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Literature summary extracted from
- Synthesis of beta-alanine from L-aspartate using L-aspartate-alpha-decarboxylase from Corynebacterium glutamicum (2014), Biotechnol. Lett., 36, 1681-1686 .
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 4.1.1.11 | gene panD, recombinant expression of the enzyme in Escherichia coli strain BL21(DE3) | Corynebacterium glutamicum |
Protein Variants
| EC Number | Protein Variants | Comment | Organism |
|---|---|---|---|
| 4.1.1.11 | additional information | synthesis of beta-alanine from L-aspartate using L-aspartate-alpha-decarboxylase from Corynebacterium glutamicum recombinantly expressed in Escherichia coli strain BL21(DE3). A pH-stat directed, fed-batch feeding strategy is developed for enzymatic synthesis of beta-alanine to keep the pH value within pH 6.0-7.2 and attenuate substrate inhibition. A maximum conversion of 97.2% is 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, method optimization, overview. Recombinant enzyme ADC shows best activity in sodium phosphate buffer at pH 6 and more than 80% activity remained between pH 4-7. The Escherichia coli BL21 (DE3)-pET heterologous system provides higher expression efficiency compared with that of homologous expression, which results in a 24fold increase in specific activity of crude enzyme | Corynebacterium glutamicum |
Natural Substrates/ Products (Substrates)
| EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 4.1.1.11 | L-aspartate | Corynebacterium glutamicum | - |
beta-alanine + CO2 | - |
? |  |
| 4.1.1.11 | L-aspartate | Corynebacterium glutamicum ATCC 13032 | - |
beta-alanine + CO2 | - |
? | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 4.1.1.11 | Corynebacterium glutamicum | Q9X4N0 | - |
- |
| 4.1.1.11 | Corynebacterium glutamicum ATCC 13032 | Q9X4N0 | - |
- |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 4.1.1.11 | recombinant enzyme from Escherichia coli strain BL21(DE3) by anion exchange chromatography, ultrafiltration, and gel filtration | Corynebacterium glutamicum |
Specific Activity [micromol/min/mg]
| EC Number | Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|---|
| 4.1.1.11 | 103 | - |
purified recombinant enzyme, pH 6.0, 37°C | Corynebacterium glutamicum |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 4.1.1.11 | L-aspartate | - |
Corynebacterium glutamicum | beta-alanine + CO2 | - |
? | |
| 4.1.1.11 | L-aspartate | - |
Corynebacterium glutamicum ATCC 13032 | beta-alanine + CO2 | - |
? | |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 4.1.1.11 | ADC | - |
Corynebacterium glutamicum |
| 4.1.1.11 | ADCC.g | - |
Corynebacterium glutamicum |
| 4.1.1.11 | L-Aspartate-alpha-decarboxylase | - |
Corynebacterium glutamicum |
| 4.1.1.11 | PanD | - |
Corynebacterium glutamicum |
Temperature Optimum [°C]
| EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 4.1.1.11 | 55 | - |
recombinant enzyme | Corynebacterium glutamicum |
Temperature Range [°C]
| EC Number | Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 4.1.1.11 | 30 | 85 | activity range, profile overview | Corynebacterium glutamicum |
Temperature Stability [°C]
| EC Number | Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 4.1.1.11 | 16 | 37 | purified enzyme, completely stable within this range, pH 6.0, after 12 h | Corynebacterium glutamicum |
| 4.1.1.11 | 55 | - |
purified enzyme, 62% activity remaining, pH 6.0, after 12 h | Corynebacterium glutamicum |
| 4.1.1.11 | 70 | - |
purified enzyme, complete loss of activity, pH 6.0, after 12 h | Corynebacterium glutamicum |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 4.1.1.11 | 6 | - |
recombinant enzyme | Corynebacterium glutamicum |
pH Range
| EC Number | pH Minimum | pH Maximum | Comment | Organism |
|---|---|---|---|---|
| 4.1.1.11 | 4 | 9 | activity range, profile overview | Corynebacterium glutamicum |
pH Stability
| EC Number | pH Stability | pH Stability Maximum | Comment | Organism |
|---|---|---|---|---|
| 4.1.1.11 | 3 | 8 | purified enzyme, 37°C, over 60% activity remaining within this range, after 12 h | Corynebacterium glutamicum |
| 4.1.1.11 | 4 | 7 | purified enzyme, 37°C, over 80% activity remaining within this range, after 12 h | Corynebacterium glutamicum |
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