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Information on EC 6.3.1.2 - glutamine synthetase and Organism(s) Zea mays and UniProt Accession P38562

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IUBMB Comments
Glutamine synthetase, which catalyses the incorporation of ammonium into glutamate, is a key enzyme of nitrogen metabolism found in all domains of life. Several types have been described, differing in their oligomeric structures and cofactor requirements.
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Zea mays
UNIPROT: P38562
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The taxonomic range for the selected organisms is: Zea mays
The enzyme appears in selected viruses and cellular organisms
Synonyms
glutamine synthetase, gamma-glutamyl transferase, gs-ii, gsiii, taase, glna1, glna2, gln1;2, gln synthetase, gs(1), more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Chloroplast GS2
-
-
-
-
Clone lambda-GS28
-
-
-
-
Clone lambda-GS31
-
-
-
-
Clone lambda-GS8
-
-
-
-
Cytoplasmic GS3
-
-
-
-
Cytosolic GS1
-
-
-
-
Gln isozyme alpha
-
-
-
-
Gln isozyme beta
-
-
-
-
Gln isozyme gamma
-
-
-
-
Glutamate--ammonia ligase
-
-
-
-
glutamate-ammonia ligase
-
-
-
-
Glutamine synthetase
Glutamylhydroxamic synthetase
-
-
-
-
GS
-
-
-
-
GS(1)
-
-
-
-
GS1
-
-
-
-
GS107
-
-
-
-
GS112
-
-
-
-
GS117
-
-
-
-
GS122
-
-
-
-
GS1a
-
-
GS2
-
-
-
-
GSI
-
-
-
-
GSII
-
-
-
-
GSIII
-
-
-
-
Isozyme delta
-
-
-
-
L-Glutamine synthetase
-
-
-
-
N47/N48
-
-
-
-
S2205/S2287
-
-
-
-
Synthetase, glutamine
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
ATP + L-glutamate + NH3 = ADP + phosphate + L-glutamine
show the reaction diagram
reaction mechanism
-
SYSTEMATIC NAME
IUBMB Comments
L-glutamate:ammonia ligase (ADP-forming)
Glutamine synthetase, which catalyses the incorporation of ammonium into glutamate, is a key enzyme of nitrogen metabolism found in all domains of life. Several types have been described, differing in their oligomeric structures and cofactor requirements.
CAS REGISTRY NUMBER
COMMENTARY hide
9023-70-5
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
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-glutamate + NH3
ADP + phosphate + L-glutamine
show the reaction diagram
additional information
?
-
-
structure-activity relationship, overview
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mn2+
-
essential for activity, contains three Mn2+ ions per subunit
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
5-oxolysine
Phosphinothricin
-
isolated from Streptomyces viridochromogenes
[[(2,3-dichlorophenyl)amino]methanediyl]bis(phosphonic acid)
non-competitive mechanism against glutamate and uncompetitive mechanism against ATP
[[(2,4-dichlorophenyl)amino]methanediyl]bis(phosphonic acid)
non-competitive mechanism against glutamate and uncompetitive mechanism against ATP
[[(2,6-dichlorophenyl)amino]methanediyl]bis(phosphonic acid)
non-competitive mechanism against glutamate and uncompetitive mechanism against ATP
[[(3,5-dichlorophenyl)amino]methanediyl]bis(phosphonic acid)
non-competitive mechanism against glutamate and uncompetitive mechanism against ATP
[[(4-chlorophenyl)amino]methanediyl]bis(phosphonic acid)
non-competitive mechanism against glutamate and uncompetitive mechanism against ATP
additional information
-
structure-activity relationships and inhibitor design, overview
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
additional information
-
-
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.49 - 0.85
5-oxolysine
0.002 - 0.004
Phosphinothricin
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0128
[[(2,3-dichlorophenyl)amino]methanediyl]bis(phosphonic acid)
Zea mays
-
0.0212
[[(2,4-dichlorophenyl)amino]methanediyl]bis(phosphonic acid)
Zea mays
-
0.015
[[(2,6-dichlorophenyl)amino]methanediyl]bis(phosphonic acid)
Zea mays
-
0.0076
[[(3,5-dichlorophenyl)amino]methanediyl]bis(phosphonic acid)
Zea mays
-
0.021
[[(4-chlorophenyl)amino]methanediyl]bis(phosphonic acid)
Zea mays
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
-
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
isozyme GS2
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
-
the total capacity of the enzyme-mediated ligation of free ammonium and glutamate to form glutamine in the leaves of maize plants is not impaired upon severe magnesium starvation. The total GS-mediated primary or secondary assimilation of free NH4+ is not a limiting enzymatic reaction under Mg-deficiency and thus cannot be accountable for the observed restriction of plant growth and productivity in Mg-deficient maize, phenotype, overview
physiological function
-
glutamine synthetase is one of the key enzymes in nitrogen assimilation, ligating-free ammonium to glutamate to form glutamine and it is therefore crucial for plant growth and productivity
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
GLNA4_MAIZE
355
0
38981
Swiss-Prot
other Location (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40000
SDS-PAGE
44000
SDS-PAGE
300000 - 350000
-
gel filtration
40000
-
8 * 40000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
decamer
octamer
-
8 * 40000
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging drop vapour diffusion method, GS crystals in complex with ADP and methionine sulfoximine phosphate, using 9% (w/v) polyethylene glycol 8000, 100 mM Tris-HCl pH 7.8, 5% (v/v) 2-methyl-2,4-pentanediol, 10 mM MnCl2
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
gln1-3gln1-4 mutant
gln1-3mutant
gln1-4 mutant
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli JM109 cells
-
overexpression in Escherichia coli
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Sakakibara, H.; Shimizu, H.; Hase, T.; Yamazaki, Y.; Takao, T.; Shimonishi, Y.; Sugiyama, T.
