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Literature summary extracted from
- Cysteine sulfinic acid decarboxylase activity of Aedes aegypti aspartate 1-decarboxylase: the structural basis of its substrate selectivity (2012), Insect Biochem. Mol. Biol., 42, 396-403.
Crystallization (Commentary)
| EC Number | Crystallization (Comment) | Organism |
|---|---|---|
| 4.1.1.29 | homology modeling and substrate docking suggest that residue Q377, localized at the active site of aspartate decarboxylase, can better interact with aspartate through hydrogen bonding, which may play a role in aspartate selectivity. A leucine residue in mammalian CSADC occupies the same position | Aedes aegypti |
Protein Variants
| EC Number | Protein Variants | Comment | Organism |
|---|---|---|---|
| 4.1.1.11 | Q377L | site-directed mutagenesis, mutation at position 377 from glutamine to leucine in aspartate 1-decarboxylase diminishes its decarboxylation activity to aspartate with no major effect on its cysteine sulfinic acid decarboxylase activity | Aedes aegypti |
| 4.1.1.29 | Q377L | mutation diminishes the decarboxylation activity to aspartate with no major effect on its activity to cysteine sulfinic acid. Mutation leads to increase in the zwitterion form of the internal aldimine tautomer | Aedes aegypti |
KM Value [mM]
| EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 4.1.1.11 | 2.04 | - |
L-aspartate | pH 7.0, 25°C, wild-type enzyme | Aedes aegypti |  |
| 4.1.1.11 | 3.18 | - |
L-aspartate | pH 7.0, 25°C, mutant Q377L | Aedes aegypti | |
| 4.1.1.29 | 1.14 | - |
L-cysteine sulfinate | mutant Q37L, 25°C, pH not specified in the publication | Aedes aegypti | |
| 4.1.1.29 | 1.16 | - |
L-cysteine sulfinate | wild-type, 25°C, pH not specified in the publication | Aedes aegypti | |
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 | Drosophila melanogaster | - |
beta-alanine + CO2 | - |
? | |
| 4.1.1.11 | L-aspartate | Aedes aegypti | - |
beta-alanine + CO2 | - |
? | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 4.1.1.11 | Aedes aegypti | - |
- |
- |
| 4.1.1.11 | Drosophila melanogaster | - |
- |
- |
| 4.1.1.29 | Aedes aegypti | - |
- |
- |
Specific Activity [micromol/min/mg]
| EC Number | Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|---|
| 4.1.1.29 | 6.7 | - |
wild-type, 25°C, pH not specified in the publication | Aedes aegypti |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 4.1.1.11 | L-aspartate | - |
Drosophila melanogaster | beta-alanine + CO2 | - |
? | |
| 4.1.1.11 | L-aspartate | - |
Aedes aegypti | beta-alanine + CO2 | - |
? | |
| 4.1.1.11 | additional information | the enzyme also shows cysteine sulfinic acid decarboxylase activity, EC 4.1.1.29, catalyzing the decarboxylation of cysteine sulfinic acid and cysteic acid | Drosophila melanogaster | ? | - |
? | |
| 4.1.1.11 | additional information | the enzyme also shows cysteine sulfinic acid decarboxylase activity, EC 4.1.1.29, catalyzing the decarboxylation of cysteine sulfinic acid and cysteic acid. Homology modeling of AeADC and substrate docking suggest that residue Q377, localized at the active site of AeADC, could better interact with aspartate through hydrogen bonding, which may play a role in aspartate selectivity | Aedes aegypti | ? | - |
? | |
| 4.1.1.29 | L-Cysteine sulfinate | besides its activity to aspartate, the mosquito enzyme catalyzes the decarboxylation of cysteine sulfinic acid and cysteic acid as efficiently as those of mammalian CSADC under the same testing conditions | Aedes aegypti | 2-Aminoethane sulfinate + CO2 | - |
? | |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 4.1.1.11 | ADC | - |
Drosophila melanogaster |
| 4.1.1.11 | ADC | - |
Aedes aegypti |
| 4.1.1.11 | aspartate-alpha-decarboxylase | - |
Drosophila melanogaster |
| 4.1.1.11 | aspartate-alpha-decarboxylase | - |
Aedes aegypti |
Temperature Optimum [°C]
| EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 4.1.1.11 | 25 | - |
assay at | Drosophila melanogaster |
| 4.1.1.11 | 25 | - |
assay at | Aedes aegypti |
Turnover Number [1/s]
| EC Number | Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 4.1.1.11 | 2.11 | - |
L-aspartate | pH 7.0, 25°C, mutant Q377L | Aedes aegypti | |
| 4.1.1.11 | 7.03 | - |
L-aspartate | pH 7.0, 25°C, wild-type enzyme | Aedes aegypti | |
| 4.1.1.29 | 5.52 | - |
L-cysteine sulfinate | mutant Q377L, 25°C, pH not specified in the publication | Aedes aegypti | |
| 4.1.1.29 | 5.86 | - |
L-cysteine sulfinate | wild-type, 25°C, pH not specified in the publication | Aedes aegypti | |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 4.1.1.11 | 7 | - |
assay at | Drosophila melanogaster |
| 4.1.1.11 | 7 | - |
assay at | Aedes aegypti |
Cofactor
| EC Number | Cofactor | Comment | Organism | Structure |
|---|---|---|---|---|
| 4.1.1.11 | pyridoxal 5'-phosphate | tautomers of the internal aldimine between PLP and enzyme, overview | Aedes aegypti | |
General Information
| EC Number | General Information | Comment | Organism |
|---|---|---|---|
| 4.1.1.11 | additional information | homology modeling and substrate docking, evaluation of potential substrate interacting residues, overview | Aedes aegypti |
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 | 0.66 | - |
L-aspartate | pH 7.0, 25°C, mutant Q377L | Aedes aegypti | |
| 4.1.1.11 | 3.44 | - |
L-aspartate | pH 7.0, 25°C, wild-type enzyme | Aedes aegypti | |
| 4.1.1.29 | 4.84 | - |
L-cysteine sulfinate | mutant Q37L, 25°C, pH not specified in the publication | Aedes aegypti | |
| 4.1.1.29 | 5.05 | - |
L-cysteine sulfinate | wild-type, 25°C, pH not specified in the publication | Aedes aegypti | |
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