Inhibitors | Comment | Organism | Structure |
---|---|---|---|
3-acetylpyridine adenine dinucleotide | competitive inhibitor with respect to NADH | Lupinus angustifolius | |
NADH | substrate inhibition at high concentrations | Lupinus angustifolius |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.0013 | - |
NADH | - |
Lupinus angustifolius | |
0.0014 | - |
NADH | NADH-dependent reduction of oxidized form of 3-acetylpyridine adenine dinucleotide | Lupinus angustifolius | |
0.003 | - |
3-acetylpyridine adenine dinucleotide | reduced form | Lupinus angustifolius | |
0.006 | - |
2-oxoglutarate | with reduced form of 3-acetylpyridine adenine dinucleotide as reductant | Lupinus angustifolius | |
0.014 | - |
3-acetylpyridine adenine dinucleotide | NADH-dependent reduction of oxidized form of 3-acetylpyridine adenine dinucleotide | Lupinus angustifolius | |
0.024 | - |
2-oxoglutarate | - |
Lupinus angustifolius | |
0.125 | - |
L-glutamine | with reduced form of 3-acetylpyridine adenine dinucleotide as reductant | Lupinus angustifolius | |
0.5 | - |
L-glutamine | - |
Lupinus angustifolius |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
cytosol | - |
Lupinus angustifolius | 5829 | - |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
L-glutamine + 2-oxoglutarate + NADH | Lupinus angustifolius | key enzyme in pathway of assimilation of symbiotically fixed N2 into amino acids | glutamate + NAD+ | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Lupinus angustifolius | - |
- |
- |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
root nodule | - |
Lupinus angustifolius | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
L-glutamine + 2-oxoglutarate + NADH | NADH binds first before enzyme is capable to bind other substrates | Lupinus angustifolius | L-glutamate + NAD+ | - |
? | |
L-glutamine + 2-oxoglutarate + NADH | key enzyme in pathway of assimilation of symbiotically fixed N2 into amino acids | Lupinus angustifolius | glutamate + NAD+ | - |
? | |
L-glutamine + 2-oxoglutarate + reduced form of 3-acetylpyridine adenine dinucleotide | reduced form of 3-acetylpyridine adenine dinucleotide is an alternative reductant to NADH, binds as tightly as NADH, enzyme catalyzes NADH-dependent reduction of AcPdAD+ by a substituted-enzyme ping-pong mechanism | Lupinus angustifolius | L-glutamine + oxidized form of 3-acetylpyridine adenine dinucleotide | - |
? | |
additional information | - |
Lupinus angustifolius | ? | - |
? |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
25 | - |
assay at | Lupinus angustifolius |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
18 | - |
3-acetylpyridine adenine dinucleotide | reduced form as reductant, glutamate synthase reaction | Lupinus angustifolius | |
51 | - |
3-acetylpyridine adenine dinucleotide | NADH-dependent reduction of oxidized form of 3-acetylpyridine adenine dinucleotide | Lupinus angustifolius | |
70 | - |
NADH | - |
Lupinus angustifolius |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
3-acetylpyridine adenine dinucleotide | reduced form is an alternative reductant, binds as tightly as NADH | Lupinus angustifolius | |
NADH | - |
Lupinus angustifolius |
Ki Value [mM] | Ki Value maximum [mM] | Inhibitor | Comment | Organism | Structure |
---|---|---|---|---|---|
0.001 | - |
3-acetylpyridine adenine dinucleotide | - |
Lupinus angustifolius | |
0.01 | - |
NADH | - |
Lupinus angustifolius |