biuret amidohydrolase

Hydrolases;
Acting on carbon-nitrogen bonds, other than peptide bonds;
In linear amides

biuret amidohydrolase

biuret + H2O = urea-1-carboxylate + NH3 [RN:R05563]

R05563;
(other) R05562

biuret [CPD:C06555];
H2O [CPD:C00001]

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].

1  [PMID:3904735]

Cook AM, Beilstein P, Grossenbacher H, Hutter R.

Ring cleavage and degradative pathway of cyanuric acid in bacteria.

Biochem. J. 231 (1985) 25-30.

Pseudomonas sp.

2  [PMID:16085834]

Cheng G, Shapir N, Sadowsky MJ, Wackett LP.

Allophanate hydrolase, not urease, functions in bacterial cyanuric acid metabolism.

Appl. Environ. Microbiol. 71 (2005) 4437-45.

3  [PMID:15901697]

Shapir N, Sadowsky MJ, Wackett LP.

Purification and characterization of allophanate hydrolase (AtzF) from Pseudomonas sp. strain ADP.

J. Bacteriol. 187 (2005) 3731-8.