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Information on EC 6.3.1.2 - glutamine synthetase and Organism(s) Bacteroides fragilis and UniProt Accession P15623

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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:
Bacteroides fragilis
UNIPROT: P15623
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The taxonomic range for the selected organisms is: Bacteroides fragilis
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
L-glutamate:ammonia ligase (ADP-forming)
-
type III 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
-
-
-
-
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
-
-
-
?
ATP + L-Glu + NH4+
ADP + phosphate + L-Gln
show the reaction diagram
-
-
-
-
?
Gln + hydroxylamine + ADP
gamma-Glutamylhydroxamate + NH4+ + ?
show the reaction diagram
-
-
-
-
?
L-Gln + hydroxylamine + ADP
L-gamma-glutamylhydroxamate + NH4+ + ?
show the reaction diagram
-
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mn2+
-
MnCl2 stimulates gamma-glutamyl transferase activity of glutamine synthethase from unshocked cells, no effect on the gamma-glutamyl transferase activity of unshocked cells
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(NH4)2SO4
-
weak, gamma-glutamyl transferase activity
Ala
-
gamma-glutamyl transferase activity
Gly
-
gamma-glutamyl transferase activity
His
-
L-His, gamma-glutamyl transferase activity
L-Arg
-
gamma-glutamyl transferase activity
L-Glu
-
gamma-glutamyl transferase activity
L-Ile
-
weak, gamma-glutamyl transferase activity
L-methionine sulfoximine
-
gamma-glutamyl transferase assay
L-Pro
-
weak, gamma-glutamyl transferase activity
Mg2+
-
above 0.5 mM, gamma-glutamyl transferase activity
Snake venom diesterase
-
-
-
additional information
-
Bacillus fragilis enzyme produced in E. coli is specifically and irreversibly inactivated by Bacillus fragilis cell extract
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
11
pH not specified in the publication, temperature not specified in the publication
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5 - 7
-
gamma-glutamyl transferase assay
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
45
-
gamma-glutamyl transferase assay
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
86000
10 * 86000, cryo-electron microscopy
860000
gel filtration
490000
-
gel filtration
75000
-
6 * 75000, isoform GS2, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
decamer
10 * 86000, cryo-electron microscopy
dodecamer
-
crystallization data
hexamer
-
6 * 75000, isoform GS2, SDS-PAGE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Ta6Br12 derivative, to 3.5 A resolution, space group C2221. The divergence of the type III from the type I and II GS enzymes is mainly due to differences in quaternary structure despite all the enzymes sharing a remarkably conserved active site fold.. The two hexameric rings of the GSIII dodecamer associate on the opposite surface relative to types I and II
-
untagged, full-length recombinant protein, to 3.0 A resolution, space group P1
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Sephacryl 300 HR gel filtration
rapid and scalable two-step protocol for expression and purification of glutamine synthetase in an auxotrophic Escherichia coli strain utilizing differential precipitation by divalent cations followed by affinity chromatography to produce suitable quantities of homogenous material for structural characterization
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli
expression in Escherichia coli
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
synthesis
rapid and scalable two-step protocol for expression and purification of glutamine synthetase in an auxotrophic Escherichia coli strain utilizing differential precipitation by divalent cations followed by affinity chromatography to produce suitable quantities of homogenous material for structural characterization
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Southern, J.A.; Parker, J.R.; Woods, D.R.
Novel structure, properties, and inactivation of glutamine synthetase cloned from Bacteroides fragilis
J. Gen. Microbiol.
133
2437-2446
1987
Bacteroides fragilis
-
Manually annotated by BRENDA team
van Rooyen, J.M.; Abratt, V.R.; Sewell, B.T.
Three-dimensional structure of a type III glutamine synthetase by single-particle reconstruction
J. Mol. Biol.
361
796-810
2006
Bacteroides fragilis (P15623), Bacteroides fragilis
Manually annotated by BRENDA team
van Rooyen, J.; Belrhali, H.; Abratt, V.; Sewell, B.T.
Proteolysis of the type III glutamine synthetase from Bacteroides fragilis causes expedient crystal-packing rearrangements
Acta Crystallogr. Sect. F
67
358-363
2011
Bacteroides fragilis (Q5LGP1), Bacteroides fragilis
Manually annotated by BRENDA team
van Rooyen, J.M.; Abratt, V.R.; Belrhali, H.; Sewell, T.
Crystal structure of Type III glutamine synthetase: surprising reversal of the inter-ring interface
Structure
19
471-483
2011
Bacteroides fragilis
Manually annotated by BRENDA team