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June 28th 2015
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June 28th 2015
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MetaCyc Reaction: 4.1.1.82

Superclasses: Reactions Classified By Conversion Type Simple Reactions Chemical Reactions
Reactions Classified By Substrate Small-Molecule Reactions

EC Number: 4.1.1.82

Enzymes and Genes:

Bacillus subtilis spizizenii ATCC 6633 : 3-phosphonopyruvate decarboxylase Inferred from experiment Inferred by computational analysis : rhiF , rhiE
Streptomyces luridus : phosphonopyruvate decarboxylase Inferred from experiment : dhpF
Streptomyces viridochromogenes : phosphonopyruvate decarboxylase Inferred from experiment : ppd
Streptomyces wedmorensis : phosphonopyruvate decarboxylase Inferred from experiment : fom2
Tetrahymena pyriformis : phosphonopyruvate decarboxylase Inferred from experiment

In Pathway: phosphinothricin tripeptide biosynthesis , dehydrophos biosynthesis , 2-aminoethylphosphonate biosynthesis , rhizocticin A and B biosynthesis , fosfomycin biosynthesis

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 Inferred by computational analysis [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.

Citations: [Nakashita97, Seidel94, Zhang03c]

Gene-Reaction Schematic: ?

Gene-Reaction Schematic

Unification Links: KEGG:R04053 , Rhea:20768

Relationship Links: BRENDA:EC:4.1.1.82 , ENZYME:EC:4.1.1.82 , IUBMB-ExplorEnz:EC:4.1.1.82


References

Latendresse13: Latendresse M. (2013). "Computing Gibbs Free Energy of Compounds and Reactions in MetaCyc."

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

Zhang03c: Zhang G, Dai J, Lu Z, Dunaway-Mariano D (2003). "The phosphonopyruvate decarboxylase from Bacteroides fragilis." J Biol Chem 278(42);41302-8. PMID: 12904299


Report Errors or Provide Feedback
Please cite the following article in publications resulting from the use of MetaCyc: Caspi et al, Nucleic Acids Research 42:D459-D471 2014
Page generated by SRI International Pathway Tools version 19.0 on Tue Jun 30, 2015, BIOCYC14A.