The enzyme 4-nitrophenylphosphatase (EC 3.1.3.41) catalyzes the reaction
| 4-nitrophenylphosphatase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 3.1.3.41 | ||||||||
| CAS no. | 9073-68-1 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
- 4-nitrophenyl phosphate + H2O 4-nitrophenol + phosphate
This enzyme belongs to the family of hydrolases, specifically those acting on phosphoric monoester bonds. The systematic name of this enzyme class is 4-nitrophenylphosphate phosphohydrolase. Other names in common use include nitrophenyl phosphatase, p-nitrophenylphosphatase, para-nitrophenyl phosphatase, K-pNPPase, NPPase, PNPPase, Ecto-p-nitrophenyl phosphatase, and p-nitrophenylphosphate phosphohydrolase. This enzyme participates in γ-hexachlorocyclohexane degradation.
Structural studies
editAs of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code PDB: 1VJR.
References
edit- Attias J, Bonnet JL (1972). "A specific alkaline p-nitrophenylphosphatase activity from baker's yeast". Biochim. Biophys. Acta. 268 (2): 422–30. doi:10.1016/0005-2744(72)90338-5. PMID 4554643.
- Attias J, Durand H (1973). "Further characterization of a specific p-nitrophenylphosphatase from baker's yeast". Biochim. Biophys. Acta. 321 (2): 561–8. doi:10.1016/0005-2744(73)90199-x. PMID 4357666.
