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Literature summary for 3.5.2.2 extracted from
- Crystal structures of monometallic dihydropyrimidinase and the human dihydroorotase domain K1556A mutant reveal no lysine carbamylation within the active site (2018), Biochem. Biophys. Res. Commun., 505, 439-444 .
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| recombinant expression of His-tagged enzyme | Pseudomonas aeruginosa |
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| mono-Zn PaDHPase, hanging drop vapor diffusion method, mixing of 20 mg/ml protein in 20 mM HEPES and 100 mM NaCl, pH 7.0, with reservoir solution containing 25% PEG 4000, 100 mM Tris-HCl, 200 mM calcium chloride, pH 8.5, at room temperature, X-ray diffraction structure determination and analysis at 2.23 A resolution | Pseudomonas aeruginosa |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| additional information | EDTA alone is a poor chelator for removal of metal in PaDHPase | Pseudomonas aeruginosa |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| additional information | EDTA alone is a poor chelator for removal of metal in PaDHPase | Pseudomonas aeruginosa | |
| Zn2+ | di-zinc metalloenzyme, one metal coordination is not sufficient to fix CO2 to the Lys in bacterial DHPase. Preparation and characterization of mono-Zn DHPase from Pseudomonas aeruginosa revealing no catalytic activity of mono-Zn PaDHPase can be detected, Lys150 is no longer carbamylated, mass spectrometric analysis. Posttranslational carbamylated Lys is not required for Znalpha binding in PaDHPase. Znalpha is coordinated by residues H59, H61, K150, D316, H183, and H239 in mono-Zn PaDHPase. In di-zinf PaDHPase, zinc alpha is coordinated by residues H59, H61, Kcx150, and D316, while zinc beta is coordinated by H183, H239, K150, and zinc alpha | Pseudomonas aeruginosa |  |
| Zn2+ | zinc metalloenzyme, one zinc ion is sufficient to stabilize Lys carbamylation in Tetraodon nigroviridis dihydropyrimidinase (DHPase). Lys155 is carbamylated, structure, overview | Tetraodon nigroviridis | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Pseudomonas aeruginosa | Q9I676 | - |
- |
| Pseudomonas aeruginosa 1C | Q9I676 | - |
- |
| Pseudomonas aeruginosa ATCC 15692 | Q9I676 | - |
- |
| Pseudomonas aeruginosa CIP 104116 | Q9I676 | - |
- |
| Pseudomonas aeruginosa DSM 22644 | Q9I676 | - |
- |
| Pseudomonas aeruginosa JCM 14847 | Q9I676 | - |
- |
| Pseudomonas aeruginosa LMG 12228 | Q9I676 | - |
- |
| Pseudomonas aeruginosa PRS 101 | Q9I676 | - |
- |
| Tetraodon nigroviridis | - |
- |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant His-tagged enzyme by nickel affinity chromatography and dialysis to over 97% purity | Pseudomonas aeruginosa |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | one zinc ion is sufficient to stabilize Lys carbamylation in Tetraodon nigroviridis dihydropyrimidinase (DHPase) | Pseudomonas aeruginosa | ? | - |
- |
|
| additional information | one zinc ion is sufficient to stabilize Lys carbamylation in Tetraodon nigroviridis dihydropyrimidinase (DHPase) | Tetraodon nigroviridis | ? | - |
- |
|
| additional information | one zinc ion is sufficient to stabilize Lys carbamylation in Tetraodon nigroviridis dihydropyrimidinase (DHPase) | Pseudomonas aeruginosa ATCC 15692 | ? | - |
- |
|
| additional information | one zinc ion is sufficient to stabilize Lys carbamylation in Tetraodon nigroviridis dihydropyrimidinase (DHPase) | Pseudomonas aeruginosa 1C | ? | - |
- |
|
| additional information | one zinc ion is sufficient to stabilize Lys carbamylation in Tetraodon nigroviridis dihydropyrimidinase (DHPase) | Pseudomonas aeruginosa PRS 101 | ? | - |
- |
|
| additional information | one zinc ion is sufficient to stabilize Lys carbamylation in Tetraodon nigroviridis dihydropyrimidinase (DHPase) | Pseudomonas aeruginosa DSM 22644 | ? | - |
- |
|
| additional information | one zinc ion is sufficient to stabilize Lys carbamylation in Tetraodon nigroviridis dihydropyrimidinase (DHPase) | Pseudomonas aeruginosa CIP 104116 | ? | - |
- |
|
| additional information | one zinc ion is sufficient to stabilize Lys carbamylation in Tetraodon nigroviridis dihydropyrimidinase (DHPase) | Pseudomonas aeruginosa LMG 12228 | ? | - |
- |
|
| additional information | one zinc ion is sufficient to stabilize Lys carbamylation in Tetraodon nigroviridis dihydropyrimidinase (DHPase) | Pseudomonas aeruginosa JCM 14847 | ? | - |
- |
|
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| DHPase | - |
Pseudomonas aeruginosa |
| DHPase | - |
Tetraodon nigroviridis |
| PaDHPase | - |
Pseudomonas aeruginosa |
General Information
| General Information | Comment | Organism |
|---|---|---|
| evolution | dihydropyrimidinase (DHPase) is a member of the cyclic amidohydrolase family, which also includes allantoinase, dihydroorotase (DHOase), hydantoinase, and imidase. Almost all of these zinc metalloenzymes possess a binuclear metal center in which two metal ions are bridged by a post-translational carbamylated Lys | Pseudomonas aeruginosa |
| evolution | dihydropyrimidinase (DHPase) is a member of the cyclic amidohydrolase family, which also includes allantoinase, dihydroorotase (DHOase), hydantoinase, and imidase. Almost all of these zinc metalloenzymes possess a binuclear metal center in which two metal ions are bridged by a post-translational carbamylated Lys | Tetraodon nigroviridis |
| additional information | structure-activity relationship analysis | Pseudomonas aeruginosa |
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