|Superclasses:||Reactions Classified By Conversion Type → Simple Reactions → Chemical Reactions|
|Reactions Classified By Substrate → Small-Molecule Reactions|
EC Number: 18.104.22.168
Enzymes and Genes:
3-phosphonopyruvate decarboxylase : rhiF , rhiE ( Bacillus subtilis spizizenii ATCC 6633 )
phosphonopyruvate decarboxylase ( Tetrahymena pyriformis )
phosphonopyruvate decarboxylase : dhpF ( Streptomyces luridus )
phosphonopyruvate decarboxylase : ppd ( Streptomyces viridochromogenes )
phosphonopyruvate decarboxylase : fom2 ( Streptomyces wedmorensis )
The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.
Most BioCyc compounds have been protonated to a reference pH value of 7.3, and some reactions have been computationally balanced for hydrogen by adding free protons. Please see the PGDB Concepts Guide for more information.
Mass balance status: Balanced.
Enzyme Commission Primary Name: phosphonopyruvate decarboxylase
Enzyme Commission Synonyms: 3-phosphonopyruvate carboxy-lyase
Standard Gibbs Free Energy (ΔrG'° in kcal/mol): -2.8417358 [Latendresse13]
Enzyme Commission Summary:
Catalyzes a step in the biosynthetic pathway of 2 aminoethylphosphonate, a component of the capsular polysaccharide complex of Bacteroides fragilis. Activated by the divalent cations Mg(2+), Ca(2+) and Mn(2+). Pyruvate and sulfopyruvate can also act as substrates, but more slowly.
Nakashita97: Nakashita H, Watanabe K, Hara O, Hidaka T, Seto H (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. PMID: 9127192
Seidel94: 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. PMID: 8180189
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