EC 3.5.2.15 - Cyanuric acid amidohydrolase

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IntEnz Enzyme Nomenclature
EC 3.5.2.15

Names

Accepted name:
cyanuric acid amidohydrolase
Other name:
AtzD
Systematic name:
cyanuric acid amidohydrolase

Reaction

Comments:

Along with EC 3.5.1.54 (allophanate hydrolase) 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. This is a key enzyme in the pathway, catalysing the ring cleavage of cyanuric acid. The enzyme is specific for cyanuric acid as substrate as neither the structurally related compounds ammeline (2,4-diamino-6-hydroxy-s-triazine) and ammelide (2-amino-4,6-dihydroxy-s-triazine) nor a number of pyrimidine compounds, such as uracil and cytosine, can act as substrates [3].

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:0018753
CAS Registry Number: 100785-00-0
UniProtKB/Swiss-Prot: (14) [show] [UniProt]

References

  1. Eaton, R.W. and Karns, J.S.
    Cloning and comparison of the DNA encoding ammelide aminohydrolase and cyanuric acid amidohydrolase from three s-triazine-degrading bacterial strains.
    J. Bacteriol. 173: 1363-1366 (1991). [PMID: 1991731]
  2. Eaton, R.W. and Karns, J.S.
    Cloning and analysis of s-triazine catabolic genes from Pseudomonas sp. strain NRRLB-12227.
    J. Bacteriol. 173: 1215-1222 (1991). [PMID: 1846859]
  3. Karns, J.S.
    Gene sequence and properties of an s-triazine ring-cleavage enzyme from Pseudomonas sp. strain NRRLB-12227.
    Appl. Environ. Microbiol. 65: 3512-3517 (1999). [PMID: 10427042]
  4. Fruchey, I., Shapir, N., Sadowsky, M.J. and Wackett, L.P.
    On the origins of cyanuric acid hydrolase: purification, substrates, and prevalence of AtzD from Pseudomonas sp. strain ADP.
    Appl. Environ. Microbiol. 69: 3653-3657 (2003). [PMID: 12788776]

[EC 3.5.2.15 created 2000, modified 2008]