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Information on EC 6.3.1.2 - glutamine synthetase and Organism(s) Synechocystis sp. and UniProt Accession P77961

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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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This record set is specific for:
Synechocystis sp.
UNIPROT: P77961
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The taxonomic range for the selected organisms is: Synechocystis sp.
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
Glutamine synthetase
-
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
-
-
-
-
glutamine synthetase I
-
-
Glutamylhydroxamic synthetase
-
-
-
-
GS
-
-
-
-
GS type I
-
-
GS(1)
-
-
-
-
GS1
-
-
-
-
GS107
-
-
-
-
GS112
-
-
-
-
GS117
-
-
-
-
GS122
-
-
-
-
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-glutamate + NH3
ADP + phosphate + L-glutamine
show the reaction diagram
ATP + L-Glu + NH4+
ADP + phosphate + L-Gln
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
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ADP
-
strong, enzyme form GSIII
L-methionine sulfoximine
-
enzyme form GS III
NH4+
-
reversible inactivation
Phosphinothricin
-
-
additional information
structure-activity relationships and inhibitor design, overview
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.43
ATP
-
enzyme form GSIII
0.9
Glu
-
enzyme form GSIII
0.19
NH4+
-
enzyme form GSIII
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.2
-
enzyme form GSI
8.3
-
enzyme form GSIII, biosynthetic assay
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
35
-
enzyme form GSI, biosynthetic assay
42
-
enzyme form GSIII, biosynthetic assay
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
500000
-
enzyme form GSIII, gel filtration
52000
-
12 * 52000, enzyme form GSI, SDS-PAGE
624000
-
enzyme form GSI, gel filtration
79416
-
x * 79416, calculation from nucleotide sequence
80000
-
6 * 80000, enzyme form GSIII, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
-
x * 79416, calculation from nucleotide sequence
dodecamer
-
12 * 52000, enzyme form GSI, SDS-PAGE
hexamer
-
6 * 80000, enzyme form GSIII, SDS-PAGE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
two genes encode glutamine synthetase, glnN and glnA. GlnN supports Synechocystis growth in a strain whose glnA gene is inactivated by insertional mutagenesis
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
50
-
20 min, complete inactivation
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
strongly stabilized in presence of Mn2+ but not with other divalent cations. Maximal stabilization at 1 mM
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
enzyme form GSIII
-
HPLC immunoaffinity chromatography
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
glnN gene overexpressed in Escherichia coli
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Alhama, J.; Lopez-Barea, J.; Toribio, F.; Roldan, J.M.
Purification and determination of glutamine synthetase by high-performance immunoaffinity chromatography
J. Chromatogr.
589
121-126
1992
Synechocystis sp.
Manually annotated by BRENDA team
Reyes, J.C.; Florencio, F.J.
A new type of glutamine synthetase in cyanobacteria: the protein encoded by the glnN gene supports nitrogen assimilation in Synechocystis sp. strain PCC 6803
J. Bacteriol.
176
1260-1267
1994
Synechocystis sp.
Manually annotated by BRENDA team
Garcia-Dominguez, M.; Reyes, J.C.; Florencio, F.J.
Purification and characterization of a new type of glutamine synthetase from cyanobacteria
Eur. J. Biochem.
244
258-264
1997
Synechocystis sp.
Manually annotated by BRENDA team
Galmozzi, C.V.; Fernandez-Avila, M.J.; Reyes, J.C.; Florencio, F.J.; Muro-Pastor, M.I.
The ammonium-inactivated cyanobacterial glutamine synthetase I is reactivated in vivo by a mechanism involving proteolytic removal of its inactivating factors
Mol. Microbiol.
65
166-179
2007
Synechocystis sp.
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