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Literature summary for 2.6.1.47 extracted from
- Enzymatic formation of aminomalonic acid from ketomalonic acid (1958), Nature, 181, 417-418.
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| benzoquinone | 1 mM, 84% inhibition | Bombyx mori |  |
| hydroxylamine | 2 mM, 58% inhibition | Bombyx mori | |
| KCN | 1 mM, 38% inhibition | Bombyx mori | |
| p-chloromercuribenzoate | 1 mM, 99% inhibition | Bombyx mori | |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| DL-alanine + oxomalonate | Rattus norvegicus | glutamate, 2-aminobutyrate, aspartate can also act as amino donors in decreasing order of reactivity, probably involved in the biosynthesis of glycine | pyruvate + aminomalonic acid | - |
? | |
| DL-alanine + oxomalonate | Bombyx mori | glutamate, 2-aminobutyrate, aspartate can also act as amino donors in decreasing order of reactivity, probably involved in the biosynthesis of glycine | pyruvate + aminomalonic acid | - |
? | |
| DL-alanine + oxomalonate | Oryctolagus cuniculus | glutamate, 2-aminobutyrate, aspartate can also act as amino donors in decreasing order of reactivity, probably involved in the biosynthesis of glycine | pyruvate + aminomalonic acid | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Bombyx mori | - |
- |
- |
| Oryctolagus cuniculus | - |
- |
- |
| Rattus norvegicus | - |
- |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| partial | Bombyx mori |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| heart | - |
Oryctolagus cuniculus | - |
| liver | - |
Rattus norvegicus | - |
| liver | - |
Oryctolagus cuniculus | - |
| silk gland | posterior | Bombyx mori | - |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| DL-alanine + oxomalonate | glutamate, 2-aminobutyrate and aspartate can also act as amino donors in decreasing order of reactivity | Rattus norvegicus | pyruvate + aminomalonic acid | - |
? | |
| DL-alanine + oxomalonate | glutamate, 2-aminobutyrate and aspartate can also act as amino donors in decreasing order of reactivity | Bombyx mori | pyruvate + aminomalonic acid | - |
? | |
| DL-alanine + oxomalonate | glutamate, 2-aminobutyrate and aspartate can also act as amino donors in decreasing order of reactivity | Oryctolagus cuniculus | pyruvate + aminomalonic acid | - |
? | |
| DL-alanine + oxomalonate | glutamate, 2-aminobutyrate, aspartate can also act as amino donors in decreasing order of reactivity, probably involved in the biosynthesis of glycine | Rattus norvegicus | pyruvate + aminomalonic acid | - |
? | |
| DL-alanine + oxomalonate | glutamate, 2-aminobutyrate, aspartate can also act as amino donors in decreasing order of reactivity, probably involved in the biosynthesis of glycine | Bombyx mori | pyruvate + aminomalonic acid | - |
? | |
| DL-alanine + oxomalonate | glutamate, 2-aminobutyrate, aspartate can also act as amino donors in decreasing order of reactivity, probably involved in the biosynthesis of glycine | Oryctolagus cuniculus | pyruvate + aminomalonic acid | - |
? | |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 37 | - |
assay at | Bombyx mori |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 9 | 9.2 | - |
Bombyx mori |
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Release 2023.1 (January 2023)
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