
-
-
-
2 ATP + 2 L-glutamate + 2 NH3
2 ADP + 2 phosphate + D-glutamine + D-isoglutamine
GlnA2 catalyses the synthesis of D-glutamine and D-isoglutamine and is essential for bacterial growth
-
-
?
2 ATP + 2 L-glutamate + 2 NH3
2 ADP + 2 phosphate + D-glutamine + D-isoglutamine
GlnA2 catalyses the synthesis of D-glutamine and D-isoglutamine
-
-
?
2 ATP + 2 L-glutamate + 2 NH3
2 ADP + 2 phosphate + D-glutamine + D-isoglutamine
GlnA2 catalyses the synthesis of D-glutamine and D-isoglutamine and is essential for bacterial growth
-
-
?
2 ATP + 2 L-glutamate + 2 NH3
2 ADP + 2 phosphate + D-glutamine + D-isoglutamine
GlnA2 catalyses the synthesis of D-glutamine and D-isoglutamine
-
-
?
ADP + L-glutamine + hydroxylamine
gamma-glutamylhydroxamate + ?
-
-
-
r
ADP + L-glutamine + hydroxylamine
gamma-glutamylhydroxamate + ?
-
-
-
r
ADP + phosphate + L-glutamine
ATP + L-glutamate + NH3
-
-
-
r
ATP + 3-aminopentanedioate + hydroxylamine
ADP + phosphate + ?
the enzyme is more selective for L-glutamate (alpha-glutamate) than for 3-aminopentanedioate (beta-glutamate) as a substrate
-
-
?
ATP + 3-aminopentanedioate + hydroxylamine
ADP + phosphate + ?
the enzyme is more selective for L-glutamate (alpha-glutamate) than for 3-aminopentanedioate (beta-glutamate) as a substrate
-
-
?
ATP + 3-aminopentanedioate + hydroxylamine
ADP + phosphate + ?
-
the activity with is 3-aminopentanedioate (beta-glutamate) is 7fold less than the rate obtained with alpha-glutamate
-
-
?
ATP + adipate + NH4+
ADP + phosphate + ?
Q4CN04
75% of the activity observed with glutamate
-
-
?
ATP + adipate + NH4+
ADP + phosphate + ?
Q4CN04
75% of the activity observed with glutamate
-
-
?
ATP + gamma-aminobutyrate + NH4+
ADP + phosphate + ?
Q4CN04
50% of the activity observed with glutamate
-
-
?
ATP + gamma-aminobutyrate + NH4+
ADP + phosphate + ?
Q4CN04
50% of the activity observed with glutamate
-
-
?
ATP + glutamate + NH4+
ADP + phosphate + L-glutamine
-
central enzyme of nitrogen metabolism
-
-
r
ATP + glutamate + NH4+
ADP + phosphate + L-glutamine
-
central enzyme of nitrogen metabolism, ammonia assimilation
-
-
?
ATP + glutamate + NH4+
ADP + phosphate + L-glutamine
-
central enzyme of nitrogen metabolism, ammonia assimilation
-
-
?
ATP + glutamate + NH4+
ADP + phosphate + L-glutamine
-
central enzyme of nitrogen metabolism, elimination of glutamate from animal brain
-
-
?
ATP + glutamate + NH4+
ADP + phosphate + L-glutamine
-
central enzyme of nitrogen metabolism
-
-
?
ATP + glutamate + NH4+
ADP + phosphate + L-glutamine
-
central enzyme of nitrogen metabolism, ammonia assimilation
-
-
?
ATP + glutamate + NH4+
ADP + phosphate + L-glutamine
-
-
-
-
r
ATP + glutamate + NH4+
ADP + phosphate + L-glutamine
-
central enzyme of nitrogen metabolism
-
-
r
ATP + glutamate + NH4+
ADP + phosphate + L-glutamine
-
-
-
-
r
ATP + glutamate + NH4+
ADP + phosphate + L-glutamine
-
central enzyme of nitrogen metabolism
-
-
r
ATP + glutamate + NH4+
ADP + phosphate + L-glutamine
-
central enzyme of nitrogen metabolism, assimilation of ammonia for protein synthesis
-
-
?
