KEGG   ENZYME: 3.5.1.84Help
Entry
EC 3.5.1.84                 Enzyme                                 

Name
biuret amidohydrolase
Class
Hydrolases;
Acting on carbon-nitrogen bonds, other than peptide bonds;
In linear amides
BRITE hierarchy
Sysname
biuret amidohydrolase
Reaction(IUBMB)
biuret + H2O = urea-1-carboxylate + NH3 [RN:R05563]
Reaction(KEGG)
R05563;
(other) R05562
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Substrate
biuret [CPD:C06555];
H2O [CPD:C00001]
Product
urea-1-carboxylate [CPD:C01010];
NH3 [CPD:C00014]
Comment
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].
History
EC 3.5.1.84 created 2000, modified 2008
Pathway
Atrazine degradation
Metabolic pathways
Microbial metabolism in diverse environments
Reference
1  [PMID:3904735]
  Authors
Cook AM, Beilstein P, Grossenbacher H, Hutter R.
  Title
Ring cleavage and degradative pathway of cyanuric acid in bacteria.
  Journal
Biochem. J. 231 (1985) 25-30.
  Organism
Pseudomonas sp.
Reference
2  [PMID:16085834]
  Authors
Cheng G, Shapir N, Sadowsky MJ, Wackett LP.
  Title
Allophanate hydrolase, not urease, functions in bacterial cyanuric acid metabolism.
  Journal
Appl. Environ. Microbiol. 71 (2005) 4437-45.
Reference
3  [PMID:15901697]
  Authors
Shapir N, Sadowsky MJ, Wackett LP.
  Title
Purification and characterization of allophanate hydrolase (AtzF) from Pseudomonas sp. strain ADP.
  Journal
J. Bacteriol. 187 (2005) 3731-8.
  Organism
Pseudomonas sp.
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
UM-BBD (Biocatalysis/Biodegradation Database): 
BRENDA, the Enzyme Database: 
CAS: 
95567-88-7

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