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Literature summary for 4.1.1.11 extracted from
- Significance of Arg3, Arg54, and Tyr58 of L-aspartate alpha-decarboxylase from Corynebacterium glutamicum in the process of self-cleavage (2014), Biotechnol. Lett., 36, 121-126.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| gene panD, expression of wild-type and mutant enzymes in Escherichia coli | Corynebacterium glutamicum |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| R3A | site-directed mutagenesis, the mutant is no longer able to activate via self-cleavage | Corynebacterium glutamicum |
| R3D | site-directed mutagenesis, the mutant is no longer able to activate via self-cleavage | Corynebacterium glutamicum |
| R3E | site-directed mutagenesis, the mutant is no longer able to activate via self-cleavage | Corynebacterium glutamicum |
| R3L | site-directed mutagenesis, the mutant is no longer able to activate via self-cleavage | Corynebacterium glutamicum |
| R3N | site-directed mutagenesis, the mutant is no longer able to activate via self-cleavage | Corynebacterium glutamicum |
| R3Q | site-directed mutagenesis, the mutant is no longer able to activate via self-cleavage | Corynebacterium glutamicum |
| R54A | site-directed mutagenesis, the mutant shows highly reduced self-cleavage activity compared to the wild-type enzyme | Corynebacterium glutamicum |
| R54K | site-directed mutagenesis, the mutant shows highly reduced self-cleavage activity compared to the wild-type enzyme | Corynebacterium glutamicum |
| Y58A | site-directed mutagenesis, the mutant shows highly reduced self-cleavage activity compared to the wild-type enzyme | Corynebacterium glutamicum |
| Y58T | site-directed mutagenesis, the mutant shows highly reduced self-cleavage activity compared to the wild-type 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 | gene panD | - |
| Corynebacterium glutamicum ATCC 13032 | Q9X4N0 | gene panD | - |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant wild-type and mutant enzymes from Escherichia coli | Corynebacterium glutamicum |
Specific Activity [micromol/min/mg]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| 2.4 | - |
self-cleavage activity, purified recombinant mutant Z58A, pH 7.4, 37°C | Corynebacterium glutamicum |
| 2.6 | - |
self-cleavage activity, purified recombinant mutant Z58T, pH 7.4, 37°C | Corynebacterium glutamicum |
| 3.5 | - |
self-cleavage activity, purified recombinant mutant R54A, pH 7.4, 37°C | Corynebacterium glutamicum |
| 4 | - |
self-cleavage activity, purified recombinant mutant R54K, pH 7.4, 37°C | Corynebacterium glutamicum |
| 690 | - |
self-cleavage activity, purified recombinant wild-type enzyme, pH 7.4, 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 | - |
? | |
| additional information | the enzyme performs self-cleavage for catalytic activition | Corynebacterium glutamicum | ? | - |
? | |
| additional information | the enzyme performs self-cleavage for catalytic activition | Corynebacterium glutamicum ATCC 13032 | ? | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| More | proform enzyme structure homology modeling, overview | Corynebacterium glutamicum |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| ADC | - |
Corynebacterium glutamicum |
| L-Aspartate alpha-decarboxylase | - |
Corynebacterium glutamicum |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 37 | - |
assay at | Corynebacterium glutamicum |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7.4 | - |
assay at | Corynebacterium glutamicum |
General Information
| General Information | Comment | Organism |
|---|---|---|
| additional information | three key amino acid residues, R54, Y58, and R3, of L-aspartate alpha-decarboxylase act remotely from its cleavage site for its functional self-cleavage as well as for its catalytic activity. Highly conserved R54 residue contributes to the enzyme substrate specificity, and the highly conserved Y58 residue acts as the proton donor in the decarboxylation reaction. R54 and Y58 residues are also related with the self-cleavage process. The R54 and Y58 residues also block the formation of the active pyruvoyl cofactor, therefore the R54 and Y58 residues are assisting the R3 residue in the ADC self-cleavage process | Corynebacterium glutamicum |
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