Phosphonopyruvate decarboxylase

In enzymology, a phosphonopyruvate decarboxylase (EC 4.1.1.82) is an enzyme that catalyzes the chemical reaction

3-phosphonopyruvate ${\displaystyle \rightleftharpoons }$ 2-phosphonoacetaldehyde + CO₂

Hence, this enzyme has one substrate, , and two products, 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 (March 1997). "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. Tokyo. 50 (3): 212–9. doi:10.7164/antibiotics.50.212. PMID 9127192.