Information on EC 6.3.1.2 - Glutamate-ammonia ligase

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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea

EC NUMBER
COMMENTARY
6.3.1.2
-
RECOMMENDED NAME
GeneOntology No.
Glutamate-ammonia ligase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
ATP + L-glutamate + NH3 = ADP + phosphate + L-glutamine
show the reaction diagram
-
-
-
-
ATP + L-glutamate + NH3 = ADP + phosphate + L-glutamine
show the reaction diagram
ordered three-reactant system with the binding order: NH4+, L-Glu and ATP
-
ATP + L-glutamate + NH3 = ADP + phosphate + L-glutamine
show the reaction diagram
reaction mechanism
-
ATP + L-glutamate + NH3 = ADP + phosphate + L-glutamine
show the reaction diagram
reaction mechanism and transition state analogue, overview
-
ATP + L-glutamate + NH3 = ADP + phosphate + L-glutamine
show the reaction diagram
reaction mechanism
-
ATP + L-glutamate + NH3 = ADP + phosphate + L-glutamine
show the reaction diagram
reaction mechanism
P15104
ATP + L-glutamate + NH3 = ADP + phosphate + L-glutamine
show the reaction diagram
reaction mechanism; reaction mechanism
-, P13564
ATP + L-glutamate + NH3 = ADP + phosphate + L-glutamine
show the reaction diagram
reaction mechanism
P15105
ATP + L-glutamate + NH3 = ADP + phosphate + L-glutamine
show the reaction diagram
reaction mechanism
-
ATP + L-glutamate + NH3 = ADP + phosphate + L-glutamine
show the reaction diagram
reaction mechanism
P09606
ATP + L-glutamate + NH3 = ADP + phosphate + L-glutamine
show the reaction diagram
reaction mechanism
P0A1P6
ATP + L-glutamate + NH3 = ADP + phosphate + L-glutamine
show the reaction diagram
reaction mechanism
-
ATP + L-glutamate + NH3 = ADP + phosphate + L-glutamine
show the reaction diagram
reaction mechanism
P77961
ATP + L-glutamate + NH3 = ADP + phosphate + L-glutamine
show the reaction diagram
reaction mechanism
-
ATP + L-glutamate + NH3 = ADP + phosphate + L-glutamine
show the reaction diagram
random catalysis mechanism where the binding order of certain substrates is kinetically preferred by the enzyme
A0MZ70
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Acid amide hydrolysis
-
-
carboxylic
-
PATHWAY
KEGG Link
MetaCyc Link
Alanine, aspartate and glutamate metabolism
-
ammonia assimilation cycle I
-
ammonia assimilation cycle II
-
Arginine and proline metabolism
-
glutamine biosynthesis I
-
glutamine biosynthesis III
-
Glyoxylate and dicarboxylate metabolism
-
Metabolic pathways
-
Microbial metabolism in diverse environments
-
nitrate reduction II (assimilatory)
-
nitrate reduction V (assimilatory)
-
nitrate reduction VI (assimilatory)
-
Nitrogen metabolism
-
SYSTEMATIC NAME
IUBMB Comments
L-Glutamate:ammonia ligase (ADP-forming)
Also acts, more slowly, on 4-methylene-L-glutamate (cf. EC 6.3.1.7 4-methyleneglutamate---ammonia ligase).
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
ATP glutamate-ammonia ligase
-
-
Chloroplast GS2
-
-
-
-
Clone lambda-GS28
-
-
-
-
Clone lambda-GS31
-
-
-
-
Clone lambda-GS8
-
-
-
-
Cytoplasmic GS3
-
-
-
-
Cytosolic GS1
-
-
-
-
gamma-glutamyl:ammonia ligase
Q8HZM5
-
gamma-glutamyl:ammonia ligase
-
-
Gln isozyme alpha
-
-
-
-
Gln isozyme beta
-
-
-
-
Gln isozyme gamma
-
-
-
-
GLN1,1
Q56WN1
-
GLN1,4
Q9FMD9
-
GlnA
Q60182
gene name
GlnA
O08467
gene name
GlnA
Pyrococcus sp. KOD1
O08467
gene name
-
GlnA
-
gene name
GlnA
-
gene name
-
GlnA
Q9RHZ1
-
GlnA1
-
gene name
GLUL
P15104
-
Glutamate--ammonia ligase
-
-
-
-
Glutamine synthetase
-
-
-
-
Glutamine synthetase
Q43127
-
Glutamine synthetase
-
-
Glutamine synthetase
P12425
-
Glutamine synthetase
-
-
Glutamine synthetase
-
-
Glutamine synthetase
-
-
Glutamine synthetase
Q8HZM5
-
Glutamine synthetase
-
-
Glutamine synthetase
-
-
Glutamine synthetase
-
-
Glutamine synthetase
-
-
Glutamine synthetase
Q1MXG4
-
Glutamine synthetase
-
-
Glutamine synthetase
-
-
Glutamine synthetase
-
-
Glutamine synthetase
A8WCU3
-
Glutamine synthetase
-
-
Glutamine synthetase
Q0E5H7
-
Glutamine synthetase
-
-
Glutamine synthetase
P15104
-
Glutamine synthetase
-
-
Glutamine synthetase
P13564
-
Glutamine synthetase
-
-
Glutamine synthetase
-
-
Glutamine synthetase
-
-
Glutamine synthetase
P15105
-
Glutamine synthetase
-
-
Glutamine synthetase
Mycobacterium smegmatis VT301
-
-
-
Glutamine synthetase
-
-
Glutamine synthetase
P0A590
-
Glutamine synthetase
P64246, Q07752, Q33342
-
Glutamine synthetase
-
-
Glutamine synthetase
-
-
Glutamine synthetase
-
-
Glutamine synthetase
-
-
Glutamine synthetase
P81107
-
Glutamine synthetase
-
-
Glutamine synthetase
-
-
Glutamine synthetase
P09606
-
Glutamine synthetase
-
-
Glutamine synthetase
-
-
Glutamine synthetase
-
-
Glutamine synthetase
-
-
Glutamine synthetase
Sorghum sp., Spinacia oleracea
-
-
Glutamine synthetase
P15106
-
Glutamine synthetase
P46410
-
Glutamine synthetase
P77961
-
Glutamine synthetase
-
-
Glutamine synthetase
-
-
Glutamine synthetase
Q45NB2, Q45NB3, Q45NB4, Q45NB5, Q45NB6, Q45NB7, Q6RUI9, Q6RUJ0, Q6RUJ1, Q6RUJ2
-
Glutamine synthetase
-
-
Glutamine synthetase
-
-
Glutamine synthetase
-
-
Glutamine synthetase
P25462
-
glutamine synthetase I
P36687
-
glutamine synthetase I
-
-
glutamine synthetase type II
P04771
-
glutamine synthetase type III
-
-
Glutamylhydroxamic synthetase
-
-
-
-
GS
-
-
-
-
GS type I
-
-
GS(1)
-
-
-
-
GS-II
P04771
-
GS1
-
-
-
-
GS1
-
cytoplasmic enzyme form
GS1
P38562
-
GS1 kinase
-
-
GS1-1
-
-
GS107
-
-
-
-
GS112
-
-
-
-
GS117
-
-
-
-
GS122
-
-
-
-
GS1a
-
-
GS2
-
-
-
-
GS2
-
chloroplastic enzyme form
GS2
P38562
-
GSI
-
-
-
-
GSII
-
-
-
-
GSIII
-
-
-
-
Isozyme delta
-
-
-
-
L-glutamate:ammonia ligase
-
-
L-glutamate:ammonia ligase (ADP-forming)
-
-
L-Glutamine synthetase
-
-
-
-
L-Glutamine synthetase
-
-
N47/N48
-
-
-
-
OsGLN1,1
P14656
-
OsGLN1,2
P14654
-
protein transacetylase
-
-
protein transacetylase
Mycobacterium smegmatis VT301
-
-
-
S2205/S2287
-
-
-
-
SSO0366
-
gene name
SSO0366
-
gene name
-
Synthetase, glutamine
-
-
-
-
TAase
Mycobacterium smegmatis VT301
-
-
-
type I glutamine synthetase
O85177
-
type III glutamine synthetase
-
-
CAS REGISTRY NUMBER
COMMENTARY
9023-70-5
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
spiny mouse
-
-
Manually annotated by BRENDA team
Anabaena sp. PCC 7120
-
-
-
Manually annotated by BRENDA team
strains SA0 and SA1, SA1 carries a single amino acid mutation Y183C and is defective in ammonia assimilation below concentrations of 0.5 mM
-
-
Manually annotated by BRENDA team
cv. Columbia
UniProt
Manually annotated by BRENDA team
isoenzyme GLN1,1
SwissProt
Manually annotated by BRENDA team
isoenzyme GLN1,2
-
-
Manually annotated by BRENDA team
isoenzyme GLN1,3
SwissProt
Manually annotated by BRENDA team
isoenzyme GLN1,4
SwissProt
Manually annotated by BRENDA team
isoenzyme GLN1,4
-
-
Manually annotated by BRENDA team
Archaeoglobus fulgidus VC-16
-
SwissProt
Manually annotated by BRENDA team
Azolla sp.
a genus of aquatic ferns, which harbors the cyanobacterium Anabaena azollae in specialized cavities formed in its leaves
-
-
Manually annotated by BRENDA team
strain Sp245, nitrogen-fixing plant-associated bacterium
-
-
Manually annotated by BRENDA team
strain Sp245, nitrogen-fixing plant-associated bacterium
-
-
Manually annotated by BRENDA team
two enzyme forms: EI and EII
-
-
Manually annotated by BRENDA team
two isoforms: E-I and E-II
-
-
Manually annotated by BRENDA team
gene glnA
-
-
Manually annotated by BRENDA team
strain KN2
-
-
Manually annotated by BRENDA team
Bacillus subtilis KN2
strain KN2
-
-
Manually annotated by BRENDA team
isozyme GS2
-
-
Manually annotated by BRENDA team
Bifidobacterium bifidum A
A
-
-
Manually annotated by BRENDA team
Bifidobacterium bifidum B
B
-
-
Manually annotated by BRENDA team
strain 203
-
-
Manually annotated by BRENDA team
subspecies breve a; subspecies parvulorum a
-
-
Manually annotated by BRENDA team
Bifidobacterium breve 203
strain 203
-
-
Manually annotated by BRENDA team
subspecies animalis a, subspecies animalis b
-
-
Manually annotated by BRENDA team
subspecies infantis a, subspecies liberorum
-
-
Manually annotated by BRENDA team
Bifidobacterium pseudolongum A
A
-
-
Manually annotated by BRENDA team
Bifidobacterium pseudolongum B
B
-
-
Manually annotated by BRENDA team
Bifidobacterium thermophilum B
strain B
-
-
Manually annotated by BRENDA team
; two isoforms generated by alternative splicing, differences in molecular weights
-
-
Manually annotated by BRENDA team
isoenzyme GS1; isoenzyme GS2
-
-
Manually annotated by BRENDA team
oxygen-resistant mutant strain, isoforms GSI and GSII
-
-
Manually annotated by BRENDA team
strain NCIB 10338
-
-
Manually annotated by BRENDA team
Corynebacterium callunae NCIB 10338
strain NCIB 10338
-
-
Manually annotated by BRENDA team
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
-
-
Manually annotated by BRENDA team
i.e. Spiniraja whitleyi
-
-
Manually annotated by BRENDA team
a highly regenerative oligochaete annelid, gene gs
Q1MXG4
UniProt
Manually annotated by BRENDA team
female Standardbred horses
-
-
Manually annotated by BRENDA team
Standardbred mares
-
-
Manually annotated by BRENDA team
ATCC 11775
-
-
Manually annotated by BRENDA team
wild-type and several single-tryptophan mutant forms; wild-type and site-directed mutants H4A, H4C, M8L, H12L, H12D
-
-
Manually annotated by BRENDA team
wild-type and site-directed mutants H4A, H4C, M8L, H12L, H12D
-
-
Manually annotated by BRENDA team
wild-type and site-directed mutants; wild-type and site-directed mutants H4A, H4C, M8L, H12L, H12D
-
-
Manually annotated by BRENDA team
strain CpI1, 2 enzyme forms GSI and GSII
-
-
Manually annotated by BRENDA team
strain CpI1, 2 enzyme forms GSI and GSII
-
-
Manually annotated by BRENDA team
strain PAL 5, nitrogen fixing bacterium, major supplier of fixed nitrogen to sugarcane
-
-
Manually annotated by BRENDA team
strain PAL 5, nitrogen fixing bacterium, major supplier of fixed nitrogen to sugarcane
-
-
Manually annotated by BRENDA team
isozyme GS2
-
-
Manually annotated by BRENDA team
gene GhGS; allotetraploid, strains 7235 and TM-1, gene GhGS, isozymes GS1 and GS2
UniProt
Manually annotated by BRENDA team
strain DSMZ 2266T
Uniprot
Manually annotated by BRENDA team
strain ATCC 43504
-
-
Manually annotated by BRENDA team
french population
UniProt
Manually annotated by BRENDA team
male Sprague Dawley rats
-
-
Manually annotated by BRENDA team
cv. Steffi, isozyme GS2
UniProt
Manually annotated by BRENDA team
isozyme GS1
-
-
Manually annotated by BRENDA team
isozyme GS2
UniProt
Manually annotated by BRENDA team
isoform GS1a
UniProt
Manually annotated by BRENDA team
isoform GS1b
UniProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
two transcripts arising from alternative splicing of the first intron, named GC2b-alpha and GS2b-beta
UniProt
Manually annotated by BRENDA team
male C57BL/6J mice
-
-
Manually annotated by BRENDA team
male Swiss Webster mice
-
-
Manually annotated by BRENDA team
strain AF2122/97, gene glnA1
UniProt
Manually annotated by BRENDA team
strain AF2122/97, gene glnA2
UniProt
Manually annotated by BRENDA team
strain AF2122/97, gene glnA1
UniProt
Manually annotated by BRENDA team
strain AF2122/97, gene glnA2
UniProt
Manually annotated by BRENDA team
strain VT301
-
-
Manually annotated by BRENDA team
Mycobacterium smegmatis VT301
strain VT301
-
-
Manually annotated by BRENDA team
gene glnA1 or gene Rv2220 encoding isozyme GlnA1
UniProt
Manually annotated by BRENDA team
gene glnA2 or gene Rv2222c encoding isozyme GlnA2
UniProt
Manually annotated by BRENDA team
gene glnA3 or gene Rv1878, encoding isozyme GlnA3
UniProt
Manually annotated by BRENDA team
gene glnA4 or gene Rv2860c, encoding isozyme GlnA4
UniProt
Manually annotated by BRENDA team
strain H37Rv, four highly homolgous GSI protein sequences GlnA1, encoded by gene Rv2220, GlnA2, GlnA3, and GlnA4
-
-
Manually annotated by BRENDA team
strain H37Rv, gene glnA1
UniProt
Manually annotated by BRENDA team
strain H37Rv, gene glnA2
UniProt
Manually annotated by BRENDA team
isozymes GS1a and GS1b
-
-
Manually annotated by BRENDA team
isoenzyme OsGLN1,1
SwissProt
Manually annotated by BRENDA team
isoenzyme OsGLN1,2
SwissProt
Manually annotated by BRENDA team
isozymes GS1a and GS1b
UniProt
Manually annotated by BRENDA team
isoenzymes GScs from seed cytosol and isoenzyme GScl from leaf cytosol
-
-
Manually annotated by BRENDA team
pv. Tabaci
-
-
Manually annotated by BRENDA team
Pseudomonas taetrolens Y-30
srain Y-30
-
-
Manually annotated by BRENDA team
Pyrococcus sp. KOD1
-
UniProt
Manually annotated by BRENDA team
male Sprague Dawley rats
-
-
Manually annotated by BRENDA team
male Wistar rats
-
-
Manually annotated by BRENDA team
Sprague-Dawley rats
-
-
Manually annotated by BRENDA team
3 enzyme forms: GSI, GSII and GSIII
-
-
Manually annotated by BRENDA team
strain E1F1
-
-
Manually annotated by BRENDA team
Rhodobacter capsulatus E1F1
strain E1F1
-
-
Manually annotated by BRENDA team
two enzyme forms: low-activity form and high-activity form, depending on the concentration of combined nitrogen in the medium before harvest
-
-
Manually annotated by BRENDA team
isozyme GS2
-
-
Manually annotated by BRENDA team
3 enzyme forms: GSI, GSII and GSIII
-
-
Manually annotated by BRENDA team
strain CCMP 1332, isoform GS1 and GS2
-
-
Manually annotated by BRENDA team
Skeletonema costatum CCMP 1332
strain CCMP 1332, isoform GS1 and GS2
-
-
Manually annotated by BRENDA team
cultivar Micro-Tom
-
-
Manually annotated by BRENDA team
cultivar Desiree
-
-
Manually annotated by BRENDA team
L. cv. Desiree, isoenzyme GS1; L. cv. Desiree, isoenzyme GS2
-
-
Manually annotated by BRENDA team
Sorghum sp.
-
-
-
Manually annotated by BRENDA team
two isoforms
-
-
Manually annotated by BRENDA team
2 enzyme forms GS1 and GS2
-
-
Manually annotated by BRENDA team
four highly homolgous GSI protein sequences GlnA1, GlnA2, GlnA3, and GlnA4
UniProt
Manually annotated by BRENDA team
strain NRRL B-2682
-
-
Manually annotated by BRENDA team
Streptomyces griseus NRRL B-2682
strain NRRL B-2682
-
-
Manually annotated by BRENDA team
two isoforms GSI and GSII encoded by the two genes glnA and glnB
-
-
Manually annotated by BRENDA team
strain DSM 639, hypothermoacidophilic crenarcheon
SwissProt
Manually annotated by BRENDA team
enzyme form GSI and GSIII encoded by the gene glnA and glnB; strain PCC 6803
-
-
Manually annotated by BRENDA team
strain PCC 6803
-
-
Manually annotated by BRENDA team
strain 111
-
-
Manually annotated by BRENDA team
Thermus thermophilus 111
strain 111
-
-
Manually annotated by BRENDA team
cyanobacterium
SwissProt
Manually annotated by BRENDA team
isoenzyme GS1
-
-
Manually annotated by BRENDA team
isozyme GS1a; cv. Cadenza, 10 genes from 4 subfamilies, from hexaploid wheat
UniProt
Manually annotated by BRENDA team
isozyme GS1b; cv. Cadenza, 10 genes from 4 subfamilies, from hexaploid wheat
UniProt
Manually annotated by BRENDA team
isozyme GS1c; cv. Cadenza, 10 genes from 4 subfamilies, from hexaploid wheat
UniProt
Manually annotated by BRENDA team
isozyme GS2
-
-
Manually annotated by BRENDA team
isozyme GS2a; cv. Cadenza, 10 genes from 4 subfamilies, from hexaploid wheat
UniProt
Manually annotated by BRENDA team
isozyme GS2b; cv. Cadenza, contains 10 genes from 4 subfamilies, from hexaploid wheat
UniProt
Manually annotated by BRENDA team
isozyme GS2c; cv. Cadenza, 10 genes from 4 subfamilies, from hexaploid wheat
UniProt
Manually annotated by BRENDA team
isozyme GSe1; cv. Cadenza, 10 genes from 4 subfamilies, from hexaploid wheat
UniProt
Manually annotated by BRENDA team
isozyme GSe2; cv. Cadenza, 10 genes from 4 subfamilies, from hexaploid wheat
UniProt
Manually annotated by BRENDA team
isozyme GSr1; cv. Cadenza, 10 genes from 4 subfamilies, from hexaploid wheat
UniProt
Manually annotated by BRENDA team
isozyme GSr2; cv. Cadenza, 10 genes from 4 subfamilies, from hexaploid wheat
UniProt
Manually annotated by BRENDA team
triticale, cultivar Fidelio
-
-
Manually annotated by BRENDA team
strain ATCC 95640
SwissProt
Manually annotated by BRENDA team
-
Uniprot
Manually annotated by BRENDA team
isozyme GS1 encoded by genes Gln1-1 to Gln1-4
-
-
Manually annotated by BRENDA team
isozyme GS1-3; isozyme GS1-4
UniProt
Manually annotated by BRENDA team
isozyme GS1; isozyme GS2
-
-
Manually annotated by BRENDA team
isozyme GS2 encoded by gene Gln2
UniProt
Manually annotated by BRENDA team
cultivar Jemalong J5
-
-
Manually annotated by BRENDA team
deduced protein contains a target peptide and is predicted to be driven to the plastid
additional information
additional information
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
metabolism
-
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
-
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
-
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
Anabaena sp. PCC 7120
-
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
-
physiological function
-
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
-
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
-
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
-
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
-
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
O08467, -
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
Pyrococcus sp. KOD1
-
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
-
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2 ATP + 2 L-glutamate + 2 NH3
2 ADP + 2 phosphate + D-glutamine + D-isoglutamine
show the reaction diagram
P0A590, P64246, Q07752, Q33342
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
show the reaction diagram
P0A590, P64246, Q07752, Q33342
GlnA2 catalyses the synthesis of D-glutamine and D-isoglutamine
-
-
?
ATP + 3-aminopentanedioate + hydroxylamine
ADP + phosphate + ?
show the reaction diagram
-
the activity with is 3-aminopentanedioate (beta-glutamate) is 7fold less than the rate obtained with alpha-glutamate
-
-
?
