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Literature summary 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

Cloned(Commentary)

EC Number Cloned (Comment) Organism
4.1.1.11 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
4.1.1.11 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
4.1.1.11 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

EC Number Protein Variants Comment Organism
4.1.1.11 I188M site-directed mutagenesis, the mutant shows increased thermostability compared to the wild-type Bacillus subtilis
4.1.1.11 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

EC Number Inhibitors Comment Organism Structure
4.1.1.11 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
4.1.1.11 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]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
4.1.1.11 additional information
-
 additional information Michaelis-Menten kinetics Corynebacterium glutamicum
4.1.1.11 additional information
-
 additional information Michaelis-Menten kinetics Escherichia coli
4.1.1.11 additional information
-
 additional information Michaelis-Menten kinetics Bacillus subtilis
4.1.1.11 1.63
-
 L-aspartate pH 7.0, 37°C, recombinant mutant I188M Bacillus subtilis
4.1.1.11 1.66
-
 L-aspartate pH 7.0, 37°C, recombinant mutant L127X Bacillus subtilis
4.1.1.11 2.02
-
 L-aspartate pH 7.0, 37°C, recombinant wild-type enzyme Bacillus subtilis

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 Escherichia coli
-
 beta-alanine + CO2
-
 ?
4.1.1.11 L-aspartate Bacillus subtilis
-
 beta-alanine + CO2
-
 ?
4.1.1.11 L-aspartate Bacillus subtilis 168
-
 beta-alanine + CO2
-
 ?
4.1.1.11 L-aspartate Corynebacterium glutamicum ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025
-
 beta-alanine + CO2
-
 ?
4.1.1.11 L-aspartate Escherichia coli K-12 / DH5alpha
-
 beta-alanine + CO2
-
 ?

Organism

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

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
4.1.1.11 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
4.1.1.11 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
4.1.1.11 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)

EC Number Purification (Comment) Organism
4.1.1.11 recombinant His6-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography to over 90% purity Corynebacterium glutamicum
4.1.1.11 recombinant His6-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography to over 90% purity Escherichia coli
4.1.1.11 recombinant His6-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography to over 90% purity Bacillus subtilis

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
-
 Escherichia coli beta-alanine + CO2
-
 ?
4.1.1.11 L-aspartate
-
 Bacillus subtilis beta-alanine + CO2
-
 ?
4.1.1.11 L-aspartate
-
 Bacillus subtilis 168 beta-alanine + CO2
-
 ?
4.1.1.11 L-aspartate
-
 Corynebacterium glutamicum ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025 beta-alanine + CO2
-
 ?
4.1.1.11 L-aspartate
-
 Escherichia coli K-12 / DH5alpha beta-alanine + CO2
-
 ?
4.1.1.11 additional information fluorometric method for beta-alanine determination, development of a high-throughput screening method for beta-alanine detection Corynebacterium glutamicum ?
-
 ?
4.1.1.11 additional information fluorometric method for beta-alanine determination, development of a high-throughput screening method for beta-alanine detection Escherichia coli ?
-
 ?
4.1.1.11 additional information fluorometric method for beta-alanine determination, development of a high-throughput screening method for beta-alanine detection Bacillus subtilis ?
-
 ?
4.1.1.11 additional information fluorometric method for beta-alanine determination, development of a high-throughput screening method for beta-alanine detection Bacillus subtilis 168 ?
-
 ?
4.1.1.11 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 ?
-
 ?
4.1.1.11 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

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

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
4.1.1.11 37
-
 assay at Corynebacterium glutamicum
4.1.1.11 37
-
 assay at Escherichia coli
4.1.1.11 37
-
 recombinant enzyme Bacillus subtilis

Temperature Range [°C]

EC Number Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
4.1.1.11 37 65 90% of maximal activity at 37°C, 80% at 50°C, and 40% at 65°C Corynebacterium glutamicum
4.1.1.11 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]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
4.1.1.11 37
-
 purified recombinant enzyme, pH 7.0, about 30% activity remaining after 4 h Bacillus subtilis
4.1.1.11 37
-
 purified recombinant enzyme, pH 7.0, about 50% activity remaining after 4 h Corynebacterium glutamicum
4.1.1.11 50
-
 purified recombinant enzyme, pH 7.0, about 20% activity remaining after 2.5 h Corynebacterium glutamicum
4.1.1.11 50
-
 purified recombinant enzyme, pH 7.0, below 10% activity remaining after 2.5 h Bacillus subtilis
4.1.1.11 60
-
 purified recombinant enzyme, pH 7.0, below 10% activity remaining after 1 h Corynebacterium glutamicum
4.1.1.11 60
-
 purified recombinant enzyme, pH 7.0, inactivation after 1 h Bacillus subtilis

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
4.1.1.11 5.28
-
 L-aspartate pH 7.0, 37°C, recombinant mutant L127X Bacillus subtilis
4.1.1.11 6.26
-
 L-aspartate pH 7.0, 37°C, recombinant wild-type enzyme Bacillus subtilis
4.1.1.11 6.6
-
 L-aspartate pH 7.0, 37°C, recombinant mutant I188M Bacillus subtilis

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
4.1.1.11 7
-
 assay at Corynebacterium glutamicum
4.1.1.11 7
-
 assay at Escherichia coli
4.1.1.11 7
-
 assay at Bacillus subtilis

Cofactor

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

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
4.1.1.11 3.1
-
 L-aspartate pH 7.0, 37°C, recombinant wild-type enzyme Bacillus subtilis
4.1.1.11 3.18
-
 L-aspartate pH 7.0, 37°C, recombinant mutant L127X Bacillus subtilis
4.1.1.11 4.05
-
 L-aspartate pH 7.0, 37°C, recombinant mutant I188M Bacillus subtilis