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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 of the enzyme in Escherichia coli strain BL21(DE3) Corynebacterium glutamicum

Protein Variants

Protein Variants Comment Organism
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)

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
-
-
Corynebacterium glutamicum ATCC 13032 Q9X4N0
-
-

Purification (Commentary)

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

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
103
-
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
-
?

Synonyms

Synonyms Comment Organism
ADC
-
Corynebacterium glutamicum
ADCC.g
-
Corynebacterium glutamicum
L-Aspartate-alpha-decarboxylase
-
Corynebacterium glutamicum
PanD
-
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
30 85 activity range, profile overview Corynebacterium glutamicum

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
16 37 purified enzyme, completely stable within this range, pH 6.0, after 12 h Corynebacterium glutamicum
55
-
purified enzyme, 62% activity remaining, pH 6.0, after 12 h Corynebacterium glutamicum
70
-
purified enzyme, complete loss of activity, pH 6.0, after 12 h 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
4 9 activity range, profile overview Corynebacterium glutamicum

pH Stability

pH Stability pH Stability Maximum Comment Organism
3 8 purified enzyme, 37°C, over 60% activity remaining within this range, after 12 h Corynebacterium glutamicum
4 7 purified enzyme, 37°C, over 80% activity remaining within this range, after 12 h Corynebacterium glutamicum