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Information on EC 6.3.1.2 - glutamine synthetase and Organism(s) Squalus acanthias and UniProt Accession P41320

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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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Squalus acanthias
UNIPROT: P41320
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The taxonomic range for the selected organisms is: Squalus acanthias
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
-
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+
?
show the reaction diagram
-
first step in urea synthesis
-
-
?
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 + L-Glu + NH4+
?
show the reaction diagram
-
first step in urea synthesis
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
-
Mg2+ in excess of that required for formation of MgATP2- is required for maximal activity
Mn2+
-
cannot effectively replace Mg2+
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Ca2+
-
inhibits in presence of Mg2+
Urea
-
physiological concentrations of urea inhibit, at least when ATP and/or glutamate are nonsaturating. Inhibition is partially reversed by trimethylamine-N-oxide
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ethylene glycol
-
4-8%, 50% activation
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.1 - 7.4
-
-
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5 - 8
-
half-maximal activity at pH 6.5 and 8.0
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
Uniprot
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
liver enzyme is targeted to mitochondria. Two different glutamine synthetase transcripts are generated by tissue-specific alternative splicing. The liver transcript contains an alternative exon that is not present in the neural one. This exon leads to acquisition of an upstream in-frame start codon and formation of a mitochondrial targeting signal
Manually annotated by BRENDA team
neural enzyme is retained in the cytoplasm. Two different glutamine synthetase transcripts are generated by tissue-specific alternative splicing. The liver transcript contains an alternative exon that is not present in the neural one
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
neural enzyme is retained in the cytoplasm. Two different glutamine synthetase transcripts are generated by tissue-specific alternative splicing. The liver transcript contains an alternative exon that is not present in the neural one
Manually annotated by BRENDA team
liver enzyme is targeted to mitochondria. Two different glutamine synthetase transcripts are generated by tissue-specific alternative splicing. The liver transcript contains an alternative exon that is not present in the neural one. This exon leads to acquisition of an upstream in-frame start codon and formation of a mitochondrial targeting signal
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
GLNA_SQUAC
403
0
45409
Swiss-Prot
Mitochondrion (Reliability: 3)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
200000
-
gel filtration, in presence of Mg2+, MgATP2-, and L-Glu the enzyme has a MW of 400000, reversible dissociation from the 400000 MW form to a species of MW 200000 in the absence of MgATP2- and L-Glu
400000
-
gel filtration, in presence of Mg2+, MgATP2-, and L-Glu, reversible dissociation to a species of MW 200000 in the absence of MgATP2- and L-Glu
46000
-
x * 46000, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
-
x * 46000, SDS-PAGE
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
stability is enhanced by the presence of ethylene glycol
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, 10 mM MgSO4, 4 mM ATP, 50 mM glutamate, 100 mM NaCl, 10% ethylene glycol, 20 mM Hepes buffer, pH 7.4, less than 5% loss of activity per week
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Shankar, R.A.; Anderson, P.M.
Purification and properties of glutamine synthetase from liver of Squalus acanthias
Arch. Biochem. Biophys.
239
248-259
1985
Squalus acanthias
Manually annotated by BRENDA team
Matthews, G.D.; Gould, R.M.; Vardimon, L.
A single glutamine synthetase gene produces tissue-specific subcellular localization by alternative splicing
FEBS Lett.
579
5527-5534
2005
Squalus acanthias (P41320), Squalus acanthias
Manually annotated by BRENDA team