ATP + 3-aminopentanedioate + hydroxylamine
ADP + phosphate + ?
show the reaction diagram
-, O29313
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 + ?
show the reaction diagram
Archaeoglobus fulgidus VC-16
O29313
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 + gamma-glutamylhydroxamate
show the reaction diagram
-, Q60182
the enzyme is more selective for L-glutamate (alpha-glutamate) than 3-aminopentanedioate (beta-glutamate) as a substrate
-
-
?
ATP + glutamate + NH4+
ADP + phosphate + L-glutamine
show the reaction diagram
-
-
-
-
r
ATP + glutamate + NH4+
ADP + phosphate + L-glutamine
show the reaction diagram
-
-
-
-
?
ATP + glutamate + NH4+
ADP + phosphate + L-glutamine
show the reaction diagram
-
-
-
-
?
ATP + glutamate + NH4+
ADP + phosphate + L-glutamine
show the reaction diagram
-
-
-
-
?
ATP + glutamate + NH4+
ADP + phosphate + L-glutamine
show the reaction diagram
-
-
-
-
?
ATP + glutamate + NH4+
ADP + phosphate + L-glutamine
show the reaction diagram
-
-
-
-
r
ATP + glutamate + NH4+
ADP + phosphate + L-glutamine
show the reaction diagram
-
-
-
-
?
ATP + glutamate + NH4+
ADP + phosphate + L-glutamine
show the reaction diagram
-
-
-
-
?
ATP + glutamate + NH4+
ADP + phosphate + L-glutamine
show the reaction diagram
-
-
-
-
?
ATP + glutamate + NH4+
ADP + phosphate + L-glutamine
show the reaction diagram
-
-
-
-
?
ATP + glutamate + NH4+
ADP + phosphate + L-glutamine
show the reaction diagram
-
-
-
-
?
ATP + glutamate + NH4+
ADP + phosphate + L-glutamine
show the reaction diagram
-
-
-
-
?
ATP + glutamate + NH4+
ADP + phosphate + L-glutamine
show the reaction diagram
-
-
-
-
?
ATP + glutamate + NH4+
ADP + phosphate + L-glutamine
show the reaction diagram
-
-
-
-
?
ATP + glutamate + NH4+
ADP + phosphate + L-glutamine
show the reaction diagram
-
-
-
-
?
ATP + glutamate + NH4+
ADP + phosphate + L-glutamine
show the reaction diagram
-
-
-
-
?
ATP + glutamate + NH4+
ADP + phosphate + L-glutamine
show the reaction diagram
-
-
-
-
r
ATP + glutamate + NH4+
ADP + phosphate + L-glutamine
show the reaction diagram
Q86ZU6, -
-
-
-
?
ATP + glutamate + NH4+
ADP + phosphate + L-glutamine
show the reaction diagram
Q9HH09, -
-
-
-
r
ATP + glutamate + NH4+
ADP + phosphate + L-glutamine
show the reaction diagram
Q9RHZ1, -
-
-
-
r
ATP + glutamate + NH4+
ADP + phosphate + L-glutamine
show the reaction diagram
-
-
-
-
r
ATP + glutamate + NH4+
ADP + phosphate + L-glutamine
show the reaction diagram
-
-
-
-
?
ATP + glutamate + NH4+
ADP + phosphate + L-glutamine
show the reaction diagram
-
central enzyme of nitrogen metabolism
-
-
?
ATP + glutamate + NH4+
ADP + phosphate + L-glutamine
show the reaction diagram
-
central enzyme of nitrogen metabolism
-
-
?
ATP + glutamate + NH4+
ADP + phosphate + L-glutamine
show the reaction diagram
-
central enzyme of nitrogen metabolism
-
-
r
ATP + glutamate + NH4+
ADP + phosphate + L-glutamine
show the reaction diagram
-
central enzyme of nitrogen metabolism
-
-
?
ATP + glutamate + NH4+
ADP + phosphate + L-glutamine
show the reaction diagram
-
central enzyme of nitrogen metabolism
-
-
?
ATP + glutamate + NH4+
ADP + phosphate + L-glutamine
show the reaction diagram
-
central enzyme of nitrogen metabolism
-
-
?
ATP + glutamate + NH4+
ADP + phosphate + L-glutamine
show the reaction diagram
-
central enzyme of nitrogen metabolism
-
-
r
ATP + glutamate + NH4+
ADP + phosphate + L-glutamine
show the reaction diagram
Q9HH09, -
central enzyme of nitrogen metabolism
-
-
r
ATP + glutamate + NH4+
ADP + phosphate + L-glutamine
show the reaction diagram
Q9RHZ1, -
central enzyme of nitrogen metabolism
-
-
r
ATP + glutamate + NH4+
ADP + phosphate + L-glutamine
show the reaction diagram
-
central enzyme of nitrogen metabolism
-
-
r
ATP + glutamate + NH4+
ADP + phosphate + L-glutamine
show the reaction diagram
-
central enzyme of nitrogen metabolism, ammonia assimilation
-
-
r
ATP + glutamate + NH4+
ADP + phosphate + L-glutamine
show the reaction diagram
-
central enzyme of nitrogen metabolism, ammonia assimilation
-
-
?
ATP + glutamate + NH4+
ADP + phosphate + L-glutamine
show the reaction diagram
-
central enzyme of nitrogen metabolism, ammonia assimilation
-
-
?
ATP + glutamate + NH4+
ADP + phosphate + L-glutamine
show the reaction diagram
-
central enzyme of nitrogen metabolism, ammonia assimilation
-
-
?
ATP + glutamate + NH4+
ADP + phosphate + L-glutamine
show the reaction diagram
-
central enzyme of nitrogen metabolism, assimilation of ammonia
-
-
r
ATP + glutamate + NH4+
ADP + phosphate + L-glutamine
show the reaction diagram
-
central enzyme of nitrogen metabolism, assimilation of ammonia for protein synthesis
-
-
?
ATP + glutamate + NH4+
ADP + phosphate + L-glutamine
show the reaction diagram
-
central enzyme of nitrogen metabolism, elimination of glutamate from animal brain
-
-
?
ATP + glutamate + NH4+
ADP + phosphate + L-glutamine
show the reaction diagram
Q86ZU6, -
central enzyme of nitrogen metabolism, involved in nitrogen assimilation pathway
-
-
?
ATP + glutamate + NH4+
ADP + phosphate + L-glutamine
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
central enzyme of nitrogen metabolism, provides glutamine for biosynthesis, ammonia assimilation
-
-
?
ATP + glutamate + NH4+
ADP + phosphate + L-glutamine
show the reaction diagram
-
-, central enzyme of nitrogen metabolism, ammonia assimilation
-
-
?
ATP + glutamate + NH4+
ADP + phosphate + L-glutamine
show the reaction diagram
Thermus thermophilus 111
-
-, central enzyme of nitrogen metabolism
-
-
?
ATP + glutamate + NH4+
ADP + phosphate + L-glutamine
show the reaction diagram
-
-, central enzyme of nitrogen metabolism
-
-
r
ATP + L-Glu + ethylamine
ADP + phosphate + ?
show the reaction diagram
Bifidobacterium bifidum, Bifidobacterium breve, Bifidobacterium pseudolongum, Bifidobacterium bifidum A, Bifidobacterium breve 203, Bifidobacterium pseudolongum A
-
slightly effective
-
-
-
ATP + L-Glu + ethylamine
ADP + phosphate + L-Gln + ?
show the reaction diagram
Pseudomonas taetrolens, Pseudomonas taetrolens Y-30
-
1% of the activity with NH4+, at pH 8.0, activated with 30 mM Mg2+
-
-
?
ATP + L-Glu + hydroxylamine
ADP + phosphate + gamma-glutamyl hydroxamate
show the reaction diagram
-
-
-
-
-
ATP + L-Glu + hydroxylamine
ADP + phosphate + gamma-glutamyl hydroxamate
show the reaction diagram
-
-
-
-
ATP + L-Glu + hydroxylamine
ADP + phosphate + gamma-glutamyl hydroxamate
show the reaction diagram
-
13% of the activity relative to NH4+
-
-
-
ATP + L-Glu + hydroxylamine
ADP + phosphate + gamma-glutamyl hydroxamate
show the reaction diagram
-
59% of the activity relative to NH4+
-
-
-
ATP + L-Glu + hydroxylamine
ADP + phosphate + gamma-glutamyl hydroxamate
show the reaction diagram
-
10% of the activity relative to NH4+
-
-
-
ATP + L-Glu + hydroxylamine
ADP + phosphate + gamma-glutamyl hydroxamate
show the reaction diagram
Bifidobacterium bifidum A
-
59% of the activity relative to NH4+
-
-
-
ATP + L-Glu + hydroxylamine
ADP + phosphate + gamma-glutamyl hydroxamate
show the reaction diagram
Bifidobacterium breve 203
-
13% of the activity relative to NH4+
-
-
-
ATP + L-Glu + hydroxylamine
ADP + phosphate + gamma-glutamyl hydroxamate
show the reaction diagram
Bifidobacterium pseudolongum A
-
10% of the activity relative to NH4+
-
-
-
ATP + L-Glu + hydroxylamine
ADP + phosphate + L-Gln + ?
show the reaction diagram
Pseudomonas taetrolens, Pseudomonas taetrolens Y-30
-
32% of the activity with NH4+
-
-
?
ATP + L-Glu + methylamine
ADP + phosphate + ?
show the reaction diagram
Bifidobacterium bifidum, Bifidobacterium breve, Bifidobacterium pseudolongum, Bifidobacterium bifidum A, Bifidobacterium breve 203, Bifidobacterium pseudolongum A
-
slightly effective
-
-
-
ATP + L-Glu + methylamine
ADP + phosphate + L-Gln + ?
show the reaction diagram
-
7% of the activity with NH4+, at pH 8.0, activated with 30 mM Mg2+
-
-
?
ATP + L-Glu + NH4+
ADP + phosphate + L-Gln
show the reaction diagram
-
-
-
-
-
ATP + L-Glu + NH4+
ADP + phosphate + L-Gln
show the reaction diagram
-
-
-
-
-
ATP + L-Glu + NH4+
ADP + phosphate + L-Gln
show the reaction diagram
-
-
-
-
-
ATP + L-Glu + NH4+
ADP + phosphate + L-Gln
show the reaction diagram
-
-
-
-
-
ATP + L-Glu + NH4+
ADP + phosphate + L-Gln
show the reaction diagram
-
-
-
-
-
ATP + L-Glu + NH4+
ADP + phosphate + L-Gln
show the reaction diagram
-
-
-
-
-
ATP + L-Glu + NH4+
ADP + phosphate + L-Gln
show the reaction diagram
-
-
-
-
-
ATP + L-Glu + NH4+
ADP + phosphate + L-Gln
show the reaction diagram
-
-
-
-
-
ATP + L-Glu + NH4+
ADP + phosphate + L-Gln
show the reaction diagram
-
-
-
-
-
ATP + L-Glu + NH4+
ADP + phosphate + L-Gln
show the reaction diagram
-
-
-
-
-
ATP + L-Glu + NH4+
ADP + phosphate + L-Gln
show the reaction diagram
-
-
-
-
?
ATP + L-Glu + NH4+
ADP + phosphate + L-Gln
show the reaction diagram
-
-
-
-
ir
ATP + L-Glu + NH4+
ADP + phosphate + L-Gln
show the reaction diagram
-
-
-
-
-
ATP + L-Glu + NH4+
ADP + phosphate + L-Gln
show the reaction diagram
-
-
-
-
?
ATP + L-Glu + NH4+
ADP + phosphate + L-Gln
show the reaction diagram
-
-
-
-
-
ATP + L-Glu + NH4+
ADP + phosphate + L-Gln
show the reaction diagram
-
-
-
-
ir
ATP + L-Glu + NH4+
ADP + phosphate + L-Gln
show the reaction diagram
-
-
-
-
-
ATP + L-Glu + NH4+
ADP + phosphate + L-Gln
show the reaction diagram
-
-
-
-
?
ATP + L-Glu + NH4+
ADP + phosphate + L-Gln
show the reaction diagram
-
-
-
-
ir
ATP + L-Glu + NH4+
ADP + phosphate + L-Gln
show the reaction diagram
-
-
-
-
-
ATP + L-Glu + NH4+
ADP + phosphate + L-Gln
show the reaction diagram
-
-
-
-
-
ATP + L-Glu + NH4+
ADP + phosphate + L-Gln
show the reaction diagram
-
-
-
-
ir
ATP + L-Glu + NH4+
ADP + phosphate + L-Gln
show the reaction diagram
-
-
-
-
?
ATP + L-Glu + NH4+
ADP + phosphate + L-Gln
show the reaction diagram
-
-
-
-
-
ATP + L-Glu + NH4+
ADP + phosphate + L-Gln
show the reaction diagram
-
-
-
-
-
ATP + L-Glu + NH4+
ADP + phosphate + L-Gln
show the reaction diagram
-
-
-
-
-
ATP + L-Glu + NH4+
ADP + phosphate + L-Gln
show the reaction diagram
-
-
-
-
?
ATP + L-Glu + NH4+
ADP + phosphate + L-Gln
show the reaction diagram
-
-
-
-
?
ATP + L-Glu + NH4+
ADP + phosphate + L-Gln
show the reaction diagram
-
-
-
-
-
ATP + L-Glu + NH4+
ADP + phosphate + L-Gln
show the reaction diagram
-
-
-
-
-
ATP + L-Glu + NH4+
ADP + phosphate + L-Gln
show the reaction diagram
-
-
-
-
-
ATP + L-Glu + NH4+
ADP + phosphate + L-Gln
show the reaction diagram
-
-
-
-
?
ATP + L-Glu + NH4+
ADP + phosphate + L-Gln
show the reaction diagram
-
-
-
-
?
ATP + L-Glu + NH4+
ADP + phosphate + L-Gln
show the reaction diagram
-
-
-
-
-
ATP + L-Glu + NH4+
ADP + phosphate + L-Gln
show the reaction diagram
-
-
-
-
-
ATP + L-Glu + NH4+
ADP + phosphate + L-Gln
show the reaction diagram
-
-
-
-
?
ATP + L-Glu + NH4+
ADP + phosphate + L-Gln
show the reaction diagram
-
-
-
-
-
ATP + L-Glu + NH4+
ADP + phosphate + L-Gln
show the reaction diagram
-
-
-
-
-
ATP + L-Glu + NH4+
ADP + phosphate + L-Gln
show the reaction diagram
-
-
-
-
-
ATP + L-Glu + NH4+
ADP + phosphate + L-Gln
show the reaction diagram
-
-
-
-
-
ATP + L-Glu + NH4+
ADP + phosphate + L-Gln
show the reaction diagram
-
-
-
-
-
ATP + L-Glu + NH4+
ADP + phosphate + L-Gln
show the reaction diagram
-
-
-
-
?
ATP + L-Glu + NH4+
ADP + phosphate + L-Gln
show the reaction diagram
-, P0A590
-
-
-
-
ATP + L-Glu + NH4+
ADP + phosphate + L-Gln
show the reaction diagram
-
-
-
-
-
ATP + L-Glu + NH4+
ADP + phosphate + L-Gln
show the reaction diagram
-
-
-
-
-
ATP + L-Glu + NH4+
ADP + phosphate + L-Gln
show the reaction diagram
-
-
-
-
-
ATP + L-Glu + NH4+
ADP + phosphate + L-Gln
show the reaction diagram
P15623
-
-
-
?
ATP + L-Glu + NH4+
ADP + phosphate + L-Gln
show the reaction diagram
-
-
-
-
-
ATP + L-Glu + NH4+
ADP + phosphate + L-Gln
show the reaction diagram
-
-
-
-
-
ATP + L-Glu + NH4+
ADP + phosphate + L-Gln
show the reaction diagram
-
-
-
-
-
ATP + L-Glu + NH4+
ADP + phosphate + L-Gln
show the reaction diagram
-
-
-
-
?
ATP + L-Glu + NH4+
ADP + phosphate + L-Gln
show the reaction diagram
-
-
-
-
-
ATP + L-Glu + NH4+
ADP + phosphate + L-Gln
show the reaction diagram
-
-
-
-
-
ATP + L-Glu + NH4+
ADP + phosphate + L-Gln
show the reaction diagram
-
-
-
-
?
ATP + L-Glu + NH4+
ADP + phosphate + L-Gln
show the reaction diagram
-
-
-
-
-
ATP + L-Glu + NH4+
ADP + phosphate + L-Gln
show the reaction diagram
-
-
-
-
-
ATP + L-Glu + NH4+
ADP + phosphate + L-Gln
show the reaction diagram
-
-
-
-
-
ATP + L-Glu + NH4+
ADP + phosphate + L-Gln
show the reaction diagram
-
-
-
-
-
ATP + L-Glu + NH4+
ADP + phosphate + L-Gln
show the reaction diagram
-
-
-
-
-
ATP + L-Glu + NH4+
ADP + phosphate + L-Gln
show the reaction diagram
-
-
-
-
-
ATP + L-Glu + NH4+
ADP + phosphate + L-Gln
show the reaction diagram
-
-
-
-
?
ATP + L-Glu + NH4+
ADP + phosphate + L-Gln
show the reaction diagram
-
-
-
-
-
ATP + L-Glu + NH4+
ADP + phosphate + L-Gln
show the reaction diagram
-
-
-
-
-
ATP + L-Glu + NH4+
ADP + phosphate + L-Gln
show the reaction diagram
-
-
-
-
-
ATP + L-Glu + NH4+
ADP + phosphate + L-Gln
show the reaction diagram
-
-
-
-
-
ATP + L-Glu + NH4+
ADP + phosphate + L-Gln
show the reaction diagram
-
-
-
-
-
ATP + L-Glu + NH4+
ADP + phosphate + L-Gln
show the reaction diagram
-
-
-
-
-
ATP + L-Glu + NH4+
ADP + phosphate + L-Gln
show the reaction diagram
-
-
-
-
-
ATP + L-Glu + NH4+
ADP + phosphate + L-Gln
show the reaction diagram
-
-
-
-
?
ATP + L-Glu + NH4+
ADP + phosphate + L-Gln
show the reaction diagram
-
-
-
-
-
ATP + L-Glu + NH4+
ADP + phosphate + L-Gln
show the reaction diagram
-
-
-
-
?
ATP + L-Glu + NH4+
ADP + phosphate + L-Gln
show the reaction diagram
-
-
-
-
-
ATP + L-Glu + NH4+
ADP + phosphate + L-Gln
show the reaction diagram
-
-
-
-
-
ATP + L-Glu + NH4+
ADP + phosphate + L-Gln
show the reaction diagram
-
-
-
-
-
ATP + L-Glu + NH4+
ADP + phosphate + L-Gln
show the reaction diagram
-
-
-
-
-
ATP + L-Glu + NH4+
ADP + phosphate + L-Gln
show the reaction diagram
-
-
-
-
?
ATP + L-Glu + NH4+
ADP + phosphate + L-Gln
show the reaction diagram
-
-
-
-
-
ATP + L-Glu + NH4+
ADP + phosphate + L-Gln
show the reaction diagram
-
-
-
-
-
ATP + L-Glu + NH4+
ADP + phosphate + L-Gln
show the reaction diagram
-
-
-
-
-
ATP + L-Glu + NH4+
ADP + phosphate + L-Gln
show the reaction diagram
-
-
-
-
-
ATP + L-Glu + NH4+
ADP + phosphate + L-Gln
show the reaction diagram
-
-
-
-
-
ATP + L-Glu + NH4+
ADP + phosphate + L-Gln
show the reaction diagram
-
-
-
-
-
ATP + L-Glu + NH4+
ADP + phosphate + L-Gln
show the reaction diagram
-
-
-
-
-
ATP + L-Glu + NH4+
ADP + phosphate + L-Gln
show the reaction diagram
-
-
-
-
-
ATP + L-Glu + NH4+
ADP + phosphate + L-Gln
show the reaction diagram
-
-
-
-
-
ATP + L-Glu + NH4+
ADP + phosphate + L-Gln
show the reaction diagram
-
-
-
-
-
ATP + L-Glu + NH4+
ADP + phosphate + L-Gln
show the reaction diagram
-
-
-
-
-
ATP + L-Glu + NH4+
ADP + phosphate + L-Gln
show the reaction diagram
-
-
-
-
?
ATP + L-Glu + NH4+
ADP + phosphate + L-Gln
show the reaction diagram
P14654, P14656
-
-
-
?
ATP + L-Glu + NH4+
ADP + phosphate + L-Gln
show the reaction diagram
-, O85177
-
-
-
?
ATP + L-Glu + NH4+
ADP + phosphate + L-Gln
show the reaction diagram
Q0E5H8
-
-
-
?
ATP + L-Glu + NH4+
ADP + phosphate + L-Gln
show the reaction diagram
P04771
-
-
-
ir
ATP + L-Glu + NH4+
ADP + phosphate + L-Gln
show the reaction diagram
P38562
-
-
-
?
ATP + L-Glu + NH4+
ADP + phosphate + L-Gln
show the reaction diagram
-
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
show the reaction diagram
-
enzyme can bind 8 M of ATP per mol of enzyme
-
-
-
ATP + L-Glu + NH4+
ADP + phosphate + L-Gln
show the reaction diagram
-
1 mol of enzyme can bind 5 M ATP
-
-
-
ATP + L-Glu + NH4+
ADP + phosphate + L-Gln
show the reaction diagram
-
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
show the reaction diagram
P14654, P14656
serves for assimilation of ammonium in rice root, and ameliorates the toxic effect of ammonium excess
-
-
?
