Any feedback?
Literature summary for 6.3.1.2 extracted from
- Expression, purification, and characterization of recombinant mangrove glutamine synthetase (2014), Mol. Biol. Rep., 41, 7575-7583 .
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| 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
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| cytosol | - |
Avicennia marina | 5829 | - |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Al3+ | results in 8.91tivity compared to Mg2+ | Avicennia marina |  |
| Ca2+ | results in 43.9% activity compared to Mg2+ | Avicennia marina | |
| Co2+ | results in 109.1% activity compared to Mg2+ | Avicennia marina | |
| Cu2+ | results in 22.2% activity compared to Mg2+ | Avicennia marina | |
| Fe2+ | results in 22.3% activity compared to Mg2+ | Avicennia marina | |
| Mg2+ | required | Avicennia marina | |
| Mn2+ | results in 17.12% activity compared to Mg2+ | Avicennia marina | |
| Ni2+ | results in 8.92% activity compared to Mg2+ | Avicennia marina | |
| Zn2+ | results in 9.58% activity compared to Mg2+ | Avicennia marina | |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ATP + L-glutamate + NH3 | Avicennia marina | - |
ADP + phosphate + L-glutamine | - |
r | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Avicennia marina | Q9AXD8 | - |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant His-tagged enzyme from Escherichia coli strain glnA mutant JW3841-1 by nickel affinity chromatography and dialysis | Avicennia marina |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ATP + L-glutamate + NH3 | - |
Avicennia marina | ADP + phosphate + L-glutamine | - |
r | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| ? | x * 39300, recombinant His-tagged enzyme, SDS-PAGE | Avicennia marina |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| AmGLN1 | - |
Avicennia marina |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 35 | - |
assay at | Avicennia marina |
Temperature Range [°C]
| Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 30 | 42 | activity range | Avicennia marina |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 45 | - |
purified recombinant enzyme, enzymatic activity of AmGLN1 is lost after 30 min of incubation at 45°C | Avicennia marina |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 6.5 | - |
rcombinant enzyme | Avicennia marina |
pH Stability
| pH Stability | pH Stability Maximum | Comment | Organism |
|---|---|---|---|
| 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 |
| 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
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| ATP | - |
Avicennia marina | |
General Information
| General Information | Comment | Organism |
|---|---|---|
| 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 |
| 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 |
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
