Cloned (Comment) | Organism |
---|---|
gene panD, recombinant expression in Escherichia coli strain BL21(DE3) | Corynebacterium glutamicum |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
L-aspartate | substrate inhibition | Corynebacterium glutamicum |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
L-aspartate | Corynebacterium glutamicum | - |
beta-alanine + CO2 | - |
? | |
L-aspartate | Corynebacterium glutamicum ATCC 13032 | - |
beta-alanine + CO2 | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Corynebacterium glutamicum | Q9X4N0 | gene panD | - |
Corynebacterium glutamicum ATCC 13032 | Q9X4N0 | gene panD | - |
Purification (Comment) | Organism |
---|---|
recombinant enzyme 2.1fold from Escherichia coli strain BL21(DE3) by anion exchange chromatography and gel filtration | Corynebacterium glutamicum |
Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|
additional information | - |
maximum conversion of 97.2% obtained with an initial 5 g L-aspartate/l and another three feedings of 0.5% w/v L-aspartate at 8 h intervals. The final beta-alanine concentration is 12.85 g/l after 36 h | Corynebacterium glutamicum |
0.83 | - |
crude recombinant enzyme, pH 6.0, 37°C | Corynebacterium glutamicum |
1.72 | - |
purified recombinant enzyme, pH 6.0, 37°C | Corynebacterium glutamicum |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
L-aspartate | - |
Corynebacterium glutamicum | beta-alanine + CO2 | - |
? | |
L-aspartate | - |
Corynebacterium glutamicum ATCC 13032 | beta-alanine + CO2 | - |
? | |
additional information | large-scale enzymatic production of beta-alanine from L-aspartate by pH-stat directed, fed-batch-feeding strategy, method development and evaluation, overview | Corynebacterium glutamicum | ? | - |
? | |
additional information | large-scale enzymatic production of beta-alanine from L-aspartate by pH-stat directed, fed-batch-feeding strategy, method development and evaluation, overview | Corynebacterium glutamicum ATCC 13032 | ? | - |
? |
Synonyms | Comment | Organism |
---|---|---|
ADC | - |
Corynebacterium glutamicum |
L-Aspartate-alpha-decarboxylase | - |
Corynebacterium glutamicum |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
55 | - |
recombinant enzyme | Corynebacterium glutamicum |
Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
---|---|---|---|
20 | 80 | activity range, profile overview | Corynebacterium glutamicum |
Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|
16 | 37 | purified recombinant enzyme, highly stable at, the enzyme retains over 30% activity within this range after 12 h at pH 6.0, inactivation at 80°C and above | Corynebacterium glutamicum |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
6 | - |
recombinant enzyme | Corynebacterium glutamicum |
pH Minimum | pH Maximum | Comment | Organism |
---|---|---|---|
3 | 9 | activity range, profile overview | Corynebacterium glutamicum |
pH Stability | pH Stability Maximum | Comment | Organism |
---|---|---|---|
4 | 7 | purified recombinant enzyme, highly stable at, the enzyme retains over 80% activity within this range after 12 h at 37°C | Corynebacterium glutamicum |