EC 4.1.1.82 - Phosphonopyruvate decarboxylase

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IntEnz Enzyme Nomenclature
EC 4.1.1.82

Names

Accepted name:
phosphonopyruvate decarboxylase
Other name:
3-phosphonopyruvate carboxy-lyase
Systematic name:
3-phosphonopyruvate carboxy-lyase (2-phosphonoacetaldehyde-forming)

Reaction

Cofactors

Comments:

The enzyme catalyses a step in the biosynthetic pathway of 2-aminoethylphosphonate, a component of the capsular polysaccharide complex of Bacteroides fragilis. Requires thiamine diphosphate and Mg2+ as cofactors. The enzyme is activated by the divalent cations Mg2+, Ca2+ and Mn2+. Pyruvate and sulfopyruvate can also act as substrates, but more slowly.

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , DIAGRAM , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Protein domains and families: PROSITE:PDOC00166
Structural data: CSA , EC2PDB
Gene Ontology: GO:0033980
UniProtKB/Swiss-Prot:

References

  1. Zhang, G., Dai, J., Lu, Z. and Dunaway-Mariano, D.
    The phosphonopyruvate decarboxylase from Bacteroides fragilis.
    J. Biol. Chem. 278: 41302-41308 (2003). [PMID: 12904299]
  2. Seidel, H.M. and Knowles, J.R.
    Interaction of inhibitors with phosphoenolpyruvate mutase: implications for the reaction mechanism and the nature of the active site.
    Biochemistry 33: 5641-5646 (1994). [PMID: 8180189]
  3. Nakashita, H., Watanabe, K., Hara, O., Hidaka, T. and 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. Antibiot. 50: 212-219 (1997). [PMID: 9127192]

[EC 4.1.1.82 created 2005]