Molecular identification and characterization of cytosolic isoforms of glutamine synthetase in maize roots
J. Biol. Chem.
271
29561-29568
1996
Zea mays
Manually annotated by BRENDA team
Unno, H.; Uchida, T.; Sugawara, H.; Kurisu, G.; Sugiyama, T.; Yamaya, T.; Sakakibara, H.; Hase, T.; Kusunoki, M.
Atomic structure of plant glutamine synthetase: a key enzyme for plant productivity
J. Biol. Chem.
281
29287-29296
2006
Zea mays
Manually annotated by BRENDA team
Martin, A.; Lee, J.; Kichey, T.; Gerentes, D.; Zivy, M.; Tatout, C.; Dubois, F.; Balliau, T.; Valot, B.; Davanture, M.; Terce-Laforgue, T.; Quillere, I.; Coque, M.; Gallais, A.; Gonzalez-Moro, M.B.; Bethencourt, L.; Habash, D.Z.; Lea, P.J.; Charcosset, A.; Perez, P.; Murigneux, A.; Sakakibara, H.; Ed, E.d.w.
Two cytosolic glutamine synthetase isoforms of maize are specifically involved in the control of grain production
Plant Cell
18
3252-3274
2006
Zea mays (P38562), Zea mays
Manually annotated by BRENDA team
Valadier, M.H.; Yoshida, A.; Grandjean, O.; Morin, H.; Kronenberger, J.; Boutet, S.; Raballand, A.; Hase, T.; Yoneyama, T.; Suzuki, A.
Implication of the glutamine synthetase/glutamate synthase pathway in conditioning the amino acid metabolism in bundle sheath and mesophyll cells of maize leaves
FEBS J.
275
3193-3206
2008
Zea mays, Zea mays (P25462)
Manually annotated by BRENDA team
Berlicki, L.
Inhibitors of glutamine synthetase and their potential application in medicine
Mini Rev. Med. Chem.
8
869-878
2008
Beta vulgaris, Bradyrhizobium japonicum, Chlorella sp., Columba sp., Escherichia coli, Ovis aries, Hordeum vulgare, Hordeum vulgare (P13564), Oryza sativa, Vigna radiata, Pisum sativum, Sorghum sp., Spinacia oleracea, Triticum aestivum, Zea mays, Senna obtusifolia, Rattus norvegicus (P09606), Salmonella enterica subsp. enterica serovar Typhimurium (P0A1P6), Bacillus subtilis (P12425), Homo sapiens (P15104), Mus musculus (P15105), Synechocystis sp. (P77961), Mycobacterium tuberculosis (P9WN39), Mycobacterium tuberculosis H37Rv (P9WN39)
Manually annotated by BRENDA team
Occhipinti, A.; Berlicki, L.; Giberti, S.; Dziedziola, G.; Kafarski, P.; Forlani, G.
Effectiveness and mode of action of phosphonate inhibitors of plant glutamine synthetase
Pest Manag. Sci.
66
51-58
2010
Zea mays (P38561), Zea mays
Manually annotated by BRENDA team
Jezek, M.; Geilfus, C.M.; Muehling, K.H.
Glutamine synthetase activity in leaves of Zea mays L. as influenced by magnesium status
Planta
242
1309-1319
2015
Zea mays
Manually annotated by BRENDA team