EC 3.5.1.84 - Biuret amidohydrolase

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IntEnz Enzyme Nomenclature
EC 3.5.1.84

Names

Accepted name:
biuret amidohydrolase
Systematic name:
biuret amidohydrolase

Reaction

Comments:

Along with EC 3.5.2.15 (cyanuric acid amidohydrolase) and EC 3.5.1.54 (allophanate hydrolase), 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. Urea-1-carboxylate rather than urea (as was thought previously) is the 2-nitrogen intermediate in cyanuric-acid metabolism in bacteria [2]. The product, urea-1-carboxylate, can spontaneously decarboxylate under acidic conditions to form urea but, under physiological conditions, it can be converted into CO2 and ammonia by the action of EC 3.5.1.54 [2].

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:0018750
UniProtKB/Swiss-Prot:

References

  1. Cook, A.M., Beilstein, P., Grossenbacher, H. and Hutter, R.
    Ring cleavage and degradative pathway of cyanuric acid in bacteria.
    Biochem. J. 231: 25-30 (1985). [PMID: 3904735]
  2. 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]
  3. 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]

[EC 3.5.1.84 created 2000, modified 2008]