ATP + glutamate + NH4+
ADP + phosphate + L-glutamine
-
central enzyme of nitrogen metabolism
-
-
r
ATP + glutamate + NH4+
ADP + phosphate + L-glutamine
-
central enzyme of nitrogen metabolism, elimination of glutamate from animal brain
-
-
?
ATP + glutamate + NH4+
ADP + phosphate + L-glutamine
-
central enzyme of nitrogen metabolism
-
-
?
ATP + glutamate + NH4+
ADP + phosphate + L-glutamine
-
central enzyme of nitrogen metabolism
-
-
?
ATP + glutamate + NH4+
ADP + phosphate + L-glutamine
-
central enzyme of nitrogen metabolism, elimination of glutamate from animal brain
-
-
?
ATP + glutamate + NH4+
ADP + phosphate + L-glutamine
-
-
-
-
?
ATP + glutamate + NH4+
ADP + phosphate + L-glutamine
-
central enzyme of nitrogen metabolism, postulated to be necessary for the synthesis of the cell wall component poly(L-glutamine-L-glutamate)
-
-
?
ATP + glutamate + NH4+
ADP + phosphate + L-glutamine
-
-
-
-
?
ATP + glutamate + NH4+
ADP + phosphate + L-glutamine
-
central enzyme of nitrogen metabolism, ammonia assimilation
-
-
?
ATP + glutamate + NH4+
ADP + phosphate + L-glutamine
-
central enzyme of nitrogen metabolism, ammonia assimilation
-
-
r
ATP + glutamate + NH4+
ADP + phosphate + L-glutamine
-
central enzyme of nitrogen metabolism, assimilation of ammonia
-
-
r
ATP + glutamate + NH4+
ADP + phosphate + L-glutamine
-
central enzyme of nitrogen metabolism, key enzyme of glutamate metabolism, reduction of local concentrations of glutamate and ammonia
-
-
?
ATP + glutamate + NH4+
ADP + phosphate + L-glutamine
-
central enzyme of nitrogen metabolism
-
-
?
ATP + glutamate + NH4+
ADP + phosphate + L-glutamine
-
-
-
r
ATP + glutamate + NH4+
ADP + phosphate + L-glutamine
central enzyme of nitrogen metabolism
-
-
r
ATP + glutamate + NH4+
ADP + phosphate + L-glutamine
-
central enzyme of nitrogen metabolism
-
-
?
ATP + glutamate + NH4+
ADP + phosphate + L-glutamine
-
central enzyme of nitrogen metabolism
-
-
?
ATP + glutamate + NH4+
ADP + phosphate + L-glutamine
central enzyme of nitrogen metabolism
-
-
r
ATP + glutamate + NH4+
ADP + phosphate + L-glutamine
-
central enzyme of nitrogen metabolism, provides glutamine for biosynthesis, ammonia assimilation
-
-
?
ATP + glutamate + NH4+
ADP + phosphate + L-glutamine
central enzyme of nitrogen metabolism, involved in nitrogen assimilation pathway
-
-
?
ATP + L-Glu + ethylamine
ADP + phosphate + ?
-
slightly effective
-
-
-
ATP + L-Glu + ethylamine
ADP + phosphate + ?
-
slightly effective
-
-
-
ATP + L-Glu + ethylamine
ADP + phosphate + ?
-
slightly effective
-
-
-
ATP + L-Glu + ethylamine
ADP + phosphate + ?
-
slightly effective
-
-
-
ATP + L-Glu + ethylamine
ADP + phosphate + ?
-
slightly effective
-
-
-
ATP + L-Glu + ethylamine
ADP + phosphate + L-Gln + ?
-
1% of the activity with NH4+, at pH 8.0, activated with 30 mM Mg2+
-
-
?
ATP + L-Glu + ethylamine
ADP + phosphate + L-Gln + ?
-
1% of the activity with NH4+, at pH 8.0, activated with 30 mM Mg2+
-
-
?
