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Literature summary for 1.1.1.40 extracted from
- Conformational changes of maize and wheat NADP-malic enzyme studied by quenching of protein native fluorescence (2007), Int. J. Biol. Macromol., 41, 64-71.
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Mg2+ | required | Triticum aestivum |  |
| Mg2+ | required | Zea mays | |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 61300 | - |
1 * 61300, about, DNA sequence calculation | Zea mays |
| 61300 | - |
2 * 61300, about, DNA sequence calculation | Zea mays |
| 61300 | - |
4 * 61300, about, DNA sequence calculation | Zea mays |
| 72000 | - |
1 * 72000, SDS-PAGE | Triticum aestivum |
| 72000 | - |
2 * 72000, SDS-PAGE | Triticum aestivum |
| 72000 | - |
4 * 72000, SDS-PAGE | Triticum aestivum |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| (S)-malate + NADP+ | Triticum aestivum | - |
pyruvate + CO2 + NADPH | - |
r | |
| (S)-malate + NADP+ | Zea mays | - |
pyruvate + CO2 + NADPH | - |
r | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Triticum aestivum | - |
- |
- |
| Zea mays | - |
- |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| (S)-malate + NADP+ | - |
Triticum aestivum | pyruvate + CO2 + NADPH | - |
r | |
| (S)-malate + NADP+ | - |
Zea mays | pyruvate + CO2 + NADPH | - |
r | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| dimer | 2 * 72000, SDS-PAGE | Triticum aestivum |
| dimer | 2 * 61300, about, DNA sequence calculation | Zea mays |
| monomer | 1 * 72000, SDS-PAGE | Triticum aestivum |
| monomer | 1 * 61300, about, DNA sequence calculation | Zea mays |
| More | the enzyme exists in several different oligomeric states depending on the metabolite concentrations, light status, ionic strength as well as pH, conformational changes of guanidine hydrochloride-denatured NADP-malic enzyme studied by quenching of protein native fluorescence with KI and acrylamide, overview | Triticum aestivum |
| More | the enzyme exists in several different oligomeric states depending on the metabolite concentrations, light status, ionic strength as well as pH, conformational changes of guanidine hydrochloride-denatured NADP-malic enzyme studied by quenching of protein native fluorescence with KI and acrylamide, overview | Zea mays |
| tetramer | 4 * 72000, SDS-PAGE | Triticum aestivum |
| tetramer | 4 * 61300, about, DNA sequence calculation | Zea mays |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| L-malate: NADP oxidoreductase [oxaloacetate decarboxylating] | - |
Triticum aestivum |
| L-malate: NADP oxidoreductase [oxaloacetate decarboxylating] | - |
Zea mays |
| NADP-malic enzyme | - |
Triticum aestivum |
| NADP-malic enzyme | - |
Zea mays |
| NADP-ME | - |
Triticum aestivum |
| NADP-ME | - |
Zea mays |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 30 | - |
assay at | Triticum aestivum |
| 30 | - |
assay at | Zea mays |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 50 | - |
15 min, pH 8.0, irreversible thermal inactivation | Zea mays |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7 | - |
assay at | Triticum aestivum |
| 8 | - |
assay at | Zea mays |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| NADP+ | - |
Triticum aestivum | |
| NADP+ | - |
Zea mays | |
| NADPH | - |
Triticum aestivum | |
| NADPH | - |
Zea mays | |
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