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].
Pathway PATH: ec00791  Atrazine degradation
PATH: ec01100  Metabolic pathways
Reference
  Authors
  Title
  Journal
  Organism
 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.
Reference
  Authors
  Title

  Journal
 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.
Reference
  Authors
  Title

  Journal
 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.
Other DBs ExplorEnz - The Enzyme Database: 3.5.1.84
IUBMB Enzyme Nomenclature: 3.5.1.84
ExPASy - ENZYME nomenclature database: 3.5.1.84
UM-BBD (Biocatalysis/Biodegradation Database): 3.5.1.84
BRENDA, the Enzyme Database: 3.5.1.84
CAS: 95567-88-7
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