Phosphonopyruvate decarboxylase

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

3-phosphonopyruvate $\rightleftharpoons$ 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.

[edit] References

IUBMB entry for 4.1.1.82
BRENDA references for 4.1.1.82 (Recommended.)
PubMed references for 4.1.1.82
PubMed Central references for 4.1.1.82
Google Scholar references for 4.1.1.82
Zhang G, Dai J, Lu Z, Dunaway-Mariano D (2003). "The phosphonopyruvate decarboxylase from Bacteroides fragilis". J. Biol. Chem. 278: 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: 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.: 212–9. PMID 9127192.