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Information on EC 6.3.1.2 - glutamine synthetase and Organism(s) Pseudomonas aeruginosa

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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:
Pseudomonas aeruginosa
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Word Map
The taxonomic range for the selected organisms is: Pseudomonas aeruginosa
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
-
-
-
-
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
-
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.4
-
fully adenylylated enzyme form
additional information
-
at pH 8.75 the transferase activity of glutamine synthetase is independent of the state of adenylylation, whereas at pH 7.4, the activity depends on the amount of enzyme present and the state of adenylylation
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
A0A8G3Z478_PSEAI
444
0
49253
TrEMBL
-
A0A069Q3A1_PSEAI
469
0
51945
TrEMBL
-
A0A8G7AED0_PSEAI
469
0
51919
TrEMBL
-
A0A8G3QPQ1_PSEAI
121
0
13690
TrEMBL
-
A0A6B1Y473_PSEAI
469
0
51961
TrEMBL
-
A0A367M9W0_PSEAI
204
0
22364
TrEMBL
-
A0A8G3IWH5_PSEAI
454
0
50596
TrEMBL
-
A0A3M5DAB8_PSEAI
100
0
11195
TrEMBL
-
A0A3S0IWW9_PSEAI
444
0
49205
TrEMBL
-
A0A3M5D954_PSEAI
342
0
37766
TrEMBL
-
A0A8G3T9K6_PSEAI
469
0
51944
TrEMBL
-
A0A367LSQ9_PSEAI
67
0
7280
TrEMBL
-
A0A1Y3L752_PSEAI
443
0
47871
TrEMBL
-
A0A8G4DRH0_PSEAI
469
0
51975
TrEMBL
-
A0A8G4D5V2_PSEAI
469
0
51959
TrEMBL
-
A0A367LTQ4_PSEAI
67
0
7183
TrEMBL
-
A0A2R3J0Z2_PSEAI
443
0
48142
TrEMBL
-
A0A8G4BA52_PSEAI
469
0
51917
TrEMBL
-
A0A367M9Z8_PSEAI
210
0
23582
TrEMBL
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
62000
-
x * 62000, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
-
x * 62000, SDS-PAGE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
adenylylation
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Janssen, D.B.; op den Camp, H.J.M.; Leenen, P.J.M.; van der Drift, C.
The enzymes of the ammonia assimilation in Pseudomonas aeruginosa
Arch. Microbiol.
124
197-203
1980
Pseudomonas aeruginosa
Manually annotated by BRENDA team
Meyer, J.M.; Stadtman, E.R.
Glutamine synthetase of pseudomonads: some biochemical and physicochemical properties
J. Bacteriol.
146
705-712
1981
Pseudomonas aeruginosa, Pseudomonas putida, Pseudomonas fluorescens
Manually annotated by BRENDA team