Phosphonopyruvate decarboxylase
| Phosphonopyruvate decarboxylase | |||||||
|---|---|---|---|---|---|---|---|
| Identifiers | |||||||
| EC number | 4.1.1.82 | ||||||
| Databases | |||||||
| IntEnz | IntEnz view | ||||||
| BRENDA | BRENDA entry | ||||||
| ExPASy | NiceZyme view | ||||||
| KEGG | KEGG entry | ||||||
| MetaCyc | metabolic pathway | ||||||
| PRIAM | profile | ||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||
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In enzymology, a phosphonopyruvate decarboxylase (EC 4.1.1.82) is an enzyme that catalyzes the chemical reaction
- 3-phosphonopyruvate
2-phosphonoacetaldehyde + CO2
Hence, this enzyme has one substrate, 3-phosphonopyruvate, and two products, 2-phosphonoacetaldehyde and CO2.
This enzyme belongs to the family of lyases, specifically the carboxy-lyases, which cleave carbon-carbon bonds. The systematic name of this enzyme class is 3-phosphonopyruvate carboxy-lyase (2-phosphonoacetaldehyde-forming). This enzyme is also called 3-phosphonopyruvate carboxy-lyase. This enzyme participates in aminophosphonate metabolism.
References
- Zhang G, Dai J, Lu Z, Dunaway-Mariano D (2003). "The phosphonopyruvate decarboxylase from Bacteroides fragilis". J. Biol. Chem. 278 (42): 41302–8. doi:10.1074/jbc.M305976200. PMID 12904299.
- Seidel HM, Knowles JR (1994). "Interaction of inhibitors with phosphoenolpyruvate mutase: implications for the reaction mechanism and the nature of the active site". Biochemistry. 33 (18): 5641–6. doi:10.1021/bi00184a037. PMID 8180189.
- Nakashita H, Watanabe K, Hara O, Hidaka T, Seto H (Tokyo). "Studies on the biosynthesis of bialaphos. Biochemical mechanism of C-P bond formation: discovery of phosphonopyruvate decarboxylase which catalyzes the formation of phosphonoacetaldehyde from phosphonopyruvate". J. Antibiot. (3): 212–9. PMID 9127192.