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Literature summary for 3.5.2.15 extracted from
- Structure of the cyanuric acid hydrolase TrzD reveals product exit channel (2017), Sci. Rep., 7, 45277 .
Application
| Application | Comment | Organism |
|---|---|---|
| environmental protection | cyanuric acid hydrolases are of industrial importance because of their use in aquatic recreational facilities to remove cyanuric acid, a stabilizer for the chlorine. Degradation of excess cyanuric acid is necessary to maintain chlorine disinfection in the waters | Enterobacter cloacae |
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| full-length trzD gene, cloned in pET28b(+)vector6, expressed in Escherichia coli BL21 (DE3) | Enterobacter cloacae |
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| crystallized with its natural substrate cyanuric acid by hanging drop, vapor-diffusion experiment in which equal volume of protein (12 mg/ml concentration) and reservoir solution are mixed and allowed to equilibrate against the reservoir at 20 °C. Crystal structure at 2.19 A resolution shows a large displacement of the catalytic lysine (Lys163) in domain 2 away from the active site core, whereas the two other active site lysines from the two other domains are not able to move | Enterobacter cloacae |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Enterobacter cloacae | P0A3V4 | - |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
- |
Enterobacter cloacae |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| cyanuric acid hydrolase | - |
Enterobacter cloacae |
| TrzD | - |
Enterobacter cloacae |
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Release 2023.1 (January 2023)
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