ATP + L-Glu + NH4+
ADP + phosphate + L-Gln
show the reaction diagram
Corynebacterium callunae NCIB 10338
-
-
-
-
-
ATP + L-Glu + NH4+
ADP + phosphate + L-Gln
show the reaction diagram
Bifidobacterium bifidum A, Bifidobacterium thermophilum B
-
-
-
-
-
ATP + L-Glu + NH4+
ADP + phosphate + L-Gln
show the reaction diagram
Skeletonema costatum CCMP 1332
-
-
-
-
-
ATP + L-Glu + NH4+
ADP + phosphate + L-Gln
show the reaction diagram
Pseudomonas taetrolens Y-30
-
-
-
-
?
ATP + L-Glu + NH4+
ADP + phosphate + L-Gln
show the reaction diagram
Rhodobacter capsulatus E1F1
-
-
-
-
-
ATP + L-Glu + NH4+
ADP + phosphate + L-Gln
show the reaction diagram
Streptomyces griseus NRRL B-2682
-
-
-
-
-
ATP + L-Glu + NH4+
ADP + phosphate + L-Gln
show the reaction diagram
-
-
-
-
-
ATP + L-Glu + NH4+
ADP + phosphate + L-Gln
show the reaction diagram
Bifidobacterium pseudolongum A, Bifidobacterium pseudolongum B, Bifidobacterium bifidum B
-
-
-
-
-
ATP + L-Glu + NH4+
ADP + phosphate + L-Gln
show the reaction diagram
Bacillus subtilis KN2
-
-
-
-
-
ATP + L-Glu + NH4+
?
show the reaction diagram
-
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+
?
show the reaction diagram
-
first step in urea synthesis
-
-
-
ATP + L-Glu + NH4+
?
show the reaction diagram
-
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+
?
show the reaction diagram
-
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+
?
show the reaction diagram
-
glutamate synthetase cycle provides the only efficient pathway for the conversion of inorganic nitrogen to the organic form
-
-
-
ATP + L-Glu + NH4+
?
show the reaction diagram
-
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-glutamate + hydroxylamine
ADP + phosphate + gamma-L-glutamyl hydroxamate + NH3
show the reaction diagram
-
in presence of Mn2+
-
-
?
ATP + L-glutamate + hydroxylamine
ADP + phosphate + L-gamma-glutamylhydroxamate
show the reaction diagram
-
photometric determination of GS activity based on formation of an L-gamma-glutamylhydroxamate ferric chloride complex using hydroxylamine instead of ammonia
-
-
?
ATP + L-glutamate + hydroxylamine
?
show the reaction diagram
O08467, -
-
-
-
?
ATP + L-glutamate + hydroxylamine
?
show the reaction diagram
Pyrococcus sp. KOD1
O08467
-
-
-
?
ATP + L-glutamate + hydroxylamine
ADP + phosphate + gamma-L-glutamylhydroxamate
show the reaction diagram
-
the activity with L-glutamate is 7fold higher than the rate obtained with 3-aminopentanedioate (beta-glutamate)
-
-
?
ATP + L-glutamate + hydroxylamine
ADP + phosphate + gamma-L-glutamylhydroxamate
show the reaction diagram
-, O29313
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
show the reaction diagram
-, Q60182
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
show the reaction diagram
Archaeoglobus fulgidus VC-16
O29313
the enzyme is more selective for L-glutamate (alpha-glutamate) than for 3-aminopentanedioate (beta-glutamate) as a substrate
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
show the reaction diagram
-
-
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
show the reaction diagram
-
-
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
show the reaction diagram
-
-
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
show the reaction diagram
-
-
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
show the reaction diagram
-
-
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
show the reaction diagram
-
-
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
show the reaction diagram
-
-
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
show the reaction diagram
-
-
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
show the reaction diagram
-
-
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
show the reaction diagram
P13564
-
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
show the reaction diagram
-
-
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
show the reaction diagram
P25462, -
-
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
show the reaction diagram
-
-
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
show the reaction diagram
-
-
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
show the reaction diagram
-
-
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
show the reaction diagram
-
-
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
show the reaction diagram
-
-
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
show the reaction diagram
-
-
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
show the reaction diagram
-
-
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
show the reaction diagram
-
-
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
show the reaction diagram
-
-
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
show the reaction diagram
-
-
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
show the reaction diagram
P09606
-
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
show the reaction diagram
P13564
-
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
show the reaction diagram
-
-
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
show the reaction diagram
P0A1P6
-
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
show the reaction diagram
P77961
-
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
show the reaction diagram
P15104
-
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
show the reaction diagram
P15105
-
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
show the reaction diagram
P12425
-
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
show the reaction diagram
-
-
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
show the reaction diagram
P64246
-
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
show the reaction diagram
Q43127
-
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
show the reaction diagram
P81107, -
-
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
show the reaction diagram
Q45NB2, Q45NB3, Q45NB4, Q45NB5, Q45NB6, Q45NB7, Q6RUI9, Q6RUJ0, Q6RUJ1, Q6RUJ2
-
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
show the reaction diagram
A8WCU3, -
-
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
show the reaction diagram
Q0E5H7
-
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
show the reaction diagram
-, P0A591, P64246
-
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
show the reaction diagram
-
-
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
show the reaction diagram
P46410
-
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
show the reaction diagram
-, Q1MXG4
-
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
show the reaction diagram
P15106
-
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
show the reaction diagram
-
brain injuries are usually associated with an increase in the expression of the glutamate-converting enzyme glutamine synthetase
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
show the reaction diagram
-
dogs show altered L-glutamate distribution and reduced enzyme content in primary glaucoma and ischemia, overview
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
show the reaction diagram
-
enzyme regulation involving L-glutamate uptake, Ca2+, and P2X7 receptors, overview
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
show the reaction diagram
-
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
show the reaction diagram
P0A590, P64246, Q07752, Q33342
GlnA1 catalyses the synthesis of L-glutamine and is nonessential for bacterial growth
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
show the reaction diagram
P0A590
glnA1 is essential for Mycobacterium tuberculosis virulence
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
show the reaction diagram
P0A590, P64246, Q07752, Q33342
GlnA3 catalyses the synthesis of L-glutamine and are nonessential for bacterial growth
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
show the reaction diagram
P0A590, P64246, Q07752, Q33342
GlnA4 catalyses the synthesis of L-glutamine and are nonessential for bacterial growth
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
show the reaction diagram
-
glutamine also acts as a signaling molecule, physiological functions of glutamine, overview
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
show the reaction diagram
P46410
glutamine synthetase catalyzes the ATP-dependent conversion of ammonia and glutamate to glutamine in the pericentral zone
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
show the reaction diagram
-
glutamine synthetase is essential for proliferation of fetal skin fibroblasts
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
show the reaction diagram
Q45NB2, Q45NB3, Q45NB4, Q45NB5, Q45NB6, Q45NB7, Q6RUI9, Q6RUJ0, Q6RUJ1, Q6RUJ2
GS sub-families vary during leaf development and senescence, overview
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
show the reaction diagram
Q45NB2, Q45NB3, Q45NB4, Q45NB5, Q45NB6, Q45NB7, Q6RUI9, Q6RUJ0, Q6RUJ1, Q6RUJ2
GS sub-families vary during leaf development and senescence, overview. The cytosolic isozymes GS1 and GSr, dominant enzyme forms during leaf senescence, play major roles in assimilating ammonia during the critical phases of remobilisation of nitrogen to the grain, overview
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
show the reaction diagram
Q0E5H7
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
show the reaction diagram
-
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
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
show the reaction diagram
P15106
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
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
show the reaction diagram
P13564
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
show the reaction diagram
Q43127
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
show the reaction diagram
-
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
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
show the reaction diagram
-
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
show the reaction diagram
Q8HZM5
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
show the reaction diagram
-
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
show the reaction diagram
-
the enzyme is involved in development of mesial temporal lobe epilepsy, MTLE
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
show the reaction diagram
P81107, -
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
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
show the reaction diagram
-
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
show the reaction diagram
-
the enzyme is involved in the regulation of the nitrogen metabolism, overview
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
show the reaction diagram
-
the enzyme is involved in the signal transduction for regulation of the nitrogen metabolism, overview
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
show the reaction diagram
-
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
show the reaction diagram
-
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
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
show the reaction diagram
-, P13564
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
show the reaction diagram
-
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
show the reaction diagram
P09606
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
P0A1P6
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
show the reaction diagram
P77961
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
show the reaction diagram
P15104
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
show the reaction diagram
P15105
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
show the reaction diagram
P12425
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
show the reaction diagram
P0A590
amino acid binding site and structure, overview
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
show the reaction diagram
P0A590, P64246, Q07752, Q33342
GlnA1 catalyses the synthesis of L-glutamine
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
show the reaction diagram
-
GlnA1 is essential for survival in vitro, while GlnA2 is probably not
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
show the reaction diagram
P0A590, P64246, Q07752, Q33342
GlnA3 catalyses the synthesis of L-glutamine
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
show the reaction diagram
P0A590, P64246, Q07752, Q33342
GlnA4 catalyses the synthesis of L-glutamine
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
show the reaction diagram
-
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
show the reaction diagram
Q8HZM5
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
show the reaction diagram
Mycobacterium smegmatis VT301
-
-
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
show the reaction diagram
P0A591, P64246
-
-
-
?
ATP + L-glutamate + NH4+
ADP + phosphate + L-glutamine
show the reaction diagram
-
-
-
-
?
ATP + L-glutamate + NH4+
ADP + phosphate + L-glutamine
show the reaction diagram
-
-
-
-
?
ATP + L-glutamate + NH4+
ADP + phosphate + L-glutamine
show the reaction diagram
A0MZ70, -
-
-
-
?
ATP + L-glutamate + NH4+
ADP + phosphate + L-glutamine
show the reaction diagram
-
-
-
-
r
ATP + L-glutamate + NH4+
ADP + phosphate + L-glutamine
show the reaction diagram
P14654, P14656
-
-
-
?
ATP + L-glutamate + NH4+
ADP + phosphate + L-glutamine
show the reaction diagram
-
-
-
-
?
ATP + L-glutamate + NH4+
ADP + phosphate + L-glutamine
show the reaction diagram
-
central enzyme of nitrogen metabolism
-
-
r
ATP + L-glutamate + NH4+
ADP + phosphate + L-glutamine
show the reaction diagram
-
ammonium assimilation by glutamine synthetase is coupled to the function of the ammonium channel AmtB
-
-
?
ATP + L-glutamate + NH4+
ADP + phosphate + L-glutamine
show the reaction diagram
-, Q56WN1, Q9FMD9, Q9LVI8
glutamine synthetase is a key enzyme in nitrogen assimilation
-
-
?
ATP + L-glutamate + NH4+
ADP + phosphate + L-glutamine
show the reaction diagram
-, Q56WN1, Q9FMD9, Q9LVI8
glutamine synthetase is a key enzyme in nitrogen assimilation. Isoenzyme GLN1,1 accumulates in the surface layers of root during nitrogen limitation
-
-
?
ATP + L-glutamate + NH4+
ADP + phosphate + L-glutamine
show the reaction diagram
-
it is proposed that the induction of glutamine synthetase genes early in development and the subsequent formation of the active protein are preparatory for the increased capacity of the embryo to convert the toxic nitrogen end product, ammonia, into glutamine, which may then be utilized in the ornithine-urea cycle or other pathways
-
-
?
ATP + L-glutamate + NH4+
ADP + phosphate + L-glutamine
show the reaction diagram
P14654, P14656
serves for assimilation of ammonium in rice root, and ameliorates the toxic effect of ammonium excess
-
-
?
ATP + L-glutamate + NH4+
ADP + phosphate + L-glutamine
show the reaction diagram
-
the GLN2 gene product functions in both leaf mitochondria and chloroplasts to faciliate ammonium recovery during photorespiration
-
-
?
ATP + L-glutamate + NH4+
ADP + phosphate + L-glutamine
show the reaction diagram
Q4ZH57, -
biosynthesis of glutamine
-
-
?
ATP + L-glutamate + NH4+
ADP + phosphate + L-glutamine
show the reaction diagram
-
-, central enzyme of nitrogen metabolism
-
-
r
Gln + hydroxylamine + ADP
gamma-Glutamylhydroxamate + NH4+ + ?
show the reaction diagram
-
-
-
-
Gln + hydroxylamine + ADP
gamma-Glutamylhydroxamate + NH4+ + ?
show the reaction diagram
-
-
-
-
-
Gln + hydroxylamine + ADP
gamma-Glutamylhydroxamate + NH4+ + ?
show the reaction diagram
-
-
-
-
Gln + hydroxylamine + ADP
gamma-Glutamylhydroxamate + NH4+ + ?
show the reaction diagram
-
-
-
-
-
Gln + hydroxylamine + ADP
gamma-Glutamylhydroxamate + NH4+ + ?
show the reaction diagram
-
-
-
-
Gln + hydroxylamine + ADP
gamma-Glutamylhydroxamate + NH4+ + ?
show the reaction diagram
-
-
-
-
-
Gln + hydroxylamine + ADP
gamma-Glutamylhydroxamate + NH4+ + ?
show the reaction diagram
-
-
-
-
-
Gln + hydroxylamine + ADP
gamma-Glutamylhydroxamate + NH4+ + ?
show the reaction diagram
-
-
-
-
-
Gln + hydroxylamine + ADP
gamma-Glutamylhydroxamate + NH4+ + ?
show the reaction diagram
-
-
-
-
Gln + hydroxylamine + ADP
gamma-Glutamylhydroxamate + NH4+ + ?
show the reaction diagram
-
-
-
-
Gln + hydroxylamine + ADP
gamma-Glutamylhydroxamate + NH4+ + ?
show the reaction diagram
-
-
-
-
-
Gln + hydroxylamine + ADP
gamma-Glutamylhydroxamate + NH4+ + ?
show the reaction diagram
-
-
-
-
-
Gln + hydroxylamine + ADP
gamma-Glutamylhydroxamate + NH4+ + ?
show the reaction diagram
-
-
-
-
Gln + hydroxylamine + ADP
gamma-Glutamylhydroxamate + NH4+ + ?
show the reaction diagram
-
-
-
-
-
Gln + hydroxylamine + ADP
gamma-Glutamylhydroxamate + NH4+ + ?
show the reaction diagram
-
-
-
-
Gln + hydroxylamine + ADP
gamma-Glutamylhydroxamate + NH4+ + ?
show the reaction diagram
-
ADP or ATP required
-
-
Gln + hydroxylamine + ADP
gamma-Glutamylhydroxamate + NH4+ + ?
show the reaction diagram
Corynebacterium callunae, Corynebacterium callunae NCIB 10338
-
maximal transferase activity with ADP, and good activity with AMP and GDP
-
-
-
Gln + hydroxylamine + ADP
gamma-Glutamylhydroxamate + NH4+ + ?
show the reaction diagram
Bifidobacterium bifidum A
-
-
-
-
Gln + hydroxylamine + ADP
gamma-Glutamylhydroxamate + NH4+ + ?
show the reaction diagram
Rhodobacter capsulatus E1F1
-
-
-
-
-
Gln + hydroxylamine + ADP
gamma-Glutamylhydroxamate + NH4+ + ?
show the reaction diagram
Bifidobacterium breve 203, Bifidobacterium pseudolongum A
-
-
-
-
GTP + L-Glu + NH4+
GDP + phosphate + L-Gln
show the reaction diagram
-
no activity
-
-
-
GTP + L-Glu + NH4+
GDP + phosphate + L-Gln
show the reaction diagram
-
59% of the activity relative to ATP
-
-
-
GTP + L-Glu + NH4+
GDP + phosphate + L-Gln
show the reaction diagram
-
15% of the activity relative to ATP
-
-
-
GTP + L-Glu + NH4+
GDP + phosphate + L-Gln
show the reaction diagram
-
enzyme form EII is almost absolutely specific for ATP, but enzyme form E1 can also use ITP, GTP and UTP
-
-
-
GTP + L-Glu + NH4+
GDP + phosphate + L-Gln
show the reaction diagram
-
45% of the activity relative to ATP
-
-
-
GTP + L-Glu + NH4+
GDP + phosphate + L-Gln
show the reaction diagram
-
26% of the activity with ATP
-
-
?
GTP + L-Glu + NH4+
GDP + phosphate + L-Gln
show the reaction diagram
Bifidobacterium bifidum A
-
15% of the activity relative to ATP
-
-
-
GTP + L-Glu + NH4+
GDP + phosphate + L-Gln
show the reaction diagram
Pseudomonas taetrolens Y-30
-
26% of the activity with ATP
-
-
?
GTP + L-Glu + NH4+
GDP + phosphate + L-Gln
show the reaction diagram
Bifidobacterium breve 203, Bifidobacterium pseudolongum A
-
no activity
-
-
-
ITP + L-Glu + NH4+
IDP + phosphate + L-Gln
show the reaction diagram
-
enzyme form EII is almost absolutely specific for ATP, but E1 can also use ITP, GTP and UTP
-
-
-
ITP + L-Glu + NH4+
IDP + phosphate + L-Gln
show the reaction diagram
-
32% of the activity relative to ATP
-
-
-
ITP + L-Glu + NH4+
IDP + phosphate + L-Gln
show the reaction diagram
Pseudomonas taetrolens, Pseudomonas taetrolens Y-30
-
18% of the activity with ATP
-
-
?
L-Gln + hydroxylamine + ADP
gamma-glutamylhydroxamate + NH4+ + ?
show the reaction diagram
-
-
-
-
?
L-Gln + hydroxylamine + ADP
gamma-glutamylhydroxamate + NH4+ + ?
show the reaction diagram
-
-
-
-
?
L-Gln + hydroxylamine + ADP
L-gamma-glutamylhydroxamate + NH4+ + ?
show the reaction diagram
Q5LGP1
-
-
-
?
L-glutamine + hydroxylamine + ADP
gamma-glutamylhydroxamate + NH4+ + ?
show the reaction diagram
-
-
-
-
?
L-glutamine + hydroxylamine + ADP
gamma-glutamylhydroxamate + NH4+ + ?
show the reaction diagram
Q4ZH57, -
gamma-glutamyltransferase activity
-
-
?
TTP + L-Glu + NH4+
TDP + phosphate + L-Gln
show the reaction diagram
-
10% of the activity relative to ATP
-
-
-
UTP + L-Glu + NH4+
UDP + phosphate + L-Gln
show the reaction diagram
-
10% of the activity relative to ATP
-
-
-
UTP + L-Glu + NH4+
UDP + phosphate + L-Gln
show the reaction diagram
-
enzyme form EII is almost absolutely specific for ATP, but E1 can also use ITP, GTP and UTP
-
-
-
L-glutamine + hydroxylamine + ADP
gamma-glutamylhydroxamate + NH3 + ?
show the reaction diagram
-
partial reverse reaction
-
-
?
additional information
?
-
-
enzyme form GS2 shows maximal activity under photoautotrophic conditions, enzyme form GS1 shows maximal activity under heterotrophic conditions
-
-
-
additional information
?
-
-
essential enzyme involved in the pathogenicity of Mycobacterium tuberculosis
-
-
-
additional information
?
-
-
glutamine synthetase is likely to play a regulatory role in the control of sporulation
-
-
-
additional information
?
-
-
deficiency in hippocampal glutamine synthetase causes recurrent seizures, even in the absence of classical mesial temporal sclerosis, overview
-
-
-
additional information
?
-
-
elevations in c-jun may be a potential cause of the glutamine synthetase deficiency in mesial temporal lobe epilepsy, MTLE, pathology, overview. The enzyme is also regulated by glucocorticoids and proinflammatory cytokines
-
-
-
additional information
?
-
-
extracellular glutamate in the hippocampus causes recurrent seizures and is involved in medically intractable mesial temporal lobe epilepsy, MTLE, overview
-
-
-
additional information
?
-
-
feedback-inhibited glutamine synthetase acts as a molecular chaperone to stabilize the association of dimers of transcripion factor GlnR, the repressor of the glutamine synthetase operon in Bacillus subtilis, with their DNA binding sites, molecular mechanism, overview. The cell shuts off synthesis of GS, and hence of glutamine, when both the enzyme and its product are in excess. The feedback-inhibited enzyme also regulates the activity of TnrA, the global regulator of nitrogen metabolism genes, but by a very different mechanism, overview
-
-
-
additional information
?
-
P0A590, P64246, Q07752, Q33342
glutamine synthetase is involved in nitrogen metabolism, and four enzymes are regulating glutamine synthetase activity and/or nitrogen and glutamate metabolism: adenylyl transferase, i.e. GlnE, gamma-glutamylcysteine synthase, i.e. GshA, UDP-N-acetylmuramoylalanine-D-glutamate ligase, i.e. MurD, and glutamate racemase, i.e. MurI
-
-
-
additional information
?
-
-
glutamine synthetase protects the spinal cord against hypoxia-induced and GABA(A) receptor-activated axonal depressions, it may inhibit the depression of CAP amplitudes by blocking GABAA receptors, overview. GS significantly reduces the axonal depression effects of isoguvacine
-
-
-
additional information
?
-
A8WCU3, -
GS is involved in the assimilation of ammonia in the plant. GS catalyzes the ATP-dependent condensation of NH3 with glutamate to produce glutamine
-
-
-
additional information
?
