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Literature summary for 4.1.1.11 extracted from

  • Deng, S.; Zhang, J.; Cai, Z.; Li, Y.
    Characterization of L-aspartate-alpha-decarboxylase from Bacillus subtilis (2015), Chin. J. Biotechnol., 31, 1184-1193 .
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
PanZ the enzyme requires activation by PanZ to be posttranslationally cleaved Escherichia coli

Application

Application Comment Organism
synthesis the enzyme is used for industrial production of beta-alanine from L-aspartate Corynebacterium glutamicum
synthesis the enzyme is used for industrial production of beta-alanine from L-aspartate Escherichia coli
synthesis the enzyme is used for industrial production of beta-alanine from L-aspartate Bacillus subtilis

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 Escherichia coli
-
beta-alanine + CO2
-
?
L-aspartate Bacillus subtilis
-
beta-alanine + CO2
-
?
L-aspartate Bacillus subtilis 168
-
beta-alanine + CO2
-
?
L-aspartate Corynebacterium glutamicum DSM 20300
-
beta-alanine + CO2
-
?

Organism

Organism UniProt Comment Textmining
Bacillus subtilis P52999
-
-
Bacillus subtilis 168 P52999
-
-
Corynebacterium glutamicum Q9X4N0
-
-
Corynebacterium glutamicum DSM 20300 Q9X4N0
-
-
Escherichia coli P0A790
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
proteolytic modification the enzyme performs self-cleavage posttranslationally Corynebacterium glutamicum
proteolytic modification the enzyme performs self-cleavage posttranslationally Bacillus subtilis
proteolytic modification the enzyme requires activation by PanZ to be posttranslationally cleaved Escherichia coli

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
0.98
-
pH and temperature not specified in the publication Escherichia coli
7.52
-
pH and temperature not specified in the publication Corynebacterium glutamicum
8.4
-
pH and temperature not specified in the publication Bacillus subtilis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-aspartate
-
Corynebacterium glutamicum beta-alanine + CO2
-
?
L-aspartate
-
Escherichia coli beta-alanine + CO2
-
?
L-aspartate
-
Bacillus subtilis beta-alanine + CO2
-
?
L-aspartate
-
Bacillus subtilis 168 beta-alanine + CO2
-
?
L-aspartate
-
Corynebacterium glutamicum DSM 20300 beta-alanine + CO2
-
?

Synonyms

Synonyms Comment Organism
L-Aspartate-alpha-decarboxylase
-
Corynebacterium glutamicum
L-Aspartate-alpha-decarboxylase
-
Escherichia coli
L-Aspartate-alpha-decarboxylase
-
Bacillus subtilis
PanD
-
Corynebacterium glutamicum
PanD
-
Escherichia coli
PanD
-
Bacillus subtilis

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
60
-
-
Bacillus subtilis
65
-
-
Corynebacterium glutamicum

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6.5
-
-
Corynebacterium glutamicum
6.5
-
-
Bacillus subtilis