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Literature summary 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)

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

Inhibitors

EC Number Inhibitors Comment Organism Structure
4.1.1.11 L-aspartate substrate inhibition 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 gene panD
-
4.1.1.11 Corynebacterium glutamicum ATCC 13032 Q9X4N0 gene panD
-

Purification (Commentary)

EC Number Purification (Comment) Organism
4.1.1.11 recombinant enzyme 2.1fold from Escherichia coli strain BL21(DE3) by anion exchange chromatography 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 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
4.1.1.11 0.83
-
 crude recombinant enzyme, pH 6.0, 37°C Corynebacterium glutamicum
4.1.1.11 1.72
-
 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
-
 ?
4.1.1.11 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 ?
-
 ?
4.1.1.11 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

EC Number Synonyms Comment Organism
4.1.1.11 ADC
-
 Corynebacterium glutamicum
4.1.1.11 L-Aspartate-alpha-decarboxylase
-
 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 20 80 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 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

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 3 9 activity range, profile overview Corynebacterium glutamicum

pH Stability

EC Number pH Stability pH Stability Maximum Comment Organism
4.1.1.11 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