ATP + L-Glu + hydroxylamine
ADP + phosphate + gamma-glutamyl hydroxamate
-
59% of the activity relative to NH4+
-
-
-
ATP + L-Glu + hydroxylamine
ADP + phosphate + gamma-glutamyl hydroxamate
-
59% of the activity relative to NH4+
-
-
-
ATP + L-Glu + hydroxylamine
ADP + phosphate + gamma-glutamyl hydroxamate
-
13% of the activity relative to NH4+
-
-
-
ATP + L-Glu + hydroxylamine
ADP + phosphate + gamma-glutamyl hydroxamate
-
13% of the activity relative to NH4+
-
-
-
ATP + L-Glu + hydroxylamine
ADP + phosphate + gamma-glutamyl hydroxamate
-
10% of the activity relative to NH4+
-
-
-
ATP + L-Glu + hydroxylamine
ADP + phosphate + gamma-glutamyl hydroxamate
-
10% of the activity relative to NH4+
-
-
-
ATP + L-Glu + hydroxylamine
ADP + phosphate + gamma-glutamyl hydroxamate
-
-
-
-
ATP + L-Glu + hydroxylamine
ADP + phosphate + gamma-glutamyl hydroxamate
-
-
-
?
ATP + L-Glu + hydroxylamine
ADP + phosphate + L-Gln + ?
-
32% of the activity with NH4+
-
-
?
ATP + L-Glu + hydroxylamine
ADP + phosphate + L-Gln + ?
-
32% of the activity with NH4+
-
-
?
ATP + L-Glu + methylamine
ADP + phosphate + ?
-
slightly effective
-
-
-
ATP + L-Glu + methylamine
ADP + phosphate + ?
-
slightly effective
-
-
-
ATP + L-Glu + methylamine
ADP + phosphate + ?
-
slightly effective
-
-
-
ATP + L-Glu + methylamine
ADP + phosphate + ?
-
slightly effective
-
-
-
ATP + L-Glu + methylamine
ADP + phosphate + ?
-
slightly effective
-
-
-
ATP + L-Glu + methylamine
ADP + phosphate + ?
-
slightly effective
-
-
-
ATP + L-Glu + NH4+
?
-
glutamate synthetase cycle provides the only efficient pathway for the conversion of inorganic nitrogen to the organic form
-
-
-
ATP + L-Glu + NH4+
?
-
kinetic regulation of this enzyme may play a significant role in ammonia detoxication and rate of formation of Gln-derived neurotransmitters in fish brain
-
-
-
ATP + L-Glu + NH4+
?
-
glutamine produced by the enzyme serves as a source of nitrogen atoms in the biosynthesis of all amino acids, purine and pyrimidine nucleotides, of glucosamine 6-phosphate, 4-aminobenzoic acid, and of nicotinamide derivatives. Glutamine synthetase links the assimilation of NH4+ with biosynthetic pathways leading to the formation of proteins, nucleic acids, complex polysaccharides, and different coenzymes
-
-
-
ATP + L-Glu + NH4+
?
-
roles of the enzyme in pathogenesis of Mycobacterium tuberculosis infection: 1. synthesis of Glu, that is a major component of the cell wall of pathogenic mycobacteria, 2. modulation of the NH4+ level in the Mycobacterium tuberculosis phagosome
-
-
-
ATP + L-Glu + NH4+
?
-
first step at which nitrogen is brought into cellular metabolism, the product Glu, a source of nitrogen in the biosynthesis of many other metabolites
-
-
-
ATP + L-Glu + NH4+
ADP + phosphate + L-Gln
-
enzyme form EII is almost absolutely specific for ATP, but enzyme form E1 can also use ITP, GTP and UTP
-
-
-
ATP + L-Glu + NH4+
ADP + phosphate + L-Gln
-
-
-
-
-
ATP + L-Glu + NH4+
ADP + phosphate + L-Gln
-
isoenzyme GS1b (EC 6.3.1.2) in concert with NADH-dependent GOGAT (EC 1.4.1.14) constitute the major route of assimilation of ammonium derived from reserve mobilization and glutamic acid/glutamine synthesis in germinating Medicago truncatula seeds. However, during post-germinative growth, although germination is held in darkness, expression of GS2 and Fd-GOGAT (EC 1.4.7.1) increases and expression of GS1b decreases in cotyledons but not in the embryo axis
-
-
?
