EC 3.11.1.1 - Phosphonoacetaldehyde hydrolase

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IntEnz Enzyme Nomenclature
EC 3.11.1.1

Names

Accepted name:
phosphonoacetaldehyde hydrolase
Other names:
2-phosphonoacetylaldehyde phosphonohydrolase
phosphonatase
phosphonoacetylaldehyde phosphonohydrolase
Systematic name:
2-oxoethylphosphonate phosphonohydrolase

Reaction

Cofactor

Comments:

This enzyme destabilizes the C-P bond, by forming an imine between one of its lysine residues and the carbonyl group of the substrate, thus allowing this, normally stable, bond to be broken. The mechanism is similar to that used by EC 4.1.2.13, fructose-bisphosphate aldolase, to break a C-C bond.

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Structural data: CSA , EC2PDB
Gene Ontology: GO:0050194
CAS Registry Number: 37289-42-2
UniProtKB/Swiss-Prot: (67) [show] [UniProt]

References

  1. La Nauze, J.M. and Rosenberg, H.
    The identification of 2-phosphonoacetaldehyde as an intermediate in the degradation of 2-aminoethylphosphonate by Bacillus cereus.
    Biochim. Biophys. Acta 165: 438-447 (1968). [PMID: 4982500]
  2. La Nauze, J.M., Rosenberg, H. and Shaw, D.C.
    The enzymic cleavage of the carbon-phosphorus bond: purification and properties of phosphonatase.
    Biochim. Biophys. Acta 212: 332-350 (1970). [PMID: 4989158]
  3. La Nauze, J.M., Coggins, J.R. and Dixon, H.B.F.
    Aldolase-like imine formation in the mechanism of action of phosphonoacetaldehyde hydrolase.
    Biochem. J. 165: 409-411 (1977). [PMID: 200222]
  4. Olsen, D.B., Hepburn, T.W., Moos, M., Mariano, P.S. and Dunaway-Mariano, D.
    Substrate binding and catalytic groups of the P-C bond cleaving enzyme, phosphonoacetaldehyde hydrolase.
    Biochemistry 27: 2229-2234 (1988). [PMID: 3132206]
  5. Baker, A.S., Ciocci, M.J., Metcalf, W.W., Kim, J., Babbitt, P.C., Wanner, B.L., Martin, B.M. and Dunaway-Mariano, D.
    Insights into the mechanism of catalysis by the P-C bond-cleaving enzyme phosphonoacetaldehyde hydrolase derived from gene sequence analysis and mutagenesis.
    Biochemistry 37: 9305-9315 (1998). [PMID: 9649311]

[EC 3.11.1.1 created 1972, modified 1976, modified 2001]