-
-
loss of glutamine synthetase activity either inherited or induced through L-methionine sulfoximine leads to an upregulation of the glutamine synthetase protein but not of the glutamine synthetase mRNA and results in a significant drop in the proliferation rate but has no effect on apoptosis. Exogenous glutamine does not influence the rate of apoptosis but increases proliferation rates of the fetal but not the mature fibroblasts
-
-
-
additional information
?
-
P81107, -
PpDof5 has an antagonistic regulatory function in the expression of GS1a and GS1b promoters in pine protoplasts transfected with the transcription factor under control of CaMV 35S promoter, overview
-
-
-
additional information
?
-
-
rats with pentylenetetrazole-induced repetitive epileptic seizures show increased heat shock responseand reduced enzyme activity, overview
-
-
-
additional information
?
-
-
the enzyme acts as an acetyl-CoA independent acetyltransferase mediating the transfer of acetyl group(s) from polyphenolic acetates to certain functional proteins in mammalian cells, e.g. protein acetylation by a model acetoxy drug 7, 8-diacetoxy-4-methylcoumarin, or acetylation and inhibition of glutathione transferase using polyphenolic actetate, overview
-
-
-
additional information
?
-
-
the enzyme acts as an acetyl-CoA independent acetyltransferase mediating the transfer of acetyl group(s) from polyphenolic acetates to certain functional proteins in mammalian cells, e.g. protein acetylation by a model acetoxy drug 7, 8-diacetoxy-4-methylcoumarin, or acetylation and inhibition of glutathione transferase using polyphenolic actetate, substrate specificity, overview. The TAase activity of MTAase is independent of the catalytic activity of the glutamine synthetase
-
-
-
additional information
?
-
P15104
the enzyme is a target for activation through the signal transducer protein Wnt in the Wnt pathway, overview
-
-
-
additional information
?
-
-
the glutamine synthetase transmits the nitrogen regulatory signal to GlnR, a transcription factor involved in nitrogen metabolism regulation, the enzyme interacts with GlnR via the factor's C-terminal autoinhibitory domain, the protein-protein interaction of GlnR and glutamine synthetase stabilizes the GlnR-DNA complexes, interaction analysis of enzyme with wild-type and truncated GlnR proteins, overview
-
-
-
additional information
?
-
Q8HZM5
the role of GS in humans depends on tissue localization. In the brain, it regulates the levels of toxic ammonia and converts neurotoxic glutamate to harmless glutamine, whereas in the liver, it is one of the enzymes responsible for the removal of ammonia
-
-
-
additional information
?
-
-
the role of GS in humans depends on tissue localization. In the brain, it regulates the levels of toxic ammonia and converts neurotoxic glutamate to harmless glutamine, whereas in the liver, one of the enzymes is responsible for the removal of ammonia
-
-
-
additional information
?
-
P15106
transcriptional regulation as part of the nitrogen assimilation system, overview
-
-
-
additional information
?
-
-
under healthy conditions, the major site of glutamine utilization is the absorptive columnar epithelium of the small intestine, where glutamine serves as the major respiratory fuel of enterocytes, interorgan flux of glutamine, overview
-
-
-
additional information
?
-
-
Wnt and steroid pathways control glutamate signalling by regulating glutamine synthetase activity in osteoblastic cells, overview
-
-
-
additional information
?
-
-
active site structure analysis, conformational changes near the active sites upon ligand binding, overview
-
-
-
additional information
?
-
Q8HZM5
active site structure analysis, conformational changes near the active sites upon ligand binding, overview
-
-
-
additional information
?
-
-
structure-activity relationship, overview
-
-
-
additional information
?
-
P13564
structure-activity relationship, overview
-
-
-
additional information
?
-
-
structure-activity relationship, overview
-
-
-
additional information
?
-
P09606
structure-activity relationship, overview
-
-
-
additional information
?
-
-
structure-activity relationship, overview
-
-
-
additional information
?
-
P0A1P6
structure-activity relationship, overview
-
-
-
additional information
?
-
P77961
structure-activity relationship, overview
-
-
-
additional information
?
-
P15104
structure-activity relationship, overview
-
-
-
additional information
?
-
P15105
structure-activity relationship, overview
-
-
-
additional information
?
-
P12425
structure-activity relationship, overview
-
-
-
additional information
?
-
-
structure-activity relationship, overview
-
-
-
additional information
?
-
-
the feedback-inhibited enzyme, acting as a chaperone, is required for the binding of transcription factor GlnR to DNA, the feedback inhibition of GS by L-glutamine induces the sequence-specific binding of transcription factor GlnR to DNA in nitrogen metabolism regulation by 32fold and reduces the dissociation rate by 18fold stabilizing the complexes, overview
-
-
-
additional information
?
-
O08467, -
in reactions in which Mn2+ is used, GTP, UTP, and CTP havea limited ability to replace ATP (less than 30%), while in reactions in which Mg2+ was used, complete inhibition by these NTPs is observed. Broad NTP specificity of hyperthermophilic archaeon synthetases suggests that enzymes of ancestral life forms can utilize various NTPs besides ATP
-
-
-
additional information
?
-
Pyrococcus sp. KOD1
O08467
in reactions in which Mn2+ is used, GTP, UTP, and CTP havea limited ability to replace ATP (less than 30%), while in reactions in which Mg2+ was used, complete inhibition by these NTPs is observed. Broad NTP specificity of hyperthermophilic archaeon synthetases suggests that enzymes of ancestral life forms can utilize various NTPs besides ATP
-
-
-
additional information
?
-
Mycobacterium smegmatis VT301
-
the enzyme acts as an acetyl-CoA independent acetyltransferase mediating the transfer of acetyl group(s) from polyphenolic acetates to certain functional proteins in mammalian cells, e.g. protein acetylation by a model acetoxy drug 7, 8-diacetoxy-4-methylcoumarin, or acetylation and inhibition of glutathione transferase using polyphenolic actetate, substrate specificity, overview. The TAase activity of MTAase is independent of the catalytic activity of the glutamine synthetase
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
2 ATP + 2 L-glutamate + 2 NH3
2 ADP + 2 phosphate + D-glutamine + D-isoglutamine
show the reaction diagram
P0A590, P64246, Q07752, Q33342
GlnA2 catalyses the synthesis of D-glutamine and D-isoglutamine and is essential for bacterial growth
-
-
?
ATP + glutamate + NH4+
ADP + phosphate + L-glutamine
show the reaction diagram
-
central enzyme of nitrogen metabolism
-
-
?
ATP + glutamate + NH4+
ADP + phosphate + L-glutamine
show the reaction diagram
-
central enzyme of nitrogen metabolism
-
-
?
ATP + glutamate + NH4+
ADP + phosphate + L-glutamine
show the reaction diagram
-
central enzyme of nitrogen metabolism
-
-
r
ATP + glutamate + NH4+
ADP + phosphate + L-glutamine
show the reaction diagram
-
central enzyme of nitrogen metabolism
-
-
?
ATP + glutamate + NH4+
ADP + phosphate + L-glutamine
show the reaction diagram
-
central enzyme of nitrogen metabolism
-
-
?
ATP + glutamate + NH4+
ADP + phosphate + L-glutamine
show the reaction diagram
-
central enzyme of nitrogen metabolism
-
-
?
ATP + glutamate + NH4+
ADP + phosphate + L-glutamine
show the reaction diagram
-
central enzyme of nitrogen metabolism
-
-
r
ATP + glutamate + NH4+
ADP + phosphate + L-glutamine
show the reaction diagram
Q9HH09, -
central enzyme of nitrogen metabolism
-
-
r
ATP + glutamate + NH4+
ADP + phosphate + L-glutamine
show the reaction diagram
Q9RHZ1, -
central enzyme of nitrogen metabolism
-
-
r
ATP + glutamate + NH4+
ADP + phosphate + L-glutamine
show the reaction diagram
-
central enzyme of nitrogen metabolism
-
-
r
ATP + glutamate + NH4+
ADP + phosphate + L-glutamine
show the reaction diagram
-
central enzyme of nitrogen metabolism, ammonia assimilation
-
-
r
ATP + glutamate + NH4+
ADP + phosphate + L-glutamine
show the reaction diagram
-
central enzyme of nitrogen metabolism, ammonia assimilation
-
-
?
ATP + glutamate + NH4+
ADP + phosphate + L-glutamine
show the reaction diagram
-
central enzyme of nitrogen metabolism, ammonia assimilation
-
-
?
ATP + glutamate + NH4+
ADP + phosphate + L-glutamine
show the reaction diagram
-
central enzyme of nitrogen metabolism, ammonia assimilation
-
-
?
ATP + glutamate + NH4+
ADP + phosphate + L-glutamine
show the reaction diagram
-
central enzyme of nitrogen metabolism, assimilation of ammonia
-
-
r
ATP + glutamate + NH4+
ADP + phosphate + L-glutamine
show the reaction diagram
-
central enzyme of nitrogen metabolism, assimilation of ammonia for protein synthesis
-
-
?
ATP + glutamate + NH4+
ADP + phosphate + L-glutamine
show the reaction diagram
-
central enzyme of nitrogen metabolism, elimination of glutamate from animal brain
-
-
?
ATP + glutamate + NH4+
ADP + phosphate + L-glutamine
show the reaction diagram
Q86ZU6, -
central enzyme of nitrogen metabolism, involved in nitrogen assimilation pathway
-
-
?
ATP + glutamate + NH4+
ADP + phosphate + L-glutamine
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
central enzyme of nitrogen metabolism, provides glutamine for biosynthesis, ammonia assimilation
-
-
?
ATP + glutamate + NH4+
ADP + phosphate + L-glutamine
show the reaction diagram
-
central enzyme of nitrogen metabolism, ammonia assimilation
-
-
?
ATP + glutamate + NH4+
ADP + phosphate + L-glutamine
show the reaction diagram
Thermus thermophilus 111
-
central enzyme of nitrogen metabolism
-
-
?
ATP + glutamate + NH4+
ADP + phosphate + L-glutamine
show the reaction diagram
-
central enzyme of nitrogen metabolism
-
-
r
ATP + L-Glu + NH4+
ADP + phosphate + L-Gln
show the reaction diagram
-
-
-
-
?
ATP + L-Glu + NH4+
ADP + phosphate + L-Gln
show the reaction diagram
-
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
show the reaction diagram
P14654, P14656
serves for assimilation of ammonium in rice root, and ameliorates the toxic effect of ammonium excess
-
-
?
ATP + L-Glu + NH4+
?
show the reaction diagram
-
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+
?
show the reaction diagram
-
first step in urea synthesis
-
-
-
ATP + L-Glu + NH4+
?
show the reaction diagram
-
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+
?
show the reaction diagram
-
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+
?
show the reaction diagram
-
glutamate synthetase cycle provides the only efficient pathway for the conversion of inorganic nitrogen to the organic form
-
-
-
ATP + L-Glu + NH4+
?
show the reaction diagram
-
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-glutamate + NH3
ADP + phosphate + L-glutamine
show the reaction diagram
-
-
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
show the reaction diagram
-
-
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
show the reaction diagram
-
-
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
show the reaction diagram
-
-
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
show the reaction diagram
-
-
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
show the reaction diagram
-
-
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
show the reaction diagram
-
-
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
show the reaction diagram
-
-
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
show the reaction diagram
-
-
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
show the reaction diagram
P13564
-
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
show the reaction diagram
-
-
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
show the reaction diagram
P25462, -
-
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
show the reaction diagram
-
-
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
show the reaction diagram
-
-
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
show the reaction diagram
-
-
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
show the reaction diagram
-
-
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
show the reaction diagram
-
-
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
show the reaction diagram
-
-
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
show the reaction diagram
-
-
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
show the reaction diagram
P09606
-
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
show the reaction diagram
-
-
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
show the reaction diagram
P0A1P6
-
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
show the reaction diagram
P77961
-
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
show the reaction diagram
P15104
-
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
show the reaction diagram
P15105
-
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
show the reaction diagram
P12425
-
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
show the reaction diagram
-
-
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
show the reaction diagram
P64246
-
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
show the reaction diagram
A8WCU3, -
-
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
show the reaction diagram
-, P0A591, P64246
-
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
show the reaction diagram
-
-
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
show the reaction diagram
-, Q1MXG4
-
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
show the reaction diagram
-
brain injuries are usually associated with an increase in the expression of the glutamate-converting enzyme glutamine synthetase
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
show the reaction diagram
-
dogs show altered L-glutamate distribution and reduced enzyme content in primary glaucoma and ischemia, overview
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
show the reaction diagram
-
enzyme regulation involving L-glutamate uptake, Ca2+, and P2X7 receptors, overview
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
show the reaction diagram
-
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
show the reaction diagram
P0A590, P64246, Q07752, Q33342
GlnA1 catalyses the synthesis of L-glutamine and is nonessential for bacterial growth
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
show the reaction diagram
P0A590
glnA1 is essential for Mycobacterium tuberculosis virulence
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
show the reaction diagram
P0A590, P64246, Q07752, Q33342
GlnA3 catalyses the synthesis of L-glutamine and are nonessential for bacterial growth
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
show the reaction diagram
P0A590, P64246, Q07752, Q33342
GlnA4 catalyses the synthesis of L-glutamine and are nonessential for bacterial growth
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
show the reaction diagram
-
glutamine also acts as a signaling molecule, physiological functions of glutamine, overview
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
show the reaction diagram
P46410
glutamine synthetase catalyzes the ATP-dependent conversion of ammonia and glutamate to glutamine in the pericentral zone
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
show the reaction diagram
-
glutamine synthetase is essential for proliferation of fetal skin fibroblasts
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
show the reaction diagram
Q45NB2, Q45NB3, Q45NB4, Q45NB5, Q45NB6, Q45NB7, Q6RUI9, Q6RUJ0, Q6RUJ1, Q6RUJ2
GS sub-families vary during leaf development and senescence, overview
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
show the reaction diagram
Q45NB2, Q45NB3, Q45NB4, Q45NB5, Q45NB6, Q45NB7, Q6RUI9, Q6RUJ0, Q6RUJ1, Q6RUJ2
GS sub-families vary during leaf development and senescence, overview. The cytosolic isozymes GS1 and GSr, dominant enzyme forms during leaf senescence, play major roles in assimilating ammonia during the critical phases of remobilisation of nitrogen to the grain, overview
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
show the reaction diagram
Q0E5H7
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
show the reaction diagram
-
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
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
show the reaction diagram
P15106
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
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
show the reaction diagram
P13564
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
show the reaction diagram
Q43127
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
show the reaction diagram
-
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
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
show the reaction diagram
-
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
show the reaction diagram
Q8HZM5
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
show the reaction diagram
-
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
show the reaction diagram
-
the enzyme is involved in development of mesial temporal lobe epilepsy, MTLE
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
show the reaction diagram
P81107, -
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
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
show the reaction diagram
-
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
show the reaction diagram
-
the enzyme is involved in the regulation of the nitrogen metabolism, overview
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
show the reaction diagram
-
the enzyme is involved in the signal transduction for regulation of the nitrogen metabolism, overview
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
show the reaction diagram
-
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
show the reaction diagram
-
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
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
show the reaction diagram
Mycobacterium smegmatis VT301
-
-
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
show the reaction diagram
P0A591, P64246
-
-
-
?
ATP + L-glutamate + NH4+
ADP + phosphate + L-glutamine
show the reaction diagram
-
central enzyme of nitrogen metabolism
-
-
r
ATP + L-glutamate + NH4+
ADP + phosphate + L-glutamine
show the reaction diagram
-
ammonium assimilation by glutamine synthetase is coupled to the function of the ammonium channel AmtB
-
-
?
ATP + L-glutamate + NH4+
ADP + phosphate + L-glutamine
show the reaction diagram
-, Q56WN1, Q9FMD9, Q9LVI8
glutamine synthetase is a key enzyme in nitrogen assimilation
-
-
?
ATP + L-glutamate + NH4+
ADP + phosphate + L-glutamine
show the reaction diagram
-, Q56WN1, Q9FMD9, Q9LVI8
glutamine synthetase is a key enzyme in nitrogen assimilation. Isoenzyme GLN1,1 accumulates in the surface layers of root during nitrogen limitation
-
-
?
ATP + L-glutamate + NH4+
ADP + phosphate + L-glutamine
show the reaction diagram
-
it is proposed that the induction of glutamine synthetase genes early in development and the subsequent formation of the active protein are preparatory for the increased capacity of the embryo to convert the toxic nitrogen end product, ammonia, into glutamine, which may then be utilized in the ornithine-urea cycle or other pathways
-
-
?
ATP + L-glutamate + NH4+
ADP + phosphate + L-glutamine
show the reaction diagram
P14654, P14656
serves for assimilation of ammonium in rice root, and ameliorates the toxic effect of ammonium excess
-
-
?
ATP + L-glutamate + NH4+
ADP + phosphate + L-glutamine
show the reaction diagram
-
the GLN2 gene product functions in both leaf mitochondria and chloroplasts to faciliate ammonium recovery during photorespiration
-
-
?
ATP + L-glutamate + NH4+
ADP + phosphate + L-glutamine
show the reaction diagram
-
central enzyme of nitrogen metabolism
-
-
r
additional information
?
-
-
enzyme form GS2 shows maximal activity under photoautotrophic conditions, enzyme form GS1 shows maximal activity under heterotrophic conditions
-
-
-
additional information
?
-
-
essential enzyme involved in the pathogenicity of Mycobacterium tuberculosis
-
-
-
additional information
?
-
-
glutamine synthetase is likely to play a regulatory role in the control of sporulation
-
-
-
additional information
?
-
-
deficiency in hippocampal glutamine synthetase causes recurrent seizures, even in the absence of classical mesial temporal sclerosis, overview
-
-
-
additional information
?
-
-
elevations in c-jun may be a potential cause of the glutamine synthetase deficiency in mesial temporal lobe epilepsy, MTLE, pathology, overview. The enzyme is also regulated by glucocorticoids and proinflammatory cytokines
-
-
-
additional information
?
-
-
extracellular glutamate in the hippocampus causes recurrent seizures and is involved in medically intractable mesial temporal lobe epilepsy, MTLE, overview
-
-
-
additional information
?
-
-
feedback-inhibited glutamine synthetase acts as a molecular chaperone to stabilize the association of dimers of transcripion factor GlnR, the repressor of the glutamine synthetase operon in Bacillus subtilis, with their DNA binding sites, molecular mechanism, overview. The cell shuts off synthesis of GS, and hence of glutamine, when both the enzyme and its product are in excess. The feedback-inhibited enzyme also regulates the activity of TnrA, the global regulator of nitrogen metabolism genes, but by a very different mechanism, overview
-
-
-
additional information
?
-
P0A590, P64246, Q07752, Q33342
glutamine synthetase is involved in nitrogen metabolism, and four enzymes are regulating glutamine synthetase activity and/or nitrogen and glutamate metabolism: adenylyl transferase, i.e. GlnE, gamma-glutamylcysteine synthase, i.e. GshA, UDP-N-acetylmuramoylalanine-D-glutamate ligase, i.e. MurD, and glutamate racemase, i.e. MurI
-
-
-
additional information
?
-
-
glutamine synthetase protects the spinal cord against hypoxia-induced and GABA(A) receptor-activated axonal depressions, it may inhibit the depression of CAP amplitudes by blocking GABAA receptors, overview. GS significantly reduces the axonal depression effects of isoguvacine
-
-
-
additional information
?
-
A8WCU3, -
GS is involved in the assimilation of ammonia in the plant. GS catalyzes the ATP-dependent condensation of NH3 with glutamate to produce glutamine
-
-
-
additional information
?
-
-
loss of glutamine synthetase activity either inherited or induced through L-methionine sulfoximine leads to an upregulation of the glutamine synthetase protein but not of the glutamine synthetase mRNA and results in a significant drop in the proliferation rate but has no effect on apoptosis. Exogenous glutamine does not influence the rate of apoptosis but increases proliferation rates of the fetal but not the mature fibroblasts
-
-
-
additional information
?
-
P81107, -
PpDof5 has an antagonistic regulatory function in the expression of GS1a and GS1b promoters in pine protoplasts transfected with the transcription factor under control of CaMV 35S promoter, overview
-
-
-
additional information
?
-
-
rats with pentylenetetrazole-induced repetitive epileptic seizures show increased heat shock responseand reduced enzyme activity, overview
-
-
-
additional information
?
-
-
the enzyme acts as an acetyl-CoA independent acetyltransferase mediating the transfer of acetyl group(s) from polyphenolic acetates to certain functional proteins in mammalian cells, e.g. protein acetylation by a model acetoxy drug 7, 8-diacetoxy-4-methylcoumarin, or acetylation and inhibition of glutathione transferase using polyphenolic actetate, overview
-
-
-
additional information
?
-
-
the enzyme acts as an acetyl-CoA independent acetyltransferase mediating the transfer of acetyl group(s) from polyphenolic acetates to certain functional proteins in mammalian cells, e.g. protein acetylation by a model acetoxy drug 7, 8-diacetoxy-4-methylcoumarin, or acetylation and inhibition of glutathione transferase using polyphenolic actetate, substrate specificity, overview. The TAase activity of MTAase is independent of the catalytic activity of the glutamine synthetase
-
-
-
additional information
?
-
P15104
the enzyme is a target for activation through the signal transducer protein Wnt in the Wnt pathway, overview
-
-
-
additional information
?