ATP + L-Glu + NH4+
ADP + phosphate + L-Gln
serves for assimilation of ammonium in rice root, and ameliorates the toxic effect of ammonium excess
-
-
?
ATP + L-Glu + NH4+
ADP + phosphate + L-Gln
-
enzyme can bind 8 M of ATP per mol of enzyme
-
-
-
ATP + L-Glu + NH4+
ADP + phosphate + L-Gln
-
1 mol of enzyme can bind 5 M ATP
-
-
-
ATP + L-Glu + NH4+
ADP + phosphate + L-Gln
-
-
-
-
-
ATP + L-glutamate + hydroxylamine
ADP + phosphate + gamma-L-glutamylhydroxamate
the enzyme is more selective for L-glutamate (alpha-glutamate) than for 3-aminopentanedioate (beta-glutamate) as a substrate
-
-
?
ATP + L-glutamate + hydroxylamine
ADP + phosphate + gamma-L-glutamylhydroxamate
the enzyme is more selective for L-glutamate (alpha-glutamate) than for 3-aminopentanedioate (beta-glutamate) as a substrate
-
-
?
ATP + L-glutamate + hydroxylamine
ADP + phosphate + gamma-L-glutamylhydroxamate
the enzyme is more selective for L-glutamate (alpha-glutamate) than for 3-aminopentanedioate (beta-glutamate) as a substrate
-
-
?
ATP + L-glutamate + hydroxylamine
ADP + phosphate + gamma-L-glutamylhydroxamate
-
the activity with L-glutamate is 7fold higher than the rate obtained with 3-aminopentanedioate (beta-glutamate)
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
senescence-specific downregulation of plastidic glutamine synthetase, this is retarded by fertilisation of plants with nitrate or ammonium, but not urea, at the onset of leaf senescence, overview
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
-
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
the enzyme is involved in the regulation of the nitrogen metabolism, overview
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
the enzyme is involved in the signal transduction for regulation of the nitrogen metabolism, 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, phosphate 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, phosphate 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, phosphate and ADP
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
dogs show altered L-glutamate distribution and reduced enzyme content in primary glaucoma and ischemia, overview
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
the enzyme activity eliminates cytotoxic ammonia, at the same time converting neurotoxic glutamate to harmless glutamine, enzyme activity defects are linked to neurodegenerative disorders, such as Alzheimer's disease, overview
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
loop movements near the active site generate more closed forms of the eukaryotic enzyme when substrates are bound
-
-
?
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
-
-
?
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
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
the enzyme is involved in the regulation of nitrogen metabolism and nitrogen fixation via the incorporation of ammonia the glutamine synthetase/glutamate synthase, GS/GOGAT, pathway, overview
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
GlnA1 is essential for survival in vitro, while GlnA2 is probably not
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
the enzyme expressed in the plancenta is actively involved in the provision of glutamine to the fetus
-
-
?
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
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
-
-
r
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
isozyme GS2 is involved in osmoregulation of the cells and is part of the chloride regulon of Halobacillus halophilus, overview. At moderate salinities Halobacillus halophilus mainly accumulates glutamine and glutamate to adjust turgor, while it produces proline at high salinity. Halobacillus halophilus also shifts its osmolyte strategy at the transition from the exponential to the stationary phase where proline is exchanged by ectoine, regulation mechanism, overview
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
-
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
extracellular glutamate, loss of the glutamate-metabolizing enzyme glutamine synthetase and proliferation of astrocytes are associated with mesial temporal lobe epilepsy, MTLE. Glial proliferation, i.e. gliosis, contributes to the epileptogenicity of the human hippocampus in MTLE, levels of extracellular glutamate are more than five-fold increased in the MTLE hippocampus, glutamate-glutamine cycle, overview
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
glutamine also acts as a signaling molecule, physiological functions of glutamine, overview
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
glutamine synthetase is essential for proliferation of fetal skin fibroblasts
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
the enzyme activity eliminates cytotoxic ammonia, at the same time converting neurotoxic glutamate to harmless glutamine, enzyme activity defects are linked to neurodegenerative disorders, such as Alzheimer's disease, 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, phosphate and ADP
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
loop movements near the active site generate more closed forms of the eukaryotic enzyme when substrates are bound
-
-
?
