EC - Biuret amidohydrolase

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IntEnz Enzyme Nomenclature


Accepted name:
biuret amidohydrolase
Systematic name:
biuret amidohydrolase



The enzyme, characterized from the bacterium Rhizobium leguminosarum bv. viciae 3841, participates in the degradation of cyanurate, an intermediate in the degradation of s-triazide herbicides such as atrazine [2-chloro-4-(ethylamino)-6-(isopropylamino)-1,3,5-triazine]. The substrate, biuret, forms by the spontaneous decarboxylation of 1-carboxybiuret in the absence of 1-carboxybiuret hydrolase.

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


  1. Cameron, S. M., Durchschein, K., Richman, J. E., Sadowsky, M. J., Wackett, L. P.
    A New Family of Biuret Hydrolases Involved in S-Triazine Ring Metabolism.
    ACS Catal 2011: 1075-1082 (2011). [PMID: 21897878]
  2. Esquirol, L., Peat, T. S., Wilding, M., Lucent, D., French, N. G., Hartley, C. J., Newman, J., Scott, C.
    Structural and biochemical characterization of the biuret hydrolase (BiuH) from the cyanuric acid catabolism pathway of Rhizobium leguminasorum bv. viciae 3841.
    PLoS ONE 13: e0192736 (2018). [PMID: 29425231]
  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: 29523689]

[EC created 2000, modified 2008, modified 2019]