-
-
the glutamine synthetase transmits the nitrogen regulatory signal to GlnR, a transcription factor involved in nitrogen metabolism regulation, the enzyme interacts with GlnR via the factor's C-terminal autoinhibitory domain, the protein-protein interaction of GlnR and glutamine synthetase stabilizes the GlnR-DNA complexes, interaction analysis of enzyme with wild-type and truncated GlnR proteins, overview
-
-
-
additional information
?
-
Q8HZM5
the role of GS in humans depends on tissue localization. In the brain, it regulates the levels of toxic ammonia and converts neurotoxic glutamate to harmless glutamine, whereas in the liver, it is one of the enzymes responsible for the removal of ammonia
-
-
-
additional information
?
-
-
the role of GS in humans depends on tissue localization. In the brain, it regulates the levels of toxic ammonia and converts neurotoxic glutamate to harmless glutamine, whereas in the liver, one of the enzymes is responsible for the removal of ammonia
-
-
-
additional information
?
-
P15106
transcriptional regulation as part of the nitrogen assimilation system, overview
-
-
-
additional information
?
-
-
under healthy conditions, the major site of glutamine utilization is the absorptive columnar epithelium of the small intestine, where glutamine serves as the major respiratory fuel of enterocytes, interorgan flux of glutamine, overview
-
-
-
additional information
?
-
-
Wnt and steroid pathways control glutamate signalling by regulating glutamine synthetase activity in osteoblastic cells, overview
-
-
-
additional information
?
-
Mycobacterium smegmatis VT301
-
the enzyme acts as an acetyl-CoA independent acetyltransferase mediating the transfer of acetyl group(s) from polyphenolic acetates to certain functional proteins in mammalian cells, e.g. protein acetylation by a model acetoxy drug 7, 8-diacetoxy-4-methylcoumarin, or acetylation and inhibition of glutathione transferase using polyphenolic actetate, substrate specificity, overview. The TAase activity of MTAase is independent of the catalytic activity of the glutamine synthetase
-
-
-
COFACTOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
AMP
-
bound by hydrophobic forces
ATP
P25462, -
;
ATP
P46410
-
ATP
P81107, -
-
ATP
P0A591, P64246
;
citrate
-
bound by six protein ligands
additional information
-
regulated by adenylation, unadenylated form shows highest activity
-
additional information
-
regulated by adenylation
-
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Ca2+
Q4ZH57, -
can substitute for Mg2+ in biosynthesis of glutamine with 30% of the efficiency obtained with Mg2+
Ca2+
-
stimulates activity at 1 mM
Cd2+
-
activates enzyme form EII more than EI
Cd2+
-
0.5 mM, activity rises by 96%
Cl-
-
increases the affinity of the enzyme 2fold to 4fold for Mg2+ or Mn2+
Cl-
Q0E5H8
chloride stimulates the production of active enzyme by about 300%, in the absence of chloride in the assay buffer, glutamine synthetase activity is decreased by as much as 90%; Cl- dependence of glutamine synthetase activity
Cl-
Q0E5H7
the enzyme's expression partially and activity strictly depends on chloride, strongly salinity-dependent expression of gene glnA2 with a maximal increase of transcripts of about 4fold at 1.5 M NaCl or higher compared to the value at 0.4 M NaCl, expression of glnA1 is not influenced by different salinities, optimal enzyme activity at 2.5 M NaCl or higher, chloride dependent regulatory network, overview
Co2+
-
divalent cation required, Mn2+, Co2+, or Mg2+. Mn2+ is most effective; maximal activity when Co2+ is in excess of ATP
Co2+
-
divalent cation required, Mn2+, Co2+, or Mg2+. Mn2+ is most effective; maximal activity at a ration of ATP to Co2+ of 1.0. The addition of 3 mM Co2+ to the biosynthetic reaction mixtures containing 4 mM Mg2+ results in a 3-7-fold increase in activity
Co2+
-
at pH 7.2, Mg2+ is more effective than Co2+
Co2+
-
divalent cation required, decreasing order of effectiveness at 10 mM in transferase activity: Mn2+, Cu2+, Mg2+, Co2+. For biosynthetic activity: Mg2+, Mn2+, Zn2+/Cu2+, Ni2+
Co2+
-
only enzyme form E1 is activated
Co2+
-
partially effective as activator of biosynthetic activity and transferase activity, half-maximal activation of biosynthetic reaction at 6.3 mM
Co2+
-
can partially replace Mn2+ in transferase reaction
Co2+
-
can partially replace Mg2+ in activation
Co2+
-
strongly increases activity in combination with Mg2+
Co2+
-
required, strongly bound to enzyme, can not be removed by dialysis, removal of metal ions with EDTA results in conformational changes
Co2+
-
activates, isoenzyme GS1; activates, isoenzyme GS2
Co2+
-
supports the enzymatic activity
Co2+
-
stimulates activity at 1 mM
Cu2+
-
divalent cation required, decreasing order of effectiveness at 10 mM in transferase activity: Mn2+, Cu2+, Mg2+, Co2+. For biosynthetic activity: Mg2+, Mn2+, Zn2+/Cu2+, Ni2+
Cu2+
-
partially effective as activator of transferase activity
Cu2+
-
stimulates activity at 1 mM
Fe2+
-
stimulates activity at 1 mM
K+
-
strongly stimulates transferase activity
K+
-
0.25 mM as optimal concentration for highest activity
Li+
-
50 mM LiCl increases activity
Mg2+
-
the enzyme has one structural site per subunit for Mn2+ or Mg2+ and a second site per subunit for metal ion-nucleotide complex, both of which must be filled for activity expression
Mg2+
-
divalent cation required, Mn2+, Co2+, or Mg2+. Mn2+ is most effective. Activity is maximal when Mg2+ is in excess of ATP
Mg2+
-
maximal activity at a ratio of Mg2+ to ATP of 2
Mg2+
-
optimal ratio of MgCl2 to ATP is 2:1 at 1 mM ATP, inhibition at more than 20 mM excess of MgCl2 over ATP; required
Mg2+
-
required
Mg2+
-
at pH 7.2, Mg2+ is more effective than Mn2+
Mg2+
-
optimal ratio of Mg2+ to ATP is 3:1
Mg2+
-
activates
Mg2+
-
Mg2+ in excess of that required for formation of MgATP2- is required for maximal activity
Mg2+
-
divalent cation required, order of effectiveness at 10 mM in transferase activity: Mn2+, Cu2+, Mg2+, Co2+. For biosynthetic activity: Mg2+, Mn2+, Zn2+, Cu2+, Ni2+
Mg2+
-
divalent cation required, specificity for Mg2+ in the biosynthetic assay
Mg2+
-
divalent cation required, enzyme form EI is more active with Mg2+ than with Mn2+, but EII is more active with Mn2+ than Mg2+
Mg2+
-
essential activator for biosynthetic activity, half-maximal activation at 18 mM. Partially effective as activator of transferase activity
Mg2+
-
can partially replace Mn2+ in transferase reaction
Mg2+
-
divalent cation required, specificity for Mg2+ in the biosynthetic assay; maximal activity at 30 mM
Mg2+
-
divalent metal ion required, Mg2+ is most effective. Maximal activation of GS1 at 5 mM and of GS2 at 20 mM
Mg2+
-
divalent cation required, specificity for Mg2+ in the biosynthetic assay
Mg2+
-
required, two ions bound to enzyme
Mg2+
Q9HH09, -
required for activity and for stability
Mg2+
-
required, preferred over Mn2+ at alkaline and neutral pH
Mg2+
-
required, most effective, strongly bound to enzyme, can not be removed by dialysis, removal of metal ions with EDTA results in conformational changes
Mg2+
-
required for optimum activity of enzyme from strain SA0, no activation of enzyme from strain SA1
Mg2+
-
required, less efficient than Mn2+
Mg2+
-
gamma-glutamyltransferase activity of wild-type, unadenylated enzyme is supported by either Mn2+ or Mg2+, while the adenylated enzyme is active only with Mn2+ in absence of Mg2+. The Y397F mutant behaves as the unadenylated form, consistent with its inability to be adenylated. Mutant enzymes Y397A and Y397S behave as if they are adenylated
Mg2+
-
activates, optimum: 15 mM
Mg2+
-
activates, most effectice cation, isoenzyme GS1; activates, most effectice cation, isoenzyme GS2
Mg2+
Q4ZH57, -
clear preference for Mg2+ in glutamine biosynthesis, optimal concentration is 50 mM
Mg2+
-
activates
Mg2+
-
supports the enzymatic activity
Mg2+
-
stimulates activity at 1 mM
Mg2+
P25462, -
;
Mg2+
-, Q1MXG4
binding amino acid residues, overview
Mg2+
Q8HZM5
the active site of the apoenzyme structure contains only a single Mg2+, rather than Mn2+, ion bound at the n1 position
Mg2+
-
-
Mg2+
-, P13564
;
Mg2+
P77961
-
Mg2+
P13564
-
Mg2+
P81107, -
-
Mg2+
A8WCU3, -
-
Mg2+
P0A591, P64246
;
Mg2+
-
activation up to 25 mM, inhibition above
Mg2+
-
required
Mg2+
-, O29313
assay in presence of 55 mM Mg2+
Mg2+
-, Q60182
assay in presence of 55 mM Mg2+
Mg2+
-
assay in presence of 55 mM Mg2+
Mn2+
-
MnCl2 stimulates gamma-glutamyl transferase activity of glutamine synthethase from unshocked cells, no effect on the gamma-glutamyl transferase activity of unshocked cells
Mn2+
-
the enzyme has one structural site per subunit for Mn2+ or Mg2+ and a second site per subunit for metal ion-nucleotide complex, both of which must be filled for activity expression
Mn2+
-
divalent cation required, Mn2+, Co2+, or Mg2+. Mn2+ is most effective. Activity is maximal at a ratio of ATP to Mn2+ of 1.0
Mn2+
-
maximal synthetase activity occurs when the ratio of Mg2+ to ATP is 2
Mn2+
-
optimal concentration is 2 mM, 25% of the maximal activity relative to Mg2+ activation
Mn2+
-
at pH 7.2, Mg2+ is more effective than Mn2+
Mn2+
-
activates
Mn2+
-
cannot effectively replace Mg2+
Mn2+
-
divalent cation required, order of effectiveness at 10 mM in transferase activity: Mn2+, Cu2+, Mg2+, Co2+. For biosynthetic activity: Mg2+, Mn2+, Zn2+, Cu2+, Ni2+
Mn2+
-
supports activity of adenylylated and deadenylylated enzyme, no other divalent cation can support gamma-glutamyl transferase activity, optimal concentration is 0.3 mM
Mn2+
-
divalent cation required, enzyme form EI is more active with Mg2+ than with Mn2+, but EII is more active with Mn2+ than Mg2+
Mn2+
-
required for transferase activity
Mn2+
-
required for transferase activity
Mn2+
-
activity of the low-activity form is higher than that of the high-activity form in the Mn2+-dependent biosynthetic assay
Mn2+
-
maximal activity at 1 mM; required for transferase activity
Mn2+
-
can partially replace Mg2+ in activation
Mn2+
-
required for transferase activity
Mn2+
-
required, two ions bound to enzyme
Mn2+
Q9HH09, -
required for activity and for stability
Mn2+
-
required, preferred over Mg2+ at acidic pH
Mn2+
-
slight activation, strongly bound to enzyme, can not be removed by dialysis, removal of metal ions with EDTA results in conformational changes
Mn2+
-
required for optimum activity of enzyme from strain SA1, highest activity at 0.3 mM, concentration inhibitory for enzyme from SA0
Mn2+
-
required, highest activity at 0.6-1 mM, higher concentrations inhibitory
Mn2+
-
gamma-glutamyltransferase activity of wild-type, unadenylated enzyme is supported by either Mn2+ or Mg2+, while the adenylated enzyme is active only with Mn2+ in absence of Mg2+. The Y397F mutant behaves as the unadenylated form, consistent with its inability to be adenylated. Mutant enzymes Y397A and Y397S behave as if they are adenylated
Mn2+
-
activates with 11% of the efficiency of the activation with Mg2+, optimum: 3-4 mM
Mn2+
Q4ZH57, -
optimal concentration is 1 mM, activates gamma-glutamyltransferase activity, glutamine synthetase type III. Can substitute for Mg2+ in biosynthesis of glutamine with 30% of the efficiency obtained with Mg2+
Mn2+
-
activates
Mn2+
-
Km: 0.025 mM
Mn2+
-
supports the enzymatic activity
Mn2+
-
most effective cation for stimulation of activity at 1 mM
Mn2+
-
essential for activity, contains three Mn2+ ions per subunit
Mn2+
-
-
Mn2+
-
three enzyme-bound Mn2+ ions, an additional Mn2+ ion makes contacts with Glu196 and the inorganic phosphate
Na+
-
0.5 mM as optimal concentration for highest activity
Na+
Q0E5H8
3 mM, highest activity
Na+
-
highest activity at 50 mM
Ni2+
-
divalent cation required, decreasing order of effectiveness at 10 mM in transferase activity: Mn2+, Cu2+, Mg2+, Co2+. For biosynthetic activity: Mg2+, Mn2+, Zn2+/Cu2+, Ni2+
Ni2+
-
stimulates activity at 1 mM
Zn2+
-
divalent cation required, decreasing order of effectiveness at 10 mM in transferase activity: Mn2+, Cu2+, Mg2+, Co2+. For biosynthetic activity: Mg2+, Mn2+, Zn2+/Cu2+, Ni2+
Zn2+
-
partially effective as activator of biosynthetic activity, half-maximal activation at 6.3 mM
Zn2+
-
stimulates activity at 1 mM
Mn2+
-
required, optimum concentration around 0.5 mM
additional information
Q4ZH57, -
little or no detectable activity with Mg2+, Ca2+, Co2+ or Fe2+
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
(1,4-diamino-4-oxobutyl)phosphonic acid
P09606
-
(1-amino-4-methoxy-4-oxobutyl)phosphonic acid
P09606
-
(1R,3R)-1-amino-3-(hydroxy(methyl)phosphoryl)cyclohexanecarboxylic acid
-
-
(1R,3R)-1-amino-3-(hydroxy(methyl)phosphoryl)cyclopentanecarboxylic acid
-
racemic mixture
(2R,3S)-3-aminooxetane-2-carboxylic acid
-
-
(2S)-2-amino-4-(hydroxyamino)butanoic acid
-
-
(2S)-2-amino-4-(methylsulfonyl)butanoic acid
-
-
(2S)-2-amino-4-[(1-aminoethyl)(hydroxy)phosphoryl]butanoic acid
-
-
(2S)-2-amino-4-[(2-aminoethyl)(hydroxy)phosphoryl]butanoic acid
-
-
(2S)-2-amino-4-[(3S)-3-hydroxy-2-oxoazetidin-3-yl]butanoic acid
-
irrversible
(2S)-2-amino-4-[(aminomethyl)(hydroxy)phosphoryl]butanoic acid
-
-
(2S)-2-amino-4-[hydroxy(hydroxymethyl)phosphoryl]butanoic acid
-
-
(2S)-2-amino-4-[hydroxy(nitroso)amino]butanoic acid
P15105
-
(2S,5R)-2,6-diamino-5-hydroxyhexanoic acid
-
docks at the amino acid binding site of the enzyme, structure, overview
(3,4-diamino-4-oxobutyl)methylphosphinic acid
P09606
-
(3-amino-4-methoxy-4-oxobutyl)methylphosphinic acid
P09606
-
(3-methanesulfinylphenylamino)acetic acid
-
30% inhibition at 1.0 mM
(NH4)2SO4
-
weak, gamma-glutamyl transferase activity
(R)-3-hydroxy-2-(3-sulfamoylphenylamino)propionic acid
-
33% inhibition at 1.0 mM
(R)-methionine sulfoximine phosphate
-
weak inhibition compared to the S-enantiomer
(S)-3-hydroxy-2-(3-methanesulfinylphenylamino)propionic acid
-
13% inhibition at 1.0 mM
(S)-methionine sulfoximine phosphate
-
irreversible, reaction mechanism with required phosphorylation of the inhibitor molecule in the same way as substrate L-glutamate is phosphorylated
([[2-(4-hydroxyphenyl)ethyl]amino]methanediyl)bis(phosphonic acid)
-
-
1-[(3,4-dichlorophenyl)methyl]-3,7-dimethyl-8-morpholin-4-yl-purine-2,6-dione
-
-
2-(3-aminophenyl)-6-bromo-N-cyclopentylimidazo[1,2-a]pyridin-3-amine
-
-
2-amino-2-ethyl-4-(S-methylsulfonimidoyl)butanoic acid
-
41% inhibition at 0.4 mM
2-amino-2-ethyl-4-[hydroxy(methyl)phosphoryl]butanoic acid
-
-
2-amino-4-(hydroxyamino)butanoic acid
-
-
2-amino-4-(S-ethylsulfonimidoyl)butanoic acid
-
76.4% inhibition at 10 mM
2-amino-4-(S-propylsulfonimidoyl)butanoic acid
-
35.8% inhibition at 20 mM
2-amino-4-hydroxyglutaric acid
-
-
2-amino-4-[(3,4-dichlorobenzyl)(hydroxy)phosphoryl]butanoic acid
-
20% inhibition at 12.5 mM
2-amino-4-[(3,5-dimethylbenzyl)(hydroxy)phosphoryl]butanoic acid
-
20% inhibition at 12.5 mM
2-amino-4-[(4-bromobenzyl)(hydroxy)phosphoryl]butanoic acid
-
20% inhibition at 12.5 mM
2-amino-4-[(carboxymethyl)(hydroxy)phosphoryl]butanoic acid
-
20% inhibition at 12.5 mM
2-amino-4-[(phosphonomethyl)sulfonyl]butanoic acid
-
-
2-amino-4-[(phosphonomethyl)sulfonyl]butanoic acid
-
51% inhibition at 0.5 mM
2-amino-4-[benzyl(hydroxy)phosphoryl]butanoic acid
-
30% inhibition at 12.5 mM
2-amino-4-[ethyl(hydroxy)phosphoryl]butanoic acid
-
-
2-amino-4-[hydroxy(oxido)phosphanyl]butanoic acid
-
35% inhibition at 12.5 mM
2-amino-4-[hydroxy(phenyl)phosphoryl]butanoic acid
-
30% inhibition at 0.5 mM
2-amino-4-[hydroxy(phosphonomethyl)amino]butanoic acid
-
50% inhibition at 0.5 mM
2-amino-4-[hydroxy(phosphonomethyl)phosphoryl]butanoic acid
-
-
2-amino-4-[methyl(phosphonomethyl)amino]butanoic acid
-
29% inhibition at 0.5 mM
2-amino-4-[methyl(phosphonomethyl)phosphoryl]butanoic acid
-
-
2-mercaptoethanol
-
-
2-mercaptoethanol
-
no inhibition of wild type enzyme, inhibits activity of D56A and D56E mutant enzymes
2-oxo-2,3-dihydro-1H-benzimidazole-5-sulfonamide
-
24% inhibition at 1.0 mM
2-[(diphosphonomethyl)amino]pyridine-3-carboxylic acid
-
-
3-amino-5-[hydroxy(methyl)phosphoryl]tetrahydrofuran-3-carboxylic acid
-
-
3-[(1H-1,2,4-triazol-3-ylcarbonyl)amino]benzoic acid
-
26% inhibition at 1.0 mM
3-[(diphosphonomethyl)amino]benzoic acid
-
-
3-[(phosphonoacetyl)amino]alanine
-
-
3-[6-bromo-3-(cyclopentylamino)imidazo[1,2-a]pyridin-2-yl]benzoic acid
-
-
3-[6-bromo-3-(cyclopentylamino)imidazo[1,2-a]pyridin-2-yl]phenol
-
-
4-(S-ethylsulfonimidoyl)isovaline
-
25.8% inhibition at 2 mM
4-(S-methylsulfonimidoyl)isovaline
-
80% inhibition at 0.1 mM
4-(S-propylsulfonimidoyl)isovaline
-
34.6% inhibition at 20 mM
4-amino-4-phosphonobutanoic acid
P09606
-
4-amino-4-phosphonopentanoic acid
P09606
-
4-amino-4-[hydroxy(methyl)phosphoryl]butanoic acid
P09606
-
4-amino-4-[hydroxy(methyl)phosphoryl]pentanoic acid
P09606
-
4-fluoroglutamic acid
-
-
4-phosphonohomoserine
-
-
4-phosphonoisovaline
P09606
-
4-phosphononorvaline
-
-
4-[hydroxy(methyl)phosphoryl]isovaline
-
-
4-[hydroxy(methyl)phosphoryl]isovaline
P09606
-
4-[hydroxy(methyl)phosphoryl]isovaline
Sorghum sp., Spinacia oleracea
-
-
5'-p-fluorosulfonylbenzoyladenosine
-
in presence of Mg2+ or Mn2+
5'-p-fluorosulfonylbenzoyladenosine
-
Mn2+-dependent activity
5-oxo-6-phosphononorleucine
-
-
5-oxolysine
-
isozyme GS1; isozyme GS2
5-[(3-amino-3-carboxypropyl)(hydroxy)phosphoryl]norvaline
-
20% inhibition at 12.5 mM
5-[6-bromo-3-(cyclopentylamino)imidazo[1,2-a]pyridin-2-yl]-2-methoxyphenol
-
-
5-[6-iodo-3-(cyclopentylamino)imidazo[1,2-a]pyridin-2-yl]-2-methoxyphenol
-
-
8-azidoadenosine
-
in presence of Mg2+ or Mn2+
adenosine
-
more potent inhibitor in the reaction with Mg2+ than with Mn2+
ADP
-
more potent inhibition in the reaction with Mg2+ than with Mn2+
ADP
-
biosynthetic activity
ADP
-
enzyme form GSIII
ADP
-
strong, enzyme form GSIII
ADP
A0MZ70
competitive inhibitor with respect to ATP and noncompetitive inhibitor versus both glutamate and ammonium
Ala
-
gamma-glutamyl transferase activity
Ala
-
more inhibition by L-Ala and glycine in the mixture with Mn2+ than with Mg2+
Ala
-
beta-Ala; inhibition of enzyme form GSII and GSIII
Ala
-
strong inhibition of transferase activity
Ala
-
noncompetitive with respect to glutamate
alanine
-
