The Enzyme Database

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EC 3.5.1.84     
Accepted name: biuret amidohydrolase
Reaction: biuret + H2O = urea-1-carboxylate + NH3
Glossary: biuret = imidodicarbonic diamide
allophanate = urea-1-carboxylate
Other name(s): biuH (gene name)
Systematic name: biuret amidohydrolase
Comments: The enzyme, characterized from the bacterium Rhizobium leguminosarum bv. viciae 3841, participates in the degradation of cyanuric acid, 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 EC 3.5.1.131, 1-carboxybiuret hydrolase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, UM-BBD, CAS registry number: 95567-88-7
References:
1.  Cameron, S.M., Durchschein, K., Richman, J.E., Sadowsky, M.J. and Wackett, L.P. A new family of biuret hydrolases involved in s-triazine ring metabolism. ACS Catal. 2011 (2011) 1075–1082. [PMID: 21897878]
2.  Esquirol, L., Peat, T.S., Wilding, M., Lucent, D., French, N.G., Hartley, C.J., Newman, J. and Scott, C. Structural and biochemical characterization of the biuret hydrolase (BiuH) from the cyanuric acid catabolism pathway of Rhizobium leguminosarum bv. viciae 3841. PLoS One 13:e0192736 (2018). [PMID: 29425231]
3.  Esquirol, L., Peat, T.S., Wilding, M., Liu, J.W., French, N.G., Hartley, C.J., Onagi, H., Nebl, T., Easton, C.J., Newman, J. and Scott, C. An unexpected vestigial protein complex reveals the evolutionary origins of an s-triazine catabolic enzyme. J. Biol. Chem. 293 (2018) 7880–7891. [PMID: 29523689]
[EC 3.5.1.84 created 2000, modified 2008, modified 2019]
 
 


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