EC 3.11.1.3 - Phosphonopyruvate hydrolase

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IntEnz Enzyme Nomenclature
EC 3.11.1.3

Names

Accepted name:
phosphonopyruvate hydrolase
Other name:
PPH
Systematic name:
-

Reaction

Cofactor

Comments:

Highly specific for phosphonopyruvate as substrate [2]. The reaction is not inhibited by phosphate but is inhibited by the phosphonates phosphonoformic acid, hydroxymethylphosphonic acid and 3-phosphonopropanoic acid [2]. The enzyme is activated by the divalent cations Co2+, Mg2+ and Mn2+. This enzyme is a member of the phosphoenolpyruvate mutase/isocitrate lyase superfamily [3].

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Structural data: CSA , EC2PDB
Gene Ontology: GO:0033978
UniProtKB/Swiss-Prot:

References

  1. Ternan, N.G., Hamilton, J.T.G. and Quinn, J.P.
    Initial in vitro characterisation of phosphonopyruvate hydrolase, a novel phosphate starvation-independent, carbon-phosphorus bond cleavage enzyme in Burkholderia cepacia Pal6.
    Arch. Microbiol. 173 : 35-41 (2000). [PMID: 10648102]
  2. Kulakova, A.N., Wisdom, G.B., Kulakov, L.A. and Quinn, J.P.
    The purification and characterization of phosphonopyruvate hydrolase, a novel carbon-phosphorus bond cleavage enzyme from Variovorax sp Pal2.
    J. Biol. Chem. 278 : 23426-23431 (2003). [PMID: 12697754]
  3. Chen, C.C.H., Han, Y., Niu, W., Kulakova, A.N., Howard, A., Quinn, J.P., Dunaway-Mariano, D. and Herzberg, O.
    Structure and kinetics of phosphonopyruvate hydrolase from Variovorax sp. Pal2: new insight into the divergence of catalysis within the PEP mutase/isocitrate lyase superfamily.
    Biochemistry 45 : 11491-11504 (2006). [PMID: 16981709]

[EC 3.11.1.3 created 2007]