more inhibitory for enzyme from strain SA0 than for enzyme from SA1
AMP
-
more potent inhibitor in the reaction with Mg2+ than with Mn2+
AMP
-
biosynthetic activity
AMP
Q9HH09, -
slight inhibition of the biosynthetic reaction
AMP
-
no feedback inhibition of unadenylated enzyme form, enhanced sensitivity to feedback inhibition by adenylated enzyme form
AMP
-
competitive with respect to ATP
ascorbate
-
little loss of activity with 2 mM ascorbate alone. Complete inactivation by co-incubation with 1 mM H2O2, 0.002 mM Fe3+, 2 mM ascorbate for 30 min
Asp
-
inhibition of biosynthetic and transferase activity
aspartate
-
more inhibitory for enzyme from strain SA0 than for enzyme from SA1
ATP
-
biosynthetic reaction
ATP
-
mutant S186F enzyme is resistant to feedback inhibition by glutamine and AMP
ATP
-
ATP treatment decreases glutamine synthetase activities and protein expression
Beta amyloid peptides
-
-
-
Ca2+
-
above 2 mM CaCl2, in presence of 20 mM MgCl2 and 10 mM ATP
Ca2+
-
strong inhibition of Mg2+-activated enzyme
Ca2+
-
inhibits in presence of Mg2+
Carbamoyl phosphate
-
-
Carbamoyl phosphate
-
-
Carbamoyl phosphate
-
non-competitive with respect to L-Glu
Carbamoyl-phosphoalanine
-
-
Cd2+
-
0.5 mM, activity is reduced by 60%
Co2+
-
strong inhibition of Mg2+-activated enzyme
Co2+
-
0.5-60 mM, inhibition of Mn2+-dependent transferase activity
CTP
-
biosynthetic reaction
CTP
-
no feedback inhibition of unadenylated enzyme form, enhanced sensitivity to feedback inhibition by adenylated enzyme form
cysteine
-
more inhibitory for enzyme from strain SA0 than for enzyme from SA1
cysteine
-
no inhibition of wild type enzyme, inhibits activity of D56A and D56E mutant enzymes
D,L-phosphinothricin
-
-
D-Methionine sulfone
-
-
diphosphate
-
-
diphosphate
-
enzyme form GSIII
dithioerythritol
-
no inhibition of wild type enzyme, inhibits activity of D56A and D56E mutant enzymes
dithiothreitol
-
-
DMSO
-
about 15% activation at 2%
Fe3+
-
no loss of activity with 0.002 mM Fe3+ alone. Complete inactivation by co-incubation with 1 mM H2O2, 0.002 mM Fe3+, 2 mM ascorbate for 30 min
-
Glucagon
-
slightly decreases enzyme activity
glucosamine 6-phosphate
-
-
glutamate
-
product inhibition above 20 mM when enzyme is activated with Mg2+, no inhibition when activated with Mn2+
glutamate
-, Q56WN1, Q9FMD9
at high concentrations, isoenzyme GLN1,3
glutamine
-
feed-back inhibition of wild-type enzyme, mutant S186F enzyme is resistant to feedback inhibition
Gly
-
gamma-glutamyl transferase activity
Gly
-
more inhibition by L-Ala and Gly in the mixture with Mn2+ than with Mg2+
Gly
-
inhibition of biosynthetic and transferase activity
glycine
Q9HH09, -
feed-back inhibition, competitive with L-glutamine
glycine
-
more inhibitory for enzyme from strain SA0 than for enzyme from SA1
H2O2
-
1 mM, 3 h, 63% loss of activity. Inactivation is prevented by the iron chelators 2,2'-dipyridylor 1,10-phenanthroline, but not by their non-chelating analogues
H2O2
-
1 mM, 30 min, 41% loss of activity. Complete inactivation by co-incubation with 1 mM H2O2, 0.002 mM Fe3+, 2 mM ascorbate for 30 min
His
-
L-His, gamma-glutamyl transferase activity
His
-
no feedback inhibition of unadenylated enzyme form, enhanced sensitivity to feedback inhibition by adenylated enzyme form
ITP
-
biosynthetic reaction
L-alanine
Q9HH09, -
feed-back inhibition, competitive with L-glutamine
L-alanine
-
decreases the enzyme activity considerably
L-Arg
-
gamma-glutamyl transferase activity
L-Arg
-
biosynthetic activity
L-arginine
-
inhibitory at high concentrations
L-Glu
-
gamma-glutamyl transferase activity
L-Glu
-
competitive versus L-Gln and non-competitive versus hydroxylamine; gamma-glutamyl transferase activity
L-Glu
-
50-100 mM, substrate inhibition
L-Glu
-
inhibition of transferase activity, no inhibition of biosynthetic activity
L-glutamate
-
in the presence of Mn2+ the activity decreases when exceeding a concentration of 10 mM glutamate
L-glutamine
Q86ZU6, -
-
L-glutamine
-
inhibitory at high concentrations
L-glutamine
-
the enzyme is feedback inhibited
L-glutamine
-
the enzyme is feedback inhibited, the feedback inhibition of GS induces the sequence-specific binding of transcription factor GlnR to DNA in nitrogen metabolism regulation by 32fold and reduces the dissociation rate by 18fold stabilizing the complexes, overview
L-glutamine
A0MZ70
noncompetitive
L-glutamine
-
feedback inhibition
L-glutamyl gamma-phosphinic acid
-
-
L-Glycine
-
decreases the enzyme activity considerably
L-Ile
-
weak, gamma-glutamyl transferase activity
L-Lys
-
no inhibition
L-methionine S-sulfoximine
-
IC50: 3 mM
L-Methionine sulfone
-
-
L-Methionine sulfone
-
inhibits enzyme from strain SA0 but not from SA1, more than 80% inhibition at 0.05 mM
L-methionine sulfoximine
-
gamma-glutamyl transferase assay
L-methionine sulfoximine
-
inhibition of enzyme form GSII and GSIII
L-methionine sulfoximine
-
-
L-methionine sulfoximine
-
irreversible at high concentrations, competitive with L-Glu; S,R-sulfoximine and S-sulfoximine inhibit, R-sulfoximine is ineffective
L-methionine sulfoximine
-
-
L-methionine sulfoximine
-
-
L-methionine sulfoximine
-
-
L-methionine sulfoximine
-
-
L-methionine sulfoximine
-
the concentration needed to inhibit GSIII is 50-100times higher than that needed to inhibit GSI or GSII
L-methionine sulfoximine
-
-
L-methionine sulfoximine
-
enzyme form GS III
L-methionine sulfoximine
Q86ZU6, -
50% inhibition at 47 mM
L-methionine sulfoximine
-
forward reaction: complete inhibition of wild type enzyme, only slight inhibition of mutant enzyme, reverse reaction: slight inhibition of mutant and wild-type enzyme
L-methionine sulfoximine
-
loss of glutamine synthetase activity either inherited or induced through L-methionine sulfoximine leads to an upregulation of the glutamine synthetase protein but not of the glutamine synthetase mRNA and results in a significant drop in the proliferation rate but has no effect on apoptosis
L-methionine sulfoximine
-
-
L-methionine sulfoximine
-
-
L-methionine sulfoximine
-
no inhibition of the acetyltransferase activity
L-methionine-(S)-sulfoximine
-
docks at the amino acid binding site of the enzyme, structure, overview
L-methionine-(S,R)-sulfoximine
P0A590, P64246, Q07752, Q33342
-
L-methionine-(S,R)-sulphoximine
P0A590, P64246, Q07752, Q33342
-
L-methionine-DL-sulfoximine
-
inhibits enzyme from strain SA0 but not from SA1, more than 80% inhibition at 0.05 mM
L-methionine-DL-sulfoximine
Q9RHZ1, -
MSX, complete inactivation of wild-type and mutant enzymes except D51E mutant, which shows only 10% inhibition
L-methionine-DL-sulfoximine
-
complete inhibition
L-methionine-S-sulfoximine
-
-
L-methionine-S-sulfoximine
-
-
L-methionine-sulfoximine
-
-
L-phosphinothricin
Q86ZU6, -
50% inhibition at 0.5 mM
L-Pro
-
weak, gamma-glutamyl transferase activity
L-serine
-
decreases the enzyme activity considerably
L-Tyr
-
inhibits transferase activity, no inhibition of biosynthetic activity
Met
-
irreversible, competitive
methionine sulfone
-
-
methionine sulfone amine
-
-
methionine sulfoxide
-
-
methionine sulfoxide
-
-
methionine sulfoximine
-
-
methionine sulfoximine
-
2.5 mM causes up to 60% inhibition of the transferase GS activity and in the presence of 6 mM, the transferase GS activity is around 20% of the controls
methionine sulfoximine
P04771
-
methionine sulfoximine
-
an irreversible, competitive inhibitor of glutamine synthetase activity
methionine sulfoximine
-
-
methionine sulfoximine
-
irreversible inhibition up to 97% in vivo after longterm treatment over 3 h by Intracranial infusion
methionine sulfoximine
-
treatment with methionine sulfoximine of transgenic mice that overexpresses the mutant human superoxide dismutase SOD1G93A gene, an animalmodel for the primary inherited form of the human neurodegenerative disease amyotrophic lateral sclerosis. This treatment in vivo reduces glutamine synthetase activity measured in vitro by 85% and reduces brain levels of glutamine by 60% and of glutamate by 30% in both the motor cortex and the anterior striatum, while also affecting levels of GABA and glutathione. Methionine sulfoxime treatment significantly extends the lifespan of these mice by 8%
Mg2+
-
above 0.5 mM, gamma-glutamyl transferase activity
Mg2+
-
inibits enzyme form GSIII to nearly 72%, enzyme form GSI 30%, and enzyme form GSII 33.3%
Mg2+
-
inhibition at more than 20 mM excess of MgCl2 over ATP
Mg2+
-
inhibits gamma-glutamyl transferase activity
Mg2+
-
addition of Mg2+ to the Mn2+-dependent transferase activity
Mg2+
-
between 0.5-60 mM, inhibition of Mn2+-dependent transferase activity
Mg2+
-
in gamma-glutamyl transferase assay
Mg2+
Q86ZU6, -
-
Mg2+
-
activiation up to 25 mM, inhibition above
Mn2+
-
above 2 mM MnCl2, in presence of 20 mM MgCl2 and 10 mM ATP
Mn2+
-
strong inhibition of Mg2+-activated enzyme
N-(4-hydroxy-3-sulfophenyl)glycine
-
48% inhibition at 1.0 mM
N-[[(Iodoacetyl)amino]ethyl]-5-naphthylamine-1-sulfonic acid
-
inactivates Mg2+-dependent activity and activates Mn2+-dependent activity
NaCl
-
0.25 mM decreases GS activity to 29.9% in leaves, 40% in roots
NaCl
-
84.11% decrease of activity at 300 mM
NaNO3
Q0E5H8
the specific activity of glutamine synthetase is reduced 66% in the presence of NaNO3
NH4+
-
in the presence of Mn2+ the activity decreases when exceeding a concentration of 20 mM NH4+
NH4+
-
reversible inactivation
NH4Cl
-
glutamyl transferase reaction, competitive versus L-Gln and non-competitive versus hydroxylamine
NH4Cl
-
substrate inhibition at high concentrations
Ni2+
-
0.5-60 mM, inhibition of Mn2+-dependent transferase activity
Ni2+
-
higher affinity for nickel than for the regular co-factor manganese. Upon binding, nickel interferes with the manganese-catalyzed enzymatic activity of recombinant GLUL protein. GLUL activity in testes of animals exposed to nickel sulfate is reduced
nitrogen
-
the activity of GlnA1 is downregulated under conditions of nitrogen excess, through covalent binding of an AMP-moiety to a conserved Tyr405 residue by GlnE, an adenylyltransferase
nitrogen
P15106
the activity of GlnA1 is downregulated under conditions of nitrogen excess, through covalent binding of an AMP-moiety to a conserved Tyr405 residue by GlnE, an adenylyltransferase. Both GSII activity and glnII transcription levels increase during nitrogen starvation of morphologically differentiating cultures while there was no change in glnA1 transcription
O-acetyl-4-phosphonohomoserine
Escherichia coli, Sorghum sp.
-
-
P-ethyl gamma-phosphinic L-glutamate
-
-
p-hydroxymercuribenzoate
-
biosynthetic activity
p-hydroxymercuribenzoate
-
complete inhibition of wild type and D56A mutant, 40% inhibition of D56E at 1 mM
P2X7 receptor
-
stimulation of P2X7 receptors for 2 h inhibits both activity and protein expression of glutamine synthetase, periodate-oxidized 2',3'-dialdehyde ATP abolishes the inhibition
-
peroxynitrite
-
0.005 mM, activity is decreased by about 25%
peroxynitrite
-
0.005 mM, inactivation of the enzyme
phosphate
-
transferase assay an biosynthetic assay
phosphate
A0MZ70
noncompetitive
Phosphinothricin
-
i.e. L-2-amino-4-(hydroxymethyl-phosphinyl)butanoic acid, competitive with respect to Glu, reversible first order inactivation
Phosphinothricin
-
irreversible, competitive
Phosphinothricin
-
-
Phosphinothricin
-
mechanism of inactivation
Phosphinothricin
-
-
Phosphinothricin
Q9RHZ1, -
PPT, complete inactivation of wild-type and mutant enzymes except D51E mutant, which shows 70% inhibition
Phosphinothricin
-
isolated from Streptomyces viridochromogenes
Phosphinothricin
-, P13564
isolated from Streptomyces viridochromogenes; isolated from Streptomyces viridochromogenes
Phosphinothricin
-
isolated from Streptomyces viridochromogenes
Phosphinothricin
P09606
isolated from Streptomyces viridochromogenes
Phosphinothricin
-
isolated from Streptomyces viridochromogenes
Ser
-
inhibition of biosynthetic and transferase activity
Ser
-
competitive
serine
-
more inhibitory for enzyme from strain SA0 than for enzyme from SA1
Snake venom diesterase
-
-
-
sodium gluconate
Q0E5H8
the specific activity of glutamine synthetase is reduced 34% in the presence of sodium gluconate
Sulfoxamine
-
irreversible, competitive
Tabtoxinine-beta-lactam
-
-
thiol reagents
-
suppress activity of enzyme form GS1
thymidine
-
complete inhibition of enzyme form GSII, partial inhibition of enzyme form GSI, no effect on enzyme form GSIII
Trp
-
no feedback inhibition of unadenylated enzyme form, enhanced sensitivity to feedback inhibition by adenylated enzyme form
UMP
-
competitive with respect to L-Gln
Urea
-
physiological concentrations of urea inhibit, at least when ATP and/or glutamate are nonsaturating. Inhibition is partially reversed by trimethylamine-N-oxide
UTP
-
biosynthetic reaction
Val
-
inhibition of biosynthetic and transferase activity
vitamin D
-
; 22% inhibition at 0.00001 mM, reduces dexamethasone induced increase in enzyme expression
Zn2+
-
0.5-60 mM, inhibition of Mn2+-dependent transferase activity
[(cyclohexylamino)methanediyl]bis(phosphonic acid)
-
-
[(pyridin-2-ylamino)methanediyl]bis(phosphonic acid)
-
-
[1-amino-3-(S-methylsulfonimidoyl)propyl]phosphonic acid
-
-
[3-(diethoxyphosphoryl)phenylamino]acetic acid
-
42% inhibition at 1.0 mM
[3-[6-bromo-3-(cyclopentylamino)imidazo[1,2-a]pyridin-2-yl]phenyl]methanol
-
-
[[(2,3-dichlorophenyl)amino]methanediyl]bis(phosphonic acid)
P38561
non-competitive mechanism against glutamate and uncompetitive mechanism against ATP
[[(2,4-dichlorophenyl)amino]methanediyl]bis(phosphonic acid)
P38561
non-competitive mechanism against glutamate and uncompetitive mechanism against ATP
[[(2,6-dichlorophenyl)amino]methanediyl]bis(phosphonic acid)
P38561
non-competitive mechanism against glutamate and uncompetitive mechanism against ATP
[[(3,5-dichlorophenyl)amino]methanediyl]bis(phosphonic acid)
-
-
[[(3,5-dichlorophenyl)amino]methanediyl]bis(phosphonic acid)
P38561
non-competitive mechanism against glutamate and uncompetitive mechanism against ATP
[[(3-nitrophenyl)amino]methanediyl]bis(phosphonic acid)
-
-
[[(4-chlorophenyl)amino]methanediyl]bis(phosphonic acid)
P38561
non-competitive mechanism against glutamate and uncompetitive mechanism against ATP
[[(4-methylphenyl)amino]methanediyl]bis(phosphonic acid)
-
-
[[(5-chloropyridin-2-yl)amino]methanediyl]bis(phosphonic acid)
-
-
[[(pyridin-2-ylmethyl)amino]methanediyl]bis(phosphonic acid)
-
-
Mn2+
-
inhibitory for enzyme from strain SA0
additional information
-
Bacillus fragilis enzyme produced in E. coli is specifically and irreversibly inactivated by Bacillus fragilis cell extract
-
additional information
-
combined inhibition by Gly, Ala and Ser is cumulative
-
additional information
-
inactivation by ADP-ribosylation. The site of ADP-ribosylation is Arg172
-
additional information
Q9HH09, -
no effect with L-histidine or L-tryptophane
-
additional information
-
no inhibition by L-homoserine, (R)-3-hydroxy-2-(3-methanesulfinylphenylamino)propionic acid, (R)-3-hydroxy-2-(3-methylsulfanylphenylamino)propionic acid, (3-sulfamoylphenylamino)acetic acid, (3-methylsulfanylphenylamino)acetic acid, 2-amino-3-(2-phosphonomethylphenyl)propanoic acid, 2-amino-3-(2-aminomethylphenyl)propanoic acid, and methyl 2-amino-3-(2-phosphonomethylphenyl)propanoate, inhibitor screening and docking studies, overview
-
additional information
-
the canonical Wnt signalling pathway is a negative regulator of glutamine synthetase activity; the canonical Wnt signalling pathway is a negative regulator of glutamine synthetase activity. No effects by aldosterone, estradiol, progesterone, dihydrotestosterone, or triiodothyronine
-
additional information
-
elevations in c-jun may be a potential cause of the glutamine synthetase deficiency in mesial temporal lobe epilepsy, MTLE. The activity of glutamine synthetase is decreased by 38% in tissue homogenates of the sclerotic versus the nonsclerotic hippocampus. High levels of c-jun repress the glutamine synthetase gene. The inductive effect of glucocorticoids is mediated by binding of the glucocorticoi 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
-
additional information
-
a single transcriptional repressor AmtR from the TetR family is involved in enzyme regulation, AmtB is encoded by amtB clustered together with glnK in an operon, glnK encodes for a PII signaling protein which are small trimeric proteins that are able to bind 2-oxoglutarate and play a pivotal role in the regulation of nitrogen metabolism by way of controlling the activity of signal transduction components and key metabolic enzymes. GlnK is not uridylylated but rather adenylylated/de-adenylylated by GlnD
-
additional information
P15106
GlnR is able to function as both an activator and repressor of transcription
-
additional information
Q8HZM5
design and construction of structure-based inhibitors targeting the nucleotide binding site, which varies to a large degree between mammalian and bacterial enzymes
-
additional information
-
design and construction of structure-based inhibitors targeting the nucleotide binding site, which varies to a large degree between mammalian and bacterial enzymes
-
additional information
-
3'-O-(4-benzoylbenzoyl)-ATP suppresses the enzyme expression. Removal of extracellular Ca2+ and inhibition of protein kinase C restores the ATP-decreased enzyme expression but fails to restore the P2X7-decreased L-glutamate uptake
-
additional information
-
inhibitory effects of endothelins on the expression of glutamine synthetase, cultured cortical astrocytes maintained with endothelins show an almost complete loss of glutamine synthetase, this coordinated inhibition of astroglial glutamate uptake and turnover, e.g. by ET-1, dissociates when extracellular glutamate concentrations increase, overview
-
additional information
-
the enzyme is not affeted by dietary glutamine supplementation or by Mycobacterium bovis bacillus Calmette-Guerin infection, overview
-
additional information
-
structure-activity relationships and inhibitor design, overview
-
additional information
P15104
structure-activity relationships and inhibitor design, overview
