EC Number | Cloned (Comment) | Organism |
---|---|---|
4.1.1.12 | gene asd, DNA and amino acid sequence determination and analysis, sequence comparisons | Pseudomonas sp. |
EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
2.6.1.1 | Y225R/R292K/R386A | the mutation converts its activity into an aspartate 4-decarboxylase | Escherichia coli |
4.1.1.12 | D360P | site-directed mutagenesis, the mutant shows similar 4-decarboxylation activity but reduced aminotransferase compared to the wild-type enzyme | Pseudomonas sp. |
4.1.1.12 | F204W | site-directed mutagenesis, the mutant shows slightly reduced 4-decarboxylation activity but highly increased aminotransferase compared to the wild-type enzyme | Pseudomonas sp. |
4.1.1.12 | H123Y | site-directed mutagenesis, the mutant shows reduced 4-decarboxylation activity and slightly increased aminotransferase compared to the wild-type enzyme | Pseudomonas sp. |
4.1.1.12 | H337R | site-directed mutagenesis, the mutant shows reduced 4-decarboxylation activity but similar aminotransferase compared to the wild-type enzyme | Pseudomonas sp. |
4.1.1.12 | K347R | site-directed mutagenesis, the mutant shows similar 4-decarboxylation activity but reduced aminotransferase compared to the wild-type enzyme | Pseudomonas sp. |
4.1.1.12 | M178L | site-directed mutagenesis, the mutant shows reduced 4-decarboxylation activity but unaltered aminotransferase compared to the wild-type enzyme | Pseudomonas sp. |
4.1.1.12 | V475L | site-directed mutagenesis, the mutant shows slightly reduced 4-decarboxylation activity but unaltered aminotransferase compared to the wild-type enzyme | Pseudomonas sp. |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
4.1.1.12 | L-aspartate | Pseudomonas sp. | - |
L-alanine + CO2 | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
2.6.1.1 | Escherichia coli | P00509 | - |
- |
4.1.1.12 | Pseudomonas sp. | Q53IZ1 | strain ATCC 19121 | - |
EC Number | Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|---|
2.6.1.1 | 0.06 | - |
wild type enzyme, at 37°C | Escherichia coli |
4.1.1.12 | additional information | - |
4-decarboxylation activity and aminotransferase activity of mutant enzymes, overview | Pseudomonas sp. |
4.1.1.12 | 0.06 | - |
recombinant wild-type enzyme, aminotransferase activity | Pseudomonas sp. |
4.1.1.12 | 128.8 | - |
recombinant wild-type enzyme, 4-decarboxylation activity | Pseudomonas sp. |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
2.6.1.1 | L-aspartate + 2-oxoglutarate | - |
Escherichia coli | oxaloacetate + L-glutamate | - |
? | |
4.1.1.12 | L-aspartate | - |
Pseudomonas sp. | L-alanine + CO2 | - |
? | |
4.1.1.12 | additional information | Asd is a bifunctional enzyme performing decarboxylation and aminotransferase activities on L-aspartate | Pseudomonas sp. | ? | - |
? |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
2.6.1.1 | AspAT | - |
Escherichia coli |
4.1.1.12 | Asd | - |
Pseudomonas sp. |
4.1.1.12 | L-aspartate 4-decarboxylase | - |
Pseudomonas sp. |
EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|---|
4.1.1.12 | 37 | - |
assay at | Pseudomonas sp. |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
4.1.1.12 | 5 | - |
assay at | Pseudomonas sp. |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
4.1.1.12 | pyridoxal 5'-phosphate | dependent on | Pseudomonas sp. |