Phosphonopyruvate decarboxylase
Phosphonopyruvate decarboxylase | |||||||||
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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. "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. Tokyo. Antibiot. (3): 212–9. PMID 9127192.
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