-
additional information
-, P13564
structure-activity relationships and inhibitor design, overview; structure-activity relationships and inhibitor design, overview
-
additional information
P15105
structure-activity relationships and inhibitor design, overview
-
additional information
-
structure-activity relationships and inhibitor design, overview
-
additional information
P09606
structure-activity relationships and inhibitor design, overview
-
additional information
P0A1P6
structure-activity relationships and inhibitor design, overview
-
additional information
-
structure-activity relationships and inhibitor design, overview
-
additional information
P77961
structure-activity relationships and inhibitor design, overview
-
additional information
-
structure-activity relationships and inhibitor design, overview
-
additional information
-
presence of only one glutathione synthetase inactivation factor, 7A, encoded by open reading frame asl2329, gifA, in strain PCC 7120. Upon 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
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
(R)-2-[3-(diethoxyphosphoryl)phenylamino]-3-hydroxypropionic acid
-
-
(S)-2-[3-(diethoxyphosphoryl)phenylamino]-3-hydroxypropionic acid
-
-
(S)-3-hydroxy-2-(3-methylsulfanylphenylamino)propionic acid
-
-
(S)-3-hydroxy-2-(3-sulfamoylphenylamino)propionic acid
-
-
3-((R)-1-carboxy-2-hydroxyethylamino)benzoic acid
-
-
3-((S)-1-carboxy-2-hydroxyethylamino)benzoic acid
-
-
3-(carboxymethylamino)benzoic acid
-
-
alpha-ketoglutarate
-
activates
alpha-ketoglutarate
-
-
arsenate
-
activates gamma-glutamyl transferase reaction
Cys
-
enhances activity
cysteine
-
enhances activity
dexamethasone
-
rapid and marked increase in activity
epicatechin
-
0.03 mM completely prevents inactivation of glutamine synthetase by peroxynitrite
ethylene glycol
-
4-8%, 50% activation
GlnK
-
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%
-
glutamate
-
in the presence of Mg2+ the activity increases with the concentration of the substrate
glycinebetaine
-
0.4 M, 67.7% residual activity after 60C heat treatment
L-glutamate
-
causes conformational changes similar to those produced by Cl-binding
myo-Inositol
-
0.4 M, 70.1% residual activity after 60C heat treatment
myo-Inositol
-
0.4 M protects enzymatic activity during heat treatment
NaCl
-
0.25 mM increases GS activity in growing tubers
NaCl
-
increases activity at 100 mM
NH4+
-
in the presence of Mg2+ the activity increases with the concentration of the substrate
pinitol
-
0.4 M, 74.2% residual activity after 60C heat treatment
pinitol
-
0.4 M results in maintenance of activity to 90% and 50% during heat treatment
proline
-
0.4 M, 72.2% residual activity after 60C heat treatment
quercitol
-
0.4 M, 75.5% residual activity after 60C heat treatment
resveratrol
-
activity is increased by resveratrol at concentrations of 0.01 and 0.1 mM, 0.25 mM resveratrol does not affect activity
Sorbitol
-
0.4 M, 62.0% residual activity after 60C heat treatment
trijodothyronine
-
only when cultures are simultaneously treated with growth hormone and dexamethasone
MK801
-
N-methyl-D-aspartate-type glutamate receptor antagonist, activates the enzyme and inhibits osteogenic differentiation of the rat bone marrow stem cells
additional information
-
enzyme interacts with double-stranded DNA
-
additional information
-
glucose shows little tendency to protect the enzyme from loss of activity
-
additional information
-
activity is not affected by ethanol
-
additional information
-
glucocorticoids induce the enzyme transcription and translation in osteoblasts; 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
-
additional information
-
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
-
additional information
-
the level of glnA1 transcription is upregulated under nitrogen limitation conditions
-
additional information
P15106
the level of glnA1 transcription is upregulated under nitrogen limitation conditions. GlnR is able to function as both an activator and repressor of transcription
-
additional information
-
the enzyme is not affected by dietary glutamine supplementation or by Mycobacterium bovis bacillus Calmette-Guerin infection, overview
-
additional information
P81107, -
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
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
175
-
3-aminopentanedioate
-
pH 7.0, 37C
0.0000597
-
ADP
-
gamma-glutamyl transferase assay
0.01
-
ADP
-
transferase activity
0.09
-
ADP
Q4ZH57, -
pH 6.4, 37C, wild-type enzyme
0.15
-
ADP
Q9HH09, -
80C
0.833
-
ADP
-
-
0.05
-
ATP
Q9RHZ1, -
D51A mutant, pH 7.0, 30C
0.07
-
ATP
Q9RHZ1, -
D51S mutant, pH 7.0, 30C
0.1
-
ATP
-
enzyme from strain SA0, pH 6.8
0.12
-
ATP
Q9RHZ1, -
D51N mutant, pH 7.0, 30C
0.13
-
ATP
-
enzyme from strain SA0, pH 7.5
0.17
-
ATP
Q86ZU6, -
37C, pH 7.5
0.17
-
ATP
-
enzyme from strain SA1, pH 6.8
0.2
-
ATP
-
wild-type enzyme
0.2
-
ATP
-
in the presence of Mg2+
0.21
-
ATP
-
enzyme from strain SA1, pH 7.5
0.21
-
ATP
Q9RHZ1, -
wild type enzyme, pH 7.0, 30C
0.22
-
ATP
-
biosynthetic assay
0.25
-
ATP
-
oxidized mutant enzyme E165C
0.26
-
ATP
-
reduced mutant enzyme E165C
0.3
-
ATP
-
isoform GSI
0.3
-
ATP
-
wild type enzyme, pH 7.5, 37C
0.3
-
ATP
-
wild-type and mutant enzyme, pH 7.5, 37C
0.3
-
ATP
-, Q56WN1, Q9FMD9
pH 7.8, 30C, isoenzyme GLN1,1
0.43
-
ATP
-
enzyme form GSIII
0.45
-
ATP
P14654, P14656
30C, isoenzyme OsGLN1,1
0.53
-
ATP
-
biosynthetic assay, Mg2+-activated, enzyme form EII
0.53
-
ATP
P14654, P14656
30C, isoenzyme OsGLN1,2
0.56
-
ATP
-, Q56WN1, Q9FMD9
pH 7.8, 30C, isoenzyme GLN1,4
0.79
-
ATP
-
pH 7.4, 35C
0.85
-
ATP
-, Q56WN1, Q9FMD9
pH 7.8, 30C, isoenzyme GLN1,3
1
-
ATP
-
D56E mutant enzyme, pH 7.5, 37C
1.1
-
ATP
-, Q56WN1, Q9FMD9
pH 7.8, 30C, isoenzyme GLN1,2
1.2
-
ATP
-
mutant E304H, 25C, pH not specified in the publication
1.3
-
ATP
-
short isoform, pH 7.2, 37C
1.3
-
ATP
-
pH 11.0, 30 mM Mg2+
1.4
-
ATP
-
pH 8.0, 3 mM Mn2+; pH 8.5, 30 mM Mg2+
1.5
-
ATP
-
Mg2+-stimulated
1.5
-
ATP
-
ATP, biosynthetic assay, Mn2+-activated, enzyme form EII
1.5
-
ATP
-
pH 7.5, 3 mM MN2+; pH 8.5, 3 mM Mn2+
1.6
-
ATP
-
D56A mutant enzyme, pH 7.5, 37C
1.7
-
ATP
-
Mg2+-stimulated
1.8
-
ATP
-
synthetase assay
1.9
-
ATP
-
long isoform, pH 7.2, 37C
2
-
ATP
-
Mg2+-stimulated or Mn2+-stimulated
2
-
ATP
-
pH 8.0, 30 mM Mg2+
2.3
-
ATP
-
Mn2+-stimulated
2.3
-
ATP
-
ATP, Mg2+-stimulated
2.4
-
ATP
-
wild-type enzyme
2.4
-
ATP
-
wild-type, 25C, pH not specified in the publication
2.5
-
ATP
-
Mn2+-stimulated
2.5
-
ATP
-
arsenate
2.5
-
ATP
-
L-Glu, Mg2+-stimulated
2.5
-
ATP
-
mutant enzyme S186F
2.9
-
ATP
-
biosynthetic assay, Mg2+-activated, enzyme form EI
2.9
-
ATP
-
phosphorylated GS1a, in the presence of 0.0005 mM microcystin
3
-
ATP
-
chloroplast enzyme
3
-
ATP
-
non-phosphorylated GS1a, in the presence of 0.0005 mM microcystin
4.5
-
ATP
Q4ZH57, -
pH 6.4, 37C, wild-type enzyme
5.3
-
ATP
-
mutant G302A, 25C, pH not specified in the publication
6
-
ATP
A0MZ70
pH 7.8
6.45
-
ATP
Q4ZH57, -
pH 6.4, 37C, mutant enzyme E380A
9.4
-
ATP
-
mutant Y303H, 25C, pH not specified in the publication
10.6
-
ATP
Q9RHZ1, -
D51E mutant, pH 7.0, 30C
11
-
ATP
-
mutant E304D, 25C, pH not specified in the publication
14.3
-
ATP
-
-
28
-
ATP
O08467, -
60C, pH 7.8
500
-
ethylamine
-
pH 8.5, 3 mM Mn2+
700
-
ethylamine
-
pH 11.0, 30 mM Mg2+
11.6
-
Gln
-
glutamyl transferase reaction
37.6
-
Gln
-
transferase assay
48.6
-
Gln
-
gamma-glutamyl transferase assay
0.9
-
Glu
-
enzyme form GSIII
3
-
Glu
-
ATP, biosynthetic assay, Mn2+-activated, enzyme form EI
6.3
-
Glu
-
biosynthetic assay
6.7
-
Glu
-
synthetase assay
8.58
-
Glu
-
biosynthetic assay
13.3
-
Glu
-
enzyme form GSIII
14
-
Glu
-
hydroxylamine, glutamyl transferase assay
1.4
-
glutamate
-
enzyme from strain SA0, pH 6.8
1.7
-
glutamate
-
enzyme from strain SA0, pH 7.5
5.71
-
glutamate
-
pH 7.4, 35C
9.2
-
glutamate
-
enzyme from strain SA1, pH 6.8
16.8
-
glutamate
-
enzyme from strain SA1, pH 7.5
0.35
-
hydroxylamine
-
Mn2+-activated, enzyme form EII
0.4
-
hydroxylamine
-
Mn2+-activated, enzyme form EI
0.68
-
hydroxylamine
-
mutant E304H, 25C, pH not specified in the publication
0.74
-
hydroxylamine
-
mutant E304D, 25C, pH not specified in the publication
0.83
-
hydroxylamine
-
wild-type, 25C, pH not specified in the publication
1.46
-
hydroxylamine
-
-
1.5
-
hydroxylamine
Q4ZH57, -
pH 6.4, 37C, mutant enzyme E380A
2.4
-
hydroxylamine
-
-
2.6
-
hydroxylamine
-
glutamyltransferase reaction
2.9
-
hydroxylamine
-
wild-type enzyme
3.3
-
hydroxylamine
-
-
3.37
-
hydroxylamine
-
gamma-glutamyl transferase assay
3.4
-
hydroxylamine
-
mutant enzyme S186F
4.1
-
hydroxylamine
-
transferase reaction
4.7
-
hydroxylamine
Q4ZH57, -
pH 6.4, 37C, wild-type enzyme
5.3
-
hydroxylamine
-
enzyme form GSIII
6
-
hydroxylamine
-
transferase activity
8.3
-
hydroxylamine
-
pH 7.0
10.5
-
hydroxylamine
-
at 45C
62.5
-
hydroxylamine
-
-
11.1
-
L-Gln
-
glutamyl transferase reaction
12
-
L-Gln
-
transferase activity
12.6
-
L-Gln
-
biosynthetic reaction
22.2
-
L-Gln
-
transferase reaction
25
-
L-Gln
-
at 45C
0.0025
-
L-Glu
-
in the presence of Mg2+
0.67
-
L-Glu
-
isoenzyme GLN1,4
0.83
-
L-Glu
-
mutant A174S of isoenzyme GLN1,4
1.1
-
L-Glu
-
Mg2+-stimulated
1.14
-
L-Glu
-
mutant K49Q of isoenzyme GLN1,4
1.3
-
L-Glu
-
Mn2+-stimulated
1.43
-
L-Glu
-
mutant K49Q/A174S of isoenzyme GLN1,4
1.8
-
L-Glu
-
phosphorylated GS1a, in the presence of 0.0005 mM microcystin
2.1
-
L-Glu
-
Mn2+-stimulated
2.1
-
L-Glu
-
Gln, transferase reaction
2.1
-
L-Glu
P14654, P14656
30C, isoenzyme OsGLN1,2
2.4
-
L-Glu
-
mutant K49Q/A174S of isoenzyme GLN1,3
2.8
-
L-Glu
-
non-phosphorylated GS1a, in the presence of 0.0005 mM microcystin
3.2
-
L-Glu
-
mutant A174S of isoenzyme GLN1,3; mutant K49Q of isoenzyme GLN1,3
3.3
-
L-Glu
-
wild-type enzyme
3.4
-
L-Glu
-
synthetase reaction
4.17
-
L-Glu
-
isoenzyme GLN1,3
4.9
-
L-Glu
-
at 45C
6
-
L-Glu
-
oxidized mutant enzyme E165C
7
-
L-Glu
-
reduced mutant enzyme E165C
17
-
L-Glu
-
biosynthetic assay, Mg2+-activated, enzyme form I or Mn2+-activated, enzyme form EII.
18
-
L-Glu
-
Mg2+-stimulated
18
-
L-Glu
-
L-Glu, biosynthetic assay, Mg2+-activated, enzyme form EII
21
-
L-Glu
-
Mg2+-stimulated
25
-
L-Glu
-
Mg2+-stimulated
0.32
-
L-glutamate
Q9RHZ1, -
D51A mutant, pH 7.0, 30C
0.37
-
L-glutamate
Q9RHZ1, -
D51S mutant, pH 7.0, 30C
0.6
-
L-glutamate
-, Q56WN1, Q9FMD9
pH 7.8, 30C, isoenzyme GLN1,4
0.85
-
L-glutamate
Q9RHZ1, -
D51N mutant, pH 7.0, 30C
1.1
-
L-glutamate
-
short isoform, pH 7.2, 37C
1.1
-
L-glutamate
-, Q56WN1, Q9FMD9
pH 7.8, 30C, isoenzyme GLN1,1
1.3
-
L-glutamate
-
long isoform, pH 7.2, 37C
1.5
-
L-glutamate
Q9RHZ1, -
wild type enzyme, pH 7.0, 30C
1.9
-
L-glutamate
P14654, P14656
30C, isoenzyme OsGLN1,1
2
-
L-glutamate
-
mutant enzyme, pH 7.5, 37C
3.4
-
L-glutamate
-
mutant E304H, 25C, pH not specified in the publication
3.8
-
L-glutamate
-, Q56WN1, Q9FMD9
pH 7.8, 30C, isoenzyme GLN1,2
3.9
-
L-glutamate
-, Q56WN1, Q9FMD9
pH 7.8, 30C, isoenzyme GLN1,3
7
-
L-glutamate
-
wild type enzyme, pH 7.5, 37C
7
-
L-glutamate
-
wild-type enzyme, pH 7.5, 37C
9
-
L-glutamate
A0MZ70
pH 7.8
10
-
L-glutamate
-
mutant E304D, 25C, pH not specified in the publication
16
-
L-glutamate
Q9RHZ1, -
D51E mutant, pH 7.0, 30C
18
-
L-glutamate
-
D56E mutant enzyme, pH 7.5, 37C
22
-
L-glutamate
-
chloroplast enzyme
23.5
-
L-glutamate
O08467, -
60C, pH 7.8
27
-
L-glutamate
-
wild-type enzyme
27
-
L-glutamate
-
wild-type, 25C, pH not specified in the publication
29
-
L-glutamate
-
mutant enzyme S186F
38
-
L-glutamate
-
D56A mutant enzyme, pH 7.5, 37C
58
-
L-glutamate
-, Q60182
pH 7.0, 60C
59
-
L-glutamate
-
mutant Y303H, 25C, pH not specified in the publication
84
-
L-glutamate
-
mutant G302A, 25C, pH not specified in the publication
104
-
L-glutamate
-
pH 7.0, 37C
1.3
-
L-glutamine
Q9HH09, -
80C
6.8
-
L-glutamine
Q4ZH57, -
pH 6.4, 37C, wild-type enzyme
13
-
L-glutamine
-
wild-type enzyme
14
-
L-glutamine
-
mutant enzyme S186F
20
-
Methylamine
-
pH 8.0, 3 mM Mn2+
100
-
Methylamine
-
pH 8.5, 30 mM Mg2+
0.18
-
NH3
-
wild-type, 25C, pH not specified in the publication
32
-
NH3
-
mutant E304H, 25C, pH not specified in the publication
120
-
NH3
-
mutant E304D, 25C, pH not specified in the publication
0.004
-
NH4+
-
enzyme from strain SA0, pH 6.8
0.01
-
NH4+
-, Q56WN1, Q9FMD9
pH 7.8, 30C, below, isoenzyme GLN1,1
0.0125
-
NH4+
-
biosynthetic assay
0.013
-
NH4+
-
D56E mutant enzyme, pH 7.5, 37C
0.015
-
NH4+
-
enzyme from strain SA0, pH 7.5
0.02
0.05
NH4+
-
isoforms GSI and GSII
0.02
-
NH4+
-
D56A mutant enzyme, pH 7.5, 37C
0.025
-
NH4+
-
wild type enzyme, pH 7.5, 37C
0.027
-
NH4+
P14654, P14656
30C, isoenzyme OsGLN1,1
0.028
-
NH4+
-
pH 7.4, 35C
0.04
-
NH4+
-
-
0.042
-
NH4+
-
in the presence of Mg2+
0.05
-
NH4+
Q9RHZ1, -
wild type enzyme, pH 7.0, 30C
0.073
-
NH4+
P14654, P14656
30C, isoenzyme OsGLN1,2
0.119
-
NH4+
-
mutant A174S of isoenzyme GLN1,4
0.12
-
NH4+
-
isoenzyme GLN1,4
0.18
-
NH4+
-
Mg2+-stimulated
0.19
-
NH4+
-
enzyme form GSIII
0.2
-
NH4+
-
biosynthetic assay
0.2
-
NH4+
-
NH4+, biosynthetic assay, Mg2+-activated, enzyme form EII
0.2
-
NH4+
-
NH4+
0.334
-
NH4+
-
mutant A174S of isoenzyme GLN1,3
0.4
-
NH4+
-
chloroplast enzyme
0.45
-
NH4+
-
mutant K49Q of isoenzyme GLN1,3
0.453
-
NH4+
-
mutant K49Q of isoenzyme GLN1,4
0.456
-
NH4+
-
mutant K49Q/A174S of isoenzyme GLN1,3
0.48
-
NH4+
-
biosynthetic assay, Mn2+-stimulated, enzyme form EI
0.55
-
NH4+
Q9RHZ1, -
D51E mutant, pH 7.0, 30C
0.56
-
NH4+
-
Mg2+-stimulated
0.56
-
NH4+
-
hydroxylamine, Mg2+-activated, enzyme form EII
0.56
-
NH4+
-
pH 8.0, 30 mM Mg2+
0.58
-
NH4+
-, Q56WN1, Q9FMD9
pH 7.8, 30C, below, isoenzyme GLN1,4
0.59
-
NH4+
-
Mg2+-stimulated
0.59
-
NH4+
-
pH 7.5, 3 mM MN2+
0.69
-
NH4+
-
Mn2+-stimulated
0.69
-
NH4+
-
NH4+, Mg2+-stimulated
0.71
-
NH4+
-
Mn2+-stimulated
0.736
-
NH4+
-
mutant K49Q/A174S of isoenzyme GLN1,4
0.75
-
NH4+
Q86ZU6, -
37C, pH 7.5
0.77
-
NH4+
-
Mn2+-stimulated
0.92
-
NH4+
Q9RHZ1, -
D51N mutant, pH 7.0, 30C
1.21
-
NH4+
-, Q56WN1, Q9FMD9
pH 7.8, 30C, below, isoenzyme GLN1,3
1.33
-
NH4+
-
isoenzyme GLN1,3
1.4
-
NH4+
-
enzyme from strain SA1, pH 7.5
2.45
-
NH4+
-, Q56WN1, Q9FMD9
pH 7.8, 30C, below, isoenzyme GLN1,2
5.2
-
NH4+
A0MZ70
pH 7.8
5.95
-
NH4+
Q9RHZ1, -
D51S mutant, pH 7.0, 30C
12.4
-
NH4+
-
enzyme from strain SA1, pH 6.8
12.45
-
NH4+
Q9RHZ1, -
D51A mutant, pH 7.0, 30C
33
-
NH4+
-
enzyme form GSIII
2.8
-
NH4Cl
-
second value 8.9 mM, biphasic plot
21.6
-
glutamate
-
pH 7.5
additional information
-
hydroxylamine
O08467, -
the Km value of GlnA for hydroxylamine is higher when a high concentration was used (5 to 30mM), 60C, pH 7.8
0.24
-
Mn2+
Q9HH09, -
80C
additional information
-
additional information
-
enzyme activity is controlled by adenylylation
-
additional information
-
additional information
-
the enzyme is modulated by a closed bicyclic covalent interconvertible cascade. It consists of two protein nucleotidylation cycles. One involves the cyclic adenylylation and deadenylylation of glutamine synthetase, the other involves the uridylylation and deuridylylation of Shapiros regulatory protein PII
-
additional information
-
additional information
-
-
-
additional information
-
additional information
-
enzyme activity is controlled by adenylylation
-
additional information
-
additional information
-
Km-values of wild-type and mutant enzymes D50A, D50E, E327A
-
additional information
-
additional information
-
ADP-ribosylation of glutamine synthetase could be an alternative modification to adenylylation to regulate glutamine synthetase activity
-
additional information
-
additional information
-
Km for Gln and Glu increases after adenylylation
-
additional information
-
additional information
-
the site of ADP-ribosylation is Arg172
-
additional information
-
additional information
-
-
-
additional information
-
additional information
-
-
-
additional information
-
additional information
-
-
-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
3
6
ATP
-
wild-type enzyme
11.6
-
ATP
A0MZ70
pH 7.8
25
-
ATP
-
oxidized mutant enzyme E165C
35
-
ATP
-
reduced mutant enzyme E165C
52.7
-
ATP
O08467, -
60C, pH 7.8
12.83
-
hydroxylamine
O08467, -
60C, pH 7.8
2.29
-
L-Glu
-
mutant A174S of isoenzyme GLN1,4
2.97
-
L-Glu
-
mutant K49Q/A174S of isoenzyme GLN1,4
4.18
-
L-Glu
-
isoenzyme GLN1,4
4.96
-
L-Glu
-
mutant K49Q of isoenzyme GLN1,4
6.59
-
L-Glu
-
mutant K49Q of isoenzyme GLN1,3
7.02
-
L-Glu
-
isoenzyme GLN1,3
7.97
-
L-Glu
-
mutant A174S of isoenzyme GLN1,3
8.08
-
L-Glu
-
mutant K49Q/A174S of isoenzyme GLN1,3
27
-
L-Glu
-
oxidized mutant enzyme E165C
40
-
L-Glu
-
reduced mutant enzyme E165C
0.33
-
L-glutamate
Q9RHZ1, -
D51E mutant, pH 7.0, 30C
2.6
-
L-glutamate
Q9RHZ1, -
D51A mutant, pH 7.0, 30C
13.1
-
L-glutamate
Q9RHZ1, -
D51S mutant, pH 7.0, 30C
15.2
-
L-glutamate
A0MZ70
pH 7.8
36.5
-
L-glutamate
O08467, -
60C, pH 7.8
2.16
-
NH4+
-
mutant A174S of isoenzyme GLN1,4
2.81
-
NH4+
-
mutant K49Q/A174S of isoenzyme GLN1,4
2.96
-
NH4+
-
isoenzyme GLN1,4
5.33
-
NH4+
-
mutant K49Q of isoenzyme GLN1,4
6.19
-
NH4+
-
mutant A174S of isoenzyme GLN1,3
6.83
-
NH4+
-
mutant K49Q/A174S of isoenzyme GLN1,3
7.1
-
NH4+
-
isoenzyme GLN1,3
7.23
-
NH4+
-
mutant K49Q of isoenzyme GLN1,3
13.5
-
NH4+
A0MZ70
pH 7.8
42
-
L-glutamate
Q9RHZ1, -
wild type enzyme, pH 7.0, 30C
additional information
-
additional information
-
turnover number 4200, biosynthetic activity. 102000, transferase activity
-
kcat/KM VALUE [1/mMs-1]
kcat/KM VALUE [1/mMs-1] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
1.9
-
ATP
A0MZ70
pH 7.8
22040
1.6
-
L-glutamate
O08467, -
60C, pH 7.8
12211
1.69
-
L-glutamate
A0MZ70
pH 7.8
12211
2.6
-
NH4+
A0MZ70
pH 7.8
14473
1.9
-
ATP
O08467, -
60C, pH 7.8
22040
additional information
-
hydroxylamine
O08467, -
the Km value of GlnA for hydroxylamine is higher when a high concentration was used (5 to 30mM), 60C, pH 7.8
11532
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
5.5
-
(1,4-diamino-4-oxobutyl)phosphonic acid
P09606
-
2.1
-
(1-amino-4-methoxy-4-oxobutyl)phosphonic acid
P09606
-
0.00031
-
(1R,3R)-1-amino-3-(hydroxy(methyl)phosphoryl)cyclohexanecarboxylic acid
-
-
0.02
-
(1R,3R)-1-amino-3-(hydroxy(methyl)phosphoryl)cyclohexanecarboxylic acid
Sorghum sp.
