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Literature summary for 4.1.1.11 extracted from

  • Shen, Y.; Zhao, L.; Li, Y.; Zhang, L.; Shi, G.
    Synthesis of beta-alanine from L-aspartate using L-aspartate-alpha-decarboxylase from Corynebacterium glutamicum (2014), Biotechnol. Lett., 36, 1681-1686.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
gene panD, recombinant expression in Escherichia coli strain BL21(DE3) Corynebacterium glutamicum

Inhibitors

Inhibitors Comment Organism Structure
L-aspartate substrate inhibition Corynebacterium glutamicum

Natural Substrates/ Products (Substrates)

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

Organism UniProt Comment Textmining
Corynebacterium glutamicum Q9X4N0 gene panD
-
Corynebacterium glutamicum ATCC 13032 Q9X4N0 gene panD
-

Purification (Commentary)

Purification (Comment) Organism
recombinant enzyme 2.1fold from Escherichia coli strain BL21(DE3) by anion exchange chromatography and gel filtration Corynebacterium glutamicum

Specific Activity [micromol/min/mg]

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 and Products (Substrate)

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

Synonyms Comment Organism
ADC
-
Corynebacterium glutamicum
L-Aspartate-alpha-decarboxylase
-
Corynebacterium glutamicum

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
55
-
recombinant enzyme Corynebacterium glutamicum

Temperature Range [°C]

Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
20 80 activity range, profile overview Corynebacterium glutamicum

Temperature Stability [°C]

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

pH Optimum Minimum pH Optimum Maximum Comment Organism
6
-
recombinant enzyme Corynebacterium glutamicum

pH Range

pH Minimum pH Maximum Comment Organism
3 9 activity range, profile overview Corynebacterium glutamicum

pH Stability

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