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
E9B8P8
-
-
-
r
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
the enzyme plays a pivotal role in the mammalian brain where it allows neurotransmitter glutamate recycling within astroglia
-
-
?
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
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
-
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
-
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
GlnA1 catalyses the synthesis of L-glutamine and is nonessential for bacterial growth
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
glnA1 is essential for Mycobacterium tuberculosis virulence
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
GlnA3 catalyses the synthesis of L-glutamine and are nonessential for bacterial growth
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
GlnA4 catalyses the synthesis of L-glutamine and are nonessential for bacterial growth
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
only GlnA1 appears to be the functional enzyme involved in nitrogen metabolism in vivo in the organism, the enzyme is involved in the regulation of nitrogen metabolism and nitrogen fixation via the incorporation of ammonia the glutamine synthetase/glutamate synthase, GS/GOGAT, pathway, overview. GlnA1 is associated with virulence and pathogenicity in Mycobacterium tuberculosis
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ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
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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
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ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
amino acid binding site and structure, overview
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ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
GlnA1 catalyses the synthesis of L-glutamine
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ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
GlnA3 catalyses the synthesis of L-glutamine
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?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
GlnA4 catalyses the synthesis of L-glutamine
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ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
Mycobacterium tuberculosis ATCC 25618 / H37Rv
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r
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
Mycobacterium tuberculosis ATCC 25618 / H37Rv
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?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
-
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
only GlnA1 appears to be the functional enzyme involved in nitrogen metabolism in vivo in the organism, the enzyme is involved in the regulation of nitrogen metabolism and nitrogen fixation via the incorporation of ammonia the glutamine synthetase/glutamate synthase, GS/GOGAT, pathway, overview. GlnA1 is associated with virulence and pathogenicity in Mycobacterium tuberculosis
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-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
-
-
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?
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
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-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
GlnA1 catalyses the synthesis of L-glutamine and is nonessential for bacterial growth
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?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
GlnA1 catalyses the synthesis of L-glutamine
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?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
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?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
glnA1 is essential for Mycobacterium tuberculosis virulence
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?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
amino acid binding site and structure, overview
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-
?
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
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-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
-
-
?
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
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?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
the enzyme is involved in regulation of ammonium assimilation requirements during tree development, regulatory mechanism for the transcriptional control of the spatial distribution of cytosolic GS isoforms in pine, overview
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?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
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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
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-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
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GSIII-1, and GSIII-2, no activity of GSI
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?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
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GSIII-1, and GSIII-2, no activity of GSI
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?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
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-
-
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?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
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brain injuries are usually associated with an increase in the expression of the glutamate-converting enzyme glutamine synthetase
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?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
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enzyme regulation involving L-glutamate uptake, Ca2+, and P2X7 receptors, overview
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?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
the astrocyte-specific glutamine synthetase plays a key role in glutamate recycling and gamma-aminobutyric acid metabolism, it is involved in nitrosative stress response in the brain, overview
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?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
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the enzyme is involved in development of mesial temporal lobe epilepsy, MTLE
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ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
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upon tissue damage, the enzyme endogenous GS is released from glial cells in the extracellular space, where it converts glutamate into glutamine, which is a nonneurotoxic amino acid
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?
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
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?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
-
-
?
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
-
-
?
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
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?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
Sorghum sp.
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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
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?
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
only GlnA1 appears to be the functional enzyme involved in nitrogen metabolism in vivo in the organism, the enzyme is involved in the regulation of nitrogen metabolism and nitrogen fixation via the incorporation of ammonia the glutamine synthetase/glutamate synthase, GS/GOGAT, pathway, the transcriptional regulator GlnR is involved in regulation of the enzyme activity and is able to function as both an activator and repressor of transcription, overview. GSII probably plays and important role in mycelial development as well as differential glnA1 and glnII transcriptional regulation
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ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
glutamine synthetase catalyzes the ATP-dependent conversion of ammonia and glutamate to glutamine in the pericentral zone
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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
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?