-
-
0.024
-
(1R,3R)-1-amino-3-(hydroxy(methyl)phosphoryl)cyclohexanecarboxylic acid
-
-
0.072
-
(1R,3R)-1-amino-3-(hydroxy(methyl)phosphoryl)cyclohexanecarboxylic acid
-
-
0.125
-
(1R,3R)-1-amino-3-(hydroxy(methyl)phosphoryl)cyclohexanecarboxylic acid
-
-
0.00000047
-
(1R,3R)-1-amino-3-(hydroxy(methyl)phosphoryl)cyclopentanecarboxylic acid
-
-
1.2
-
(2R,3S)-3-aminooxetane-2-carboxylic acid
-
-
3.4
-
(2R,3S)-3-aminooxetane-2-carboxylic acid
-
plastidic isozyme
0.007
-
(2S)-2-amino-4-(hydroxyamino)butanoic acid
-
-
0.021
-
(2S)-2-amino-4-(hydroxyamino)butanoic acid
-
-
0.0037
-
(2S)-2-amino-4-[(1-aminoethyl)(hydroxy)phosphoryl]butanoic acid
-
-
0.0176
-
(2S)-2-amino-4-[(1-aminoethyl)(hydroxy)phosphoryl]butanoic acid
-
-
0.0216
-
(2S)-2-amino-4-[(1-aminoethyl)(hydroxy)phosphoryl]butanoic acid
-
-
0.133
-
(2S)-2-amino-4-[(2-aminoethyl)(hydroxy)phosphoryl]butanoic acid
-
-
0.32
-
(2S)-2-amino-4-[(2-aminoethyl)(hydroxy)phosphoryl]butanoic acid
-
-
1
-
(2S)-2-amino-4-[(3S)-3-hydroxy-2-oxoazetidin-3-yl]butanoic acid
-
-
0.00059
-
(2S)-2-amino-4-[(aminomethyl)(hydroxy)phosphoryl]butanoic acid
-
-
0.0018
-
(2S)-2-amino-4-[(aminomethyl)(hydroxy)phosphoryl]butanoic acid
-
-
0.0079
-
(2S)-2-amino-4-[(aminomethyl)(hydroxy)phosphoryl]butanoic acid
-
-
0.0021
-
(2S)-2-amino-4-[hydroxy(hydroxymethyl)phosphoryl]butanoic acid
-
-
0.0085
-
(2S)-2-amino-4-[hydroxy(hydroxymethyl)phosphoryl]butanoic acid
-
-
0.0458
-
(2S)-2-amino-4-[hydroxy(hydroxymethyl)phosphoryl]butanoic acid
-
-
1.3
-
(2S)-2-amino-4-[hydroxy(nitroso)amino]butanoic acid
P15105
-
4
-
(2S)-2-amino-4-[hydroxy(nitroso)amino]butanoic acid
P15105
-
6.2
-
(3,4-diamino-4-oxobutyl)methylphosphinic acid
P09606
-
8.7
-
(3-amino-4-methoxy-4-oxobutyl)methylphosphinic acid
P09606
-
4.47
-
([[2-(4-hydroxyphenyl)ethyl]amino]methanediyl)bis(phosphonic acid)
-
-
0.022
-
2-amino-2-ethyl-4-[hydroxy(methyl)phosphoryl]butanoic acid
Sorghum sp.
-
-
0.032
-
2-amino-2-ethyl-4-[hydroxy(methyl)phosphoryl]butanoic acid
-
-
0.111
-
2-amino-2-ethyl-4-[hydroxy(methyl)phosphoryl]butanoic acid
-
-
1.42
-
2-amino-4-hydroxyglutaric acid
-
-
1.4
-
2-amino-4-[(phosphonomethyl)sulfonyl]butanoic acid
-
-
0.05
-
2-amino-4-[ethyl(hydroxy)phosphoryl]butanoic acid
-
-
0.075
-
2-amino-4-[hydroxy(phosphonomethyl)phosphoryl]butanoic acid
-
-
0.25
-
2-amino-4-[hydroxy(phosphonomethyl)phosphoryl]butanoic acid
-
-
0.75
-
2-amino-4-[hydroxy(phosphonomethyl)phosphoryl]butanoic acid
-
-
2.2
-
2-amino-4-[methyl(phosphonomethyl)phosphoryl]butanoic acid
-
-
0.334
-
2-[(diphosphonomethyl)amino]pyridine-3-carboxylic acid
-
-
0.000005
-
3-amino-5-[hydroxy(methyl)phosphoryl]tetrahydrofuran-3-carboxylic acid
-
-
1.8
-
3-[(diphosphonomethyl)amino]benzoic acid
-
-
0.31
-
3-[(phosphonoacetyl)amino]alanine
-
-
0.91
-
3-[(phosphonoacetyl)amino]alanine
-
-
1.3
-
4-amino-4-phosphonobutanoic acid
P09606
-
16
-
4-amino-4-phosphonopentanoic acid
P09606
-
0.79
-
4-amino-4-[hydroxy(methyl)phosphoryl]butanoic acid
P09606
-
9.5
-
4-amino-4-[hydroxy(methyl)phosphoryl]pentanoic acid
P09606
-
0.62
-
4-fluoroglutamic acid
-
-
0.0000008
-
4-phosphonohomoserine
-
-
0.0016
-
4-phosphonohomoserine
-
-
0.012
-
4-phosphonohomoserine
-
-
0.014
-
4-phosphonohomoserine
Sorghum sp.
-
-
0.047
-
4-phosphonohomoserine
-
-
6.3
-
4-phosphonoisovaline
P09606
-
0.025
-
4-phosphononorvaline
-
-
0.067
-
4-phosphononorvaline
Sorghum sp.
-
-
0.14
-
4-phosphononorvaline
-
-
0.347
-
4-phosphononorvaline
-
-
0.492
-
4-phosphononorvaline
-
-
0.0057
-
4-[hydroxy(methyl)phosphoryl]isovaline
-
-
0.016
-
4-[hydroxy(methyl)phosphoryl]isovaline
-
-
0.024
-
4-[hydroxy(methyl)phosphoryl]isovaline
Sorghum sp.
-
-
0.056
-
4-[hydroxy(methyl)phosphoryl]isovaline
P09606
-
0.125
-
4-[hydroxy(methyl)phosphoryl]isovaline
-
-
0.59
-
5-oxo-6-phosphononorleucine
-
-
0.66
-
5-oxo-6-phosphononorleucine
-
-
4.8
-
5-oxo-6-phosphononorleucine
-
-
0.49
-
5-oxolysine
-
-
0.85
-
5-oxolysine
-
-
0.2
-
ADP
A0MZ70
substrate NH4+, pH 7.8
0.47
-
ADP
A0MZ70
substrate ATP, pH 7.8
0.7
-
ADP
A0MZ70
substrate L-glutamate, pH 7.8
0.033
-
D,L-phosphinothricin
-
-
0.1
-
glycine
Q9HH09, -
80C
0.03
-
L-alanine
Q9HH09, -
80C
6.6
-
L-glutamine
A0MZ70
substrate L-glutamate, pH 7.8
7.4
-
L-glutamine
A0MZ70
substrate NH4+, pH 7.8
9.2
-
L-glutamine
A0MZ70
substrate ATP, pH 7.8
0.054
-
L-glutamyl gamma-phosphinic acid
-
-
3
-
L-glutamyl gamma-phosphinic acid
-
-
0.0002
-
L-methionine-DL-sulfoximine
Q9RHZ1, -
wild-type enzyme, biosynthetic reaction, pH 7.0, 30C
2.94
-
L-methionine-DL-sulfoximine
Q9RHZ1, -
D51E mutant enzyme, biosynthetic reaction, pH 7.0, 30C
0.067
-
L-methionine-S-sulfoximine
-
short isoform, pH 7.2, 37C
0.124
-
L-methionine-S-sulfoximine
-
long isoform, pH 7.2, 37C
0.051
-
methionine sulfone amine
-
-
5
-
methionine sulfoxide
-
above
0.002
-
methionine sulfoximine
-
-
0.1
-
methionine sulfoximine
-
-
0.161
-
methionine sulfoximine
-
-
0.21
-
methionine sulfoximine
-
-
0.033
-
O-acetyl-4-phosphonohomoserine
-
-
0.178
-
O-acetyl-4-phosphonohomoserine
Sorghum sp.
-
-
6.2
-
phosphate
A0MZ70
substrate ATP, pH 7.8
12.8
-
phosphate
A0MZ70
substrate NH4+, pH 7.8
17.3
-
phosphate
A0MZ70
substrate L-glutamate, pH 7.8
0.0003
-
Phosphinothricin
Q9RHZ1, -
wild-type enzyme, biosynthetic reaction, pH 7.0, 30C
0.0011
-
Phosphinothricin
-
-
0.002
-
Phosphinothricin
-
isozyme GS1
0.003
-
Phosphinothricin
-
-
0.0035
-
Phosphinothricin
-, P13564
isozyme GS1
0.004
-
Phosphinothricin
-
isozyme GS1
0.006
-
Phosphinothricin
-, P13564
isozyme GS2
0.0065
-
Phosphinothricin
-
isozyme GS2
0.008
-
Phosphinothricin
-
isozyme GS2
0.008
-
Phosphinothricin
Sorghum sp.
-
-
0.0085
-
Phosphinothricin
-
isozyme GS2
0.009
-
Phosphinothricin
-
isozyme GS2
0.0252
-
Phosphinothricin
-
-
0.073
-
Phosphinothricin
-
-
0.1
-
Phosphinothricin
Q9RHZ1, -
D51E mutant enzyme, biosynthetic reaction, pH 7.0, 30C
0.32
-
Phosphinothricin
P09606
-
1.1
-
[(cyclohexylamino)methanediyl]bis(phosphonic acid)
-
-
0.243
-
[(pyridin-2-ylamino)methanediyl]bis(phosphonic acid)
-
-
1.2
-
[1-amino-3-(S-methylsulfonimidoyl)propyl]phosphonic acid
-
-
0.033
-
[[(3,5-dichlorophenyl)amino]methanediyl]bis(phosphonic acid)
-
-
0.738
-
[[(3-nitrophenyl)amino]methanediyl]bis(phosphonic acid)
-
-
0.17
-
[[(4-methylphenyl)amino]methanediyl]bis(phosphonic acid)
-
-
0.069
-
[[(5-chloropyridin-2-yl)amino]methanediyl]bis(phosphonic acid)
-
-
0.064
-
[[(pyridin-2-ylmethyl)amino]methanediyl]bis(phosphonic acid)
-
-
IC50 VALUE [mM]
IC50 VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.033
-
(2S)-2-amino-4-(methylsulfonyl)butanoic acid
-
pH 7.5, 22C
0.056
0.058
(2S,5R)-2,6-diamino-5-hydroxyhexanoic acid
-
dependent on the solvent, pH 7.5, 22C
0.0025
-
1-[(3,4-dichlorophenyl)methyl]-3,7-dimethyl-8-morpholin-4-yl-purine-2,6-dione
-
-
0.01
-
2-(3-aminophenyl)-6-bromo-N-cyclopentylimidazo[1,2-a]pyridin-3-amine
-
-
0.026
-
2-amino-4-(hydroxyamino)butanoic acid
-
pH 7.5, 22C
0.00038
-
3-[6-bromo-3-(cyclopentylamino)imidazo[1,2-a]pyridin-2-yl]benzoic acid
-
-
0.0033
-
3-[6-bromo-3-(cyclopentylamino)imidazo[1,2-a]pyridin-2-yl]phenol
-
-
0.0088
-
5-[6-bromo-3-(cyclopentylamino)imidazo[1,2-a]pyridin-2-yl]-2-methoxyphenol
-
-
0.0048
-
5-[6-iodo-3-(cyclopentylamino)imidazo[1,2-a]pyridin-2-yl]-2-methoxyphenol
-
-
0.2
-
AMP
-
mutant P306A, 25C, pH not specified in the publication
0.5
-
AMP
-
wild-type, 25C, pH not specified in the publication
1
-
AMP
-
mutant Y303H, 25C, pH not specified in the publication
1.3
-
AMP
-
mutant Y303A, 25C, pH not specified in the publication
1.4
-
AMP
-
mutant V300A, 25C, pH not specified in the publication
1.5
-
AMP
-
mutant Y303L, 25C, pH not specified in the publication
1.7
-
AMP
-
mutant E304D, 25C, pH not specified in the publication; mutant G302A, 25C, pH not specified in the publication
2.1
-
AMP
-
mutant A305G, 25C, pH not specified in the publication
30
-
AMP
-
mutant E304A, 25C, pH not specified in the publication
31
-
glycine
-
wild-type, 25C, pH not specified in the publication
350
-
glycine
-
mutant A305G, 25C, pH not specified in the publication
1.5
-
L-glutamine
-
mutant P306A, 25C, pH not specified in the publication
2.4
-
L-glutamine
-
wild-type, 25C, pH not specified in the publication
4.1
-
L-glutamine
-
mutant Y303H, 25C, pH not specified in the publication
7
-
L-glutamine
-
mutant V300A, 25C, pH not specified in the publication
11
-
L-glutamine
-
mutant G302A, 25C, pH not specified in the publication
13
-
L-glutamine
-
mutant Y303A, 25C, pH not specified in the publication
19
-
L-glutamine
-
mutant Y303L, 25C, pH not specified in the publication
79
-
L-glutamine
-
mutant E304D, 25C, pH not specified in the publication
140
-
L-glutamine
-
mutant A305G, 25C, pH not specified in the publication; mutant E304A, 25C, pH not specified in the publication
3
-
L-methionine S-sulfoximine
-
IC50: 3 mM
0.081
-
L-methionine sulfoximine
-
pH 7.5, 22C
0.051
-
L-methionine-(S)-sulfoximine
-
pH 7.5, 22C
0.1
-
L-methionine-S-sulfoximine
-
mutant Y303H, 25C, pH not specified in the publication; mutant Y303L, 25C, pH not specified in the publication
0.12
-
L-methionine-S-sulfoximine
-
mutant V300A, 25C, pH not specified in the publication
0.13
-
L-methionine-S-sulfoximine
-
wild-type, 25C, pH not specified in the publication
0.25
-
L-methionine-S-sulfoximine
-
mutant P306A, 25C, pH not specified in the publication
0.28
-
L-methionine-S-sulfoximine
-
mutant G302A, 25C, pH not specified in the publication
0.61
-
L-methionine-S-sulfoximine
-
mutant Y303A, 25C, pH not specified in the publication
2.7
-
L-methionine-S-sulfoximine
-
mutant A305G, 25C, pH not specified in the publication
20
-
L-methionine-S-sulfoximine
-
mutant E304D, 25C, pH not specified in the publication
26
-
L-methionine-S-sulfoximine
-
mutant E304A, 25C, pH not specified in the publication
0.2
-
Ni2+
-
pH 6.2, 37C
0.0019
-
Phosphinothricin
-
pH 7.5, 22C
0.076
-
Phosphinothricin
-
pH 7.5, 22C
0.0132
-
[3-[6-bromo-3-(cyclopentylamino)imidazo[1,2-a]pyridin-2-yl]phenyl]methanol
-
-
0.0128
-
[[(2,3-dichlorophenyl)amino]methanediyl]bis(phosphonic acid)
P38561
-
0.0212
-
[[(2,4-dichlorophenyl)amino]methanediyl]bis(phosphonic acid)
P38561
-
0.015
-
[[(2,6-dichlorophenyl)amino]methanediyl]bis(phosphonic acid)
P38561
-
0.0076
-
[[(3,5-dichlorophenyl)amino]methanediyl]bis(phosphonic acid)
P38561
-
0.021
-
[[(4-chlorophenyl)amino]methanediyl]bis(phosphonic acid)
P38561
-
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0.0002
-
-
crude cell extract
0.0149
-
-
after 75fold purification
0.018
-
-
glutamine synthetase activity in MG-63 cells
0.022
-
-
glutamine synthetase activity in MG-63 cells in presence of MG-132
0.023
-
-
glutamine synthetase activity in MG-63 cells in presence of dexamethasone and MG-132
0.042
-
-
glutamine synthetase activity in MG-63 cells in presence of vitamin D
0.067
-
-
glutamine synthetase activity in MG-63 cells in presence of dexamethasone
1
-
-
-
1.5
-
-
wild type strain
1.53
-
Q0E5H8
in the presence of 3 mM NaCl
1.6
-
-
wild type and gltF1 deficient strain
1.6
-
-
wild-type enzyme
2.7
-
-
mutant enzyme S186F
4.4
-
-
biosynthetic assay
11
-
Q5LGP1
pH not specified in the publication, temperature not specified in the publication
12.1
-
-
purified enzyme from strain SA1
23
-
-
pH 6.5, 37C, presence of Mn2+
26.8
-
Q9HH09, -
80C, purified enzyme
33.5
-
-
chloroplastic isoform GS2
33.9
-
-
gamma-glutamylhydroxamate assay
35.1
-
-
cytoplasmic isoform GS1
41.6
-
-
gamma-glutamylhydroxamate assay
62
-
-
gamma-glutamylhydroxamate assay
73.2
-
-
gamma-glutamyl transferase assay
88.08
-
-
gamma-glutamyl transferase assay
99.6
-
-
gamma-glutamyl transferase assay
126.1
-
-
purified enzyme from strain SA0
152
-
-
gamma-glutamylhydroxamate assay
153
-
-
gamma-glutamyl transferase assay
221.3
-
-
gamma-glutamyl transferase assay