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Literature summary for 4.1.1.11 extracted from

  • Pei, W.; Zhang, J.; Deng, S.; Tigu, F.; Li, Y.; Li, Q.; Cai, Z.; Li, Y.
    Molecular engineering of L-aspartate-alpha-decarboxylase for improved activity and catalytic stability (2017), Appl. Microbiol. Biotechnol., 101, 6015-6021 .
    View publication on PubMed
Search for more literature for 4.1.1.11

Cloned(Commentary)

Cloned (Comment) Organism
gene panD, recombinant expression of N-terminally His6-tagged enzyme in Escherichia coli strain BL21(DE3), the recombinant ADC protein is mainly in its inactive uncleaved form, possibly because of insufficience of panZ, an activator involved in the cleavage of ADCE Escherichia coli
gene panD, recombinant expression of N-terminally His6-tagged enzyme in Escherichia coli strain BL21(DE3). The cleavage of the recombinant ADC protein from Bacillus subtilis after expression in Escherichia coli is almost complete Bacillus subtilis
gene panD, recombinant expression of N-terminally His6-tagged enzyme in Escherichia coli strain BL21(DE3). The cleavage of the recombinant ADC protein from Corynebacteriums glutamicum after expression in Escherichia coli is almost complete Corynebacterium glutamicum

Protein Variants

Protein Variants Comment Organism
I188M site-directed mutagenesis, the mutant shows increased thermostability compared to the wild-type Bacillus subtilis
additional information mutation of nucleotide L127 increases the enzyme's thermostability compared to the wild-type, while mutation of nuclotide V68 does not significantly affect the thermostability Bacillus subtilis

Inhibitors

Inhibitors Comment Organism Structure
additional information enzyme ADC is also subject to mechanism-based inactivation, which has been reported for many other pyruvoyl-dependent. Mechanism-based inactivation only occurs during catalysis Bacillus subtilis
additional information enzyme ADC is also subject to mechanism-based inactivation, which has been reported for many other pyruvoyl-dependent. Mechanism-based inactivation only occurs during catalysis Corynebacterium glutamicum

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information Michaelis-Menten kinetics Corynebacterium glutamicum
additional information
-
 additional information Michaelis-Menten kinetics Escherichia coli
additional information
-
 additional information Michaelis-Menten kinetics Bacillus subtilis
1.63
-
 L-aspartate pH 7.0, 37°C, recombinant mutant I188M Bacillus subtilis
1.66
-
 L-aspartate pH 7.0, 37°C, recombinant mutant L127X Bacillus subtilis
2.02
-
 L-aspartate pH 7.0, 37°C, recombinant wild-type enzyme 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 ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025
-
 beta-alanine + CO2
-
 ?
L-aspartate Escherichia coli K-12 / DH5alpha
-
 beta-alanine + CO2
-
 ?

Organism

Organism UniProt Comment Textmining
Bacillus subtilis P52999
-
-
Bacillus subtilis 168 P52999
-
-
Corynebacterium glutamicum Q9X4N0
-
-
Corynebacterium glutamicum ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025 Q9X4N0
-
-
Escherichia coli P0A790
-
-
Escherichia coli K-12 / DH5alpha P0A790
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
proteolytic modification the ADC protein is initially translated as an inactive Pi-protein (14 kDa) and then proteolytically cleaved at the Gly24-Ser25 site to generate the active species comprising the pyruvoyl-containing alpha-subunit (11 kDa) and a smaller beta-subunit (3 kDa). The enzyme requires PanZ as an activator involved in the cleavage of ADCE. The recombinant ADC protein expressed from Escherichia coli strain BL21(DE3) is mainly in its inactive uncleaved form, possibly because of insufficience of panZ, an activator involved in the cleavage of ADCE Escherichia coli
proteolytic modification the ADC protein is initially translated as an inactive Pi-protein and then proteolytically cleaved at a site to generate the active species comprising the pyruvoyl-containing alpha-subunit and a smaller beta-subunit. The cleavage of the recombinant ADC protein from Bacillus subtilis after expression in Escherichia coli is almost complete Bacillus subtilis
proteolytic modification the ADC protein is initially translated as an inactive Pi-protein and then proteolytically cleaved at a site to generate the active species comprising the pyruvoyl-containing alpha-subunit and a smaller beta-subunit. The cleavage of the recombinant ADC protein from Corynebacterium glutamicum after expression in Escherichia coli is almost complete Corynebacterium glutamicum

