| phosphonoacetate hydrolase | |||||||||
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 Structure of phosphonoacetate hydrolase. PDB entry 1e16. Zinc ions and phosphonoformate are shown in the active site. | |||||||||
| Identifiers | |||||||||
| EC no. | 3.11.1.2 | ||||||||
| CAS no. | 153570-68-4 | ||||||||
| 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 | ||||||||
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In enzymology, a phosphonoacetate hydrolase (EC 3.11.1.2) is an enzyme that catalyzes the chemical reaction
- phosphonoacetate + H2O acetate + phosphate
acetate + phosphateThus, the two substrates of this enzyme are phosphonoacetate and H2O, whereas its two products are acetate and phosphate.
This enzyme belongs to the family of hydrolases, specifically those acting on carbon-phosphorus bonds. The systematic name of this enzyme class is phosphonoacetate phosphonohydrolase. This enzyme participates in aminophosphonate metabolism. It employs one cofactor, zinc.
Structural studies
The structure of this enzyme, with the PDB accession code 1EI6, shows it adopts the alkaline phosphatase fold.
References
- McGrath JW, Wisdom GB, McMullan G, Larkin MJ, Quinn JP (1995). "The purification and properties of phosphonoacetate hydrolase, a novel carbon-phosphorus bond-cleavage enzyme from Pseudomonas fluorescens 23F". Eur. J. Biochem. 234 (1): 225–30. doi:10.1111/j.1432-1033.1995.225_c.x. PMID 8529644.
External links
Media related to Phosphonoacetate hydrolase at Wikimedia Commons
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