Literature summary extracted from
Zhao, W.; Yang, J.; Tian, Y.; Fu, X.; Zhu, B.; Xue, Y.; Gao, J.; Han, H.J.; Peng, R.; Yao, Q.H.
Expression, purification, and characterization of recombinant mangrove glutamine synthetase (2014), Mol. Biol. Rep., 41, 7575-7583 .
Cloned(Commentary)
EC Number |
Cloned (Comment) |
Organism |
---|
6.3.1.2 |
DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic tree, recombinant expression of His-tagged enzyme in Escherichia coli strain glnA mutant JW3841-1, the recombinant enzyme can complement the auxotrophic strain |
Avicennia marina |
Localization
EC Number |
Localization |
Comment |
Organism |
GeneOntology No. |
Textmining |
---|
6.3.1.2 |
cytosol |
- |
Avicennia marina |
5829 |
- |
Metals/Ions
EC Number |
Metals/Ions |
Comment |
Organism |
Structure |
---|
6.3.1.2 |
Al3+ |
results in 8.91tivity compared to Mg2+ |
Avicennia marina |
|
6.3.1.2 |
Ca2+ |
results in 43.9% activity compared to Mg2+ |
Avicennia marina |
|
6.3.1.2 |
Co2+ |
results in 109.1% activity compared to Mg2+ |
Avicennia marina |
|
6.3.1.2 |
Cu2+ |
results in 22.2% activity compared to Mg2+ |
Avicennia marina |
|
6.3.1.2 |
Fe2+ |
results in 22.3% activity compared to Mg2+ |
Avicennia marina |
|
6.3.1.2 |
Mg2+ |
required |
Avicennia marina |
|
6.3.1.2 |
Mn2+ |
results in 17.12% activity compared to Mg2+ |
Avicennia marina |
|
6.3.1.2 |
Ni2+ |
results in 8.92% activity compared to Mg2+ |
Avicennia marina |
|
6.3.1.2 |
Zn2+ |
results in 9.58% activity compared to Mg2+ |
Avicennia marina |
|
Natural Substrates/ Products (Substrates)
EC Number |
Natural Substrates |
Organism |
Comment (Nat. Sub.) |
Natural Products |
Comment (Nat. Pro.) |
Rev. |
Reac. |
---|
6.3.1.2 |
ATP + L-glutamate + NH3 |
Avicennia marina |
- |
ADP + phosphate + L-glutamine |
- |
r |
|
Organism
EC Number |
Organism |
UniProt |
Comment |
Textmining |
---|
6.3.1.2 |
Avicennia marina |
Q9AXD8 |
- |
- |
Purification (Commentary)
EC Number |
Purification (Comment) |
Organism |
---|
6.3.1.2 |
recombinant His-tagged enzyme from Escherichia coli strain glnA mutant JW3841-1 by nickel affinity chromatography and dialysis |
Avicennia marina |
Substrates and Products (Substrate)
EC Number |
Substrates |
Comment Substrates |
Organism |
Products |
Comment (Products) |
Rev. |
Reac. |
---|
6.3.1.2 |
ATP + L-glutamate + NH3 |
- |
Avicennia marina |
ADP + phosphate + L-glutamine |
- |
r |
|
Subunits
EC Number |
Subunits |
Comment |
Organism |
---|
6.3.1.2 |
? |
x * 39300, recombinant His-tagged enzyme, SDS-PAGE |
Avicennia marina |
Synonyms
EC Number |
Synonyms |
Comment |
Organism |
---|
6.3.1.2 |
AmGLN1 |
- |
Avicennia marina |
Temperature Optimum [°C]
EC Number |
Temperature Optimum [°C] |
Temperature Optimum Maximum [°C] |
Comment |
Organism |
---|
6.3.1.2 |
35 |
- |
assay at |
Avicennia marina |
Temperature Range [°C]
EC Number |
Temperature Minimum [°C] |
Temperature Maximum [°C] |
Comment |
Organism |
---|
6.3.1.2 |
30 |
42 |
activity range |
Avicennia marina |
Temperature Stability [°C]
EC Number |
Temperature Stability Minimum [°C] |
Temperature Stability Maximum [°C] |
Comment |
Organism |
---|
6.3.1.2 |
45 |
- |
purified recombinant enzyme, enzymatic activity of AmGLN1 is lost after 30 min of incubation at 45°C |
Avicennia marina |
pH Optimum
EC Number |
pH Optimum Minimum |
pH Optimum Maximum |
Comment |
Organism |
---|
6.3.1.2 |
6.5 |
- |
rcombinant enzyme |
Avicennia marina |
pH Stability
EC Number |
pH Stability |
pH Stability Maximum |
Comment |
Organism |
---|
6.3.1.2 |
additional information |
- |
the remarkable stability of the enzyme under alkaline pH might be an environmental adaptation of Avicennia marina that grows in a highly alkaline environment |
Avicennia marina |
6.3.1.2 |
4 |
10 |
the enzyme is fairly stable at pH 4.0-10.0, while he highest stability is observed at pH 7.0-9.0 |
Avicennia marina |
Cofactor
EC Number |
Cofactor |
Comment |
Organism |
Structure |
---|
6.3.1.2 |
ATP |
- |
Avicennia marina |
|
General Information
EC Number |
General Information |
Comment |
Organism |
---|
6.3.1.2 |
metabolism |
the glutamine synthetase/glutamate synthase cycle is considered as the major pathway for ammonium assimilation and regulation of nitrogen metabolism in higher plants |
Avicennia marina |
6.3.1.2 |
physiological function |
glutamine synthetase catalyzes the formation of glutamine from glutamate in the presence of NH4+, ATP, and metal cations. The reaction is the rate-limiting step in the control of N-assimilation and N-recycling during growth and development of plants |
Avicennia marina |