Purification (Commentary)

Purification (Comment) Organism
recombinant His6-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography to over 90% purity Corynebacterium glutamicum
recombinant His6-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography to over 90% purity Escherichia coli
recombinant His6-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography to over 90% purity 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 ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025 beta-alanine + CO2
-
 ?
L-aspartate
-
 Escherichia coli K-12 / DH5alpha beta-alanine + CO2
-
 ?
additional information fluorometric method for beta-alanine determination, development of a high-throughput screening method for beta-alanine detection Corynebacterium glutamicum ?
-
 ?
additional information fluorometric method for beta-alanine determination, development of a high-throughput screening method for beta-alanine detection Escherichia coli ?
-
 ?
additional information fluorometric method for beta-alanine determination, development of a high-throughput screening method for beta-alanine detection Bacillus subtilis ?
-
 ?
additional information fluorometric method for beta-alanine determination, development of a high-throughput screening method for beta-alanine detection Bacillus subtilis 168 ?
-
 ?
additional information fluorometric method for beta-alanine determination, development of a high-throughput screening method for beta-alanine detection Corynebacterium glutamicum ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025 ?
-
 ?
additional information fluorometric method for beta-alanine determination, development of a high-throughput screening method for beta-alanine detection Escherichia coli K-12 / DH5alpha ?
-
 ?

Synonyms

Synonyms Comment Organism
ADC
-
 Corynebacterium glutamicum
ADC
-
 Escherichia coli
ADC
-
 Bacillus subtilis
ADCBs
-
 Bacillus subtilis
ADCCg
-
 Corynebacterium glutamicum
ADCE
-
 Escherichia coli
L-Aspartate-alpha-decarboxylase
-
 Corynebacterium glutamicum
L-Aspartate-alpha-decarboxylase
-
 Escherichia coli
L-Aspartate-alpha-decarboxylase
-
 Bacillus subtilis

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
 assay at Corynebacterium glutamicum
37
-
 assay at Escherichia coli
37
-
 recombinant enzyme Bacillus subtilis

Temperature Range [°C]

Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
37 65 90% of maximal activity at 37°C, 80% at 50°C, and 40% at 65°C Corynebacterium glutamicum
37 65 maximal activity at 37°C, 95% of maximal activity at 50°C, 80% at 60°C, and 70% at 65°C Bacillus subtilis

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
37
-
 purified recombinant enzyme, pH 7.0, about 30% activity remaining after 4 h Bacillus subtilis
37
-
 purified recombinant enzyme, pH 7.0, about 50% activity remaining after 4 h Corynebacterium glutamicum
50
-
 purified recombinant enzyme, pH 7.0, about 20% activity remaining after 2.5 h Corynebacterium glutamicum
50
-
 purified recombinant enzyme, pH 7.0, below 10% activity remaining after 2.5 h Bacillus subtilis
60
-
 purified recombinant enzyme, pH 7.0, below 10% activity remaining after 1 h Corynebacterium glutamicum
60
-
 purified recombinant enzyme, pH 7.0, inactivation after 1 h Bacillus subtilis

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
5.28
-
 L-aspartate pH 7.0, 37°C, recombinant mutant L127X Bacillus subtilis
6.26
-
 L-aspartate pH 7.0, 37°C, recombinant wild-type enzyme Bacillus subtilis
6.6
-
 L-aspartate pH 7.0, 37°C, recombinant mutant I188M Bacillus subtilis

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7
-
 assay at Corynebacterium glutamicum
7
-
 assay at Escherichia coli
7
-
 assay at Bacillus subtilis

Cofactor

Cofactor Comment Organism Structure
additional information the enzyme requires PanZ, an activator involved in the cleavage of ADCE Escherichia coli

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
3.1
-
 L-aspartate pH 7.0, 37°C, recombinant wild-type enzyme Bacillus subtilis
3.18
-
 L-aspartate pH 7.0, 37°C, recombinant mutant L127X Bacillus subtilis
4.05
-
 L-aspartate pH 7.0, 37°C, recombinant mutant I188M Bacillus subtilis