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Information on EC 6.3.1.2 - glutamine synthetase and Organism(s) Phaseolus vulgaris and UniProt Accession P04771

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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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Phaseolus vulgaris
UNIPROT: P04771
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The taxonomic range for the selected organisms is: Phaseolus vulgaris
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 type II
-
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
-
-
-
-
GS2
-
-
-
-
GSI
-
-
-
-
GSII
-
-
-
-
GSIII
-
-
-
-
Isozyme delta
-
-
-
-
L-Glutamine synthetase
-
-
-
-
N47/N48
-
-
-
-
S2205/S2287
-
-
-
-
Synthetase, glutamine
-
-
-
-
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
-
-
-
ir
ATP + glutamate + NH4+
ADP + phosphate + L-glutamine
show the reaction diagram
ATP + L-Glu + NH4+
ADP + phosphate + L-Gln
show the reaction diagram
-
-
-
-
?
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 + glutamate + NH4+
ADP + phosphate + L-glutamine
show the reaction diagram
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
methionine sulfoximine
-
2-mercaptoethanol
-
no inhibition of wild type enzyme, inhibits activity of D56A and D56E mutant enzymes
cysteine
-
no inhibition of wild type enzyme, inhibits activity of D56A and D56E mutant enzymes
dithioerythritol
-
no inhibition of wild type enzyme, inhibits activity of D56A and D56E mutant enzymes
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
p-hydroxymercuribenzoate
-
complete inhibition of wild type and D56A mutant, 40% inhibition of D56E at 1 mM
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.3 - 1.6
ATP
2 - 38
L-glutamate
0.013 - 0.025
NH4+
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
45
-
reverse reaction of mutant enzyme
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
GLNA2_PHAVU
356
0
39205
Swiss-Prot
other Location (Reliability: 3)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
344000
gel filtration
43000
8 * 43000, gel filtration
350000
-
gel filtration
43000
-
SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
octamer
octamer
-
8 * 43000, subunits by SDS-PAGE, native mass by gel filtration
tetramer
-
4 * 43000, minor peak in gel filtration with a mass of 190000 detected for both mutant enzymes
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D56A
-
complete loss of activity in reverse reaction, 83% of wild-type activity in forward reaction, salting out at much higher ammonium sulfate concentrations than wild type enzyme
D56E
-
complete loss of activity in reverse reaction, 65% of wild-type activity in forward reaction, salting out properties only slightly affected
E297A
-
Km for ammonium strongly increased, minor effects on activity in forward reaction, reverse reaction activity strongly decreased, strong effect on binding behavior to a 2',5'-ADP-sepharose
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Sephacryl S-300 HR gel filtration
recombinant enzymes
-
recombinant mutant and wild-type enzyme
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli strain SG13009
expressed in Escherichia coli ET8894
-
mutant and native enzymes expressed in Escherichia coli
-
three cDNA clones encoding the closely related glutamine synthetase alpha, beta and gamma polypeptides of Phaseolus vulgaris expressed in Escherichia coli
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Bennett, M.; Cullimore, J.
Expression of three plant glutamine synthetase cDNA in Escherichia coli. Formation of catalytically active isoenzymes, and complementation of a glnA mutant
Eur. J. Biochem.
193
319-324
1990
Phaseolus vulgaris
Manually annotated by BRENDA team
Clemente, M.T.; Marquez, A.J.
Functional importance of Asp56 from the alpha-polypeptide of Phaseolus vulgaris glutamine synthetase: An essential residue for transferase but not for biosynthetic enzyme activity
Eur. J. Biochem.
264
453-460
1999
Phaseolus vulgaris
Manually annotated by BRENDA team
Clemente, M.T.; Marquez, A.J.
Site-directed mutagenesis of Glu-297 from the alpha-polypeptide of Phaseolus vulgaris glutamine synthetase alters kinetic and structural properties and confers resistance to L-methionine sulfoximine
Plant Mol. Biol.
40
835-845
1999
Phaseolus vulgaris
Manually annotated by BRENDA team
Llorca, O.; Betti, M.; Gonzalez, J.M.; Valencia, A.; Marquez, A.J.; Valpuesta, J.M.
The three-dimensional structure of an eukaryotic glutamine synthetase: functional implications of its oligomeric structure
J. Struct. Biol.
156
469-479
2006
Phaseolus vulgaris (P04771), Phaseolus vulgaris
Manually annotated by BRENDA team