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Literature summary for 1.4.1.14 extracted from
- Enzymes of nitrogen metabolism in legume nodules. Purification and properties of NADH-dependent glutamate synthase from lupin nodules (1977), Eur. J. Biochem., 79, 355-362.
Activating Compound
| Activating Compound | Comment | Organism | Structure |
|---|---|---|---|
| 2-mercaptoethanol | 1%, presence of a reducing agent is essential for enzyme activity | Lupinus angustifolius |  |
| dithiothreitol | 0.5 mg per ml, presence of a reducing agent is essential for enzyme activity | Lupinus angustifolius | |
General Stability
| General Stability | Organism |
|---|---|
| phenylmethylsulphonyl fluoride is used as precaution against proteolysis | Lupinus angustifolius |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| asparagine | weak inhibition, competitive with 2-oxoglutarate | Lupinus angustifolius | |
| aspartate | weak inhibition, competitive with 2-oxoglutarate | Lupinus angustifolius | |
| L-glutamate | competitive with 2-oxoglutarate | Lupinus angustifolius | |
| NAD+ | competitive with NADH | Lupinus angustifolius | |
| oxaloacetate | weak inhibition, competitive with 2-oxoglutarate | Lupinus angustifolius | |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.0013 | - |
NADH | - |
Lupinus angustifolius | |
| 0.039 | - |
2-oxoglutarate | - |
Lupinus angustifolius | |
| 0.4 | - |
L-glutamine | - |
Lupinus angustifolius | |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| cytoplasm | - |
Lupinus angustifolius | 5737 | - |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 235000 | - |
ultracentrifugation | Lupinus angustifolius |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| L-glutamine + 2-oxoglutarate + NADH | Lupinus angustifolius | role in overall ammonia assimilation system, involved in nitrogen metabolism | glutamate + NAD+ | - |
ir | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Lupinus angustifolius | - |
- |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| 500fold purification | Lupinus angustifolius |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| root nodule | - |
Lupinus angustifolius | - |
Specific Activity [micromol/min/mg]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| 18 | - |
- |
Lupinus angustifolius |
Storage Stability
| Storage Stability | Organism |
|---|---|
| phosphate buffer, per week, 20% loss of activity | Lupinus angustifolius |
| Tris buffer, overnight dialysis, total loss of activity | Lupinus angustifolius |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| L-glutamine + 2-oxoglutarate + NADH | absolute substrate specificity | Lupinus angustifolius | L-glutamate + NAD+ | - |
ir | |
| L-glutamine + 2-oxoglutarate + NADH | 2-oxoglutarate may bind first and then L-glutamine, binding steps of NADH and 2-oxoglutarate are independent and random in order, or the mechanism may be ping-pong | Lupinus angustifolius | L-glutamate + NAD+ | - |
ir | |
| L-glutamine + 2-oxoglutarate + NADH | role in overall ammonia assimilation system, involved in nitrogen metabolism | Lupinus angustifolius | glutamate + NAD+ | - |
ir | |
| additional information | no activity with L-asparagine, ammonium sulfate, 2-oxobutyrate, oxaloacetate | Lupinus angustifolius | ? | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| monomer | 1 * 235000, SDS-PAGE | Lupinus angustifolius |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 25 | - |
assay at | Lupinus angustifolius |
Turnover Number [1/s]
| Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 70 | - |
L-glutamine | independent of pH 6.5-9.5 | Lupinus angustifolius | |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 8.5 | - |
- |
Lupinus angustifolius |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| FMN | two flavin prosthetic groups per enzyme molecule, probably FMN | Lupinus angustifolius | |
| NADH | NADH-dependent enzyme, very tight binding of NADH | Lupinus angustifolius | |
Ki Value [mM]
| Ki Value [mM] | Ki Value maximum [mM] | Inhibitor | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.12 | - |
NAD+ | - |
Lupinus angustifolius | |
| 0.7 | - |
L-glutamate | - |
Lupinus angustifolius | |
| 2.7 | - |
L-aspartate | - |
Lupinus angustifolius | |
| 5 | - |
oxaloacetate | - |
Lupinus angustifolius | |
| 14 | - |
L-asparagine | - |
Lupinus angustifolius | |
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