EC 3.5.1.54 - Allophanate hydrolase

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IntEnz Enzyme Nomenclature
EC 3.5.1.54

Names

Accepted name:
allophanate hydrolase
Other names:
allophanate lyase
AtzF
TrzF
Systematic name:
urea-1-carboxylate amidohydrolase

Reaction

Comments:

Along with EC 3.5.2.15 (cyanuric acid amidohydrolase) and EC 3.5.1.84 (biuret amidohydrolase), this enzyme forms part of the cyanuric-acid metabolism pathway, which degrades s-triazide herbicides, such as atrazine [2-chloro-4-(ethylamino)-6-(isopropylamino)-1,3,5-triazine], in bacteria. The yeast enzyme (but not that from green algae) also catalyses the reaction of EC 6.3.4.6 urea carboxylase, thus bringing about the hydrolysis of urea to CO2 and NH3 in the presence of ATP and bicarbonate. The enzyme from Pseudomonas sp. strain ADP has a narrow substrate specificity, being unable to use the structurally analogous compounds urea, hydroxyurea or methylcarbamate as substrate [6].

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UM-BBD , UniPathway
Structural data: CSA , EC2PDB
Gene Ontology: GO:0004039
CAS Registry Number: 79121-96-3
UniProtKB/Swiss-Prot:

References

  1. Maitz, G.S., Haas, E.M. and Castric, P.A.
    Purification and properties of the allophanate hydrolase from Chlamydomonas reinhardii.
    Biochim. Biophys. Acta 714: 486-491 (1982).
  2. Roon, R.J. and Levenberg, B.
    Urea amidolyase. I. Properties of the enzyme from Candida utilis.
    J. Biol. Chem. 247: 4107-4113 (1972). [PMID: 4556303]
  3. Sumrada, R.A. and Cooper, T.G.
    Urea carboxylase and allophanate hydrolase are components of a multifunctional protein in yeast.
    J. Biol. Chem. 257: 9119-9127 (1982). [PMID: 6124544]
  4. Kanamori, T., Kanou, N., Kusakabe, S., Atomi, H. and Imanaka, T.
    Allophanate hydrolase of Oleomonas sagaranensis involved in an ATP-dependent degradation pathway specific to urea.
    FEMS Microbiol. Lett. 245: 61-65 (2005). [PMID: 15796980]
  5. Cheng, G., Shapir, N., Sadowsky, M.J. and Wackett, L.P.
    Allophanate hydrolase, not urease, functions in bacterial cyanuric acid metabolism.
    Appl. Environ. Microbiol. 71: 4437-4445 (2005). [PMID: 16085834]
  6. Shapir, N., Sadowsky, M.J. and Wackett, L.P.
    Purification and characterization of allophanate hydrolase (AtzF) from Pseudomonas sp. strain ADP.
    J. Bacteriol. 187: 3731-3738 (2005). [PMID: 15901697]
  7. Shapir, N., Cheng, G., Sadowsky, M.J. and Wackett, L.P.
    Purification and characterization of TrzF: biuret hydrolysis by allophanate hydrolase supports growth.
    Appl. Environ. Microbiol. 72: 2491-2495 (2006). [PMID: 16597948]

[EC 3.5.1.54 created 1986, modified 2008]