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)
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
Orthology
K19837  
biuret amidohydrolase
Genes
YPE: 
YPK: 
YPA: 
YPN: 
YPM: 
YP_0671(gatA)
YPP: 
YPG: 
YPZ: 
YPT: 
YPD: 
YPX: 
YPH: 
YPW: 
YPJ: 
YPV: 
YPL: 
YPS: 
YPO: 
YPI: 
YPY: 
YPB: 
YPQ: 
YPU: 
YPR: 
YPC: 
YPF: 
YEP: 
YEY: 
YEL: 
YET: 
YEF: 
YEE: 
YSI: 
ECA: 
PATR: 
PATO: 
PCT: 
PCC: 
PCV: 
PWA: 
PEC: 
ETA: 
EPY: 
EPR: 
EAM: 
EAMY_0854(gatA)
EAY: 
EBI: 
ERJ: 
EGE: 
ENC: 
ENO: 
EEC: 
ENL: 
ECLG: 
ECLN: 
EAS: 
EAU: 
ENR: 
ENX: 
KPN: 
KPU: 
KPM: 
KPP: 
KPK: 
KPH: 
KPZ: 
KPV: 
KPW: 
KPY: 
KPG: 
KPC: 
KPQ: 
KPT: 
KPE: 
KPO: 
KPJ: 
KPI: 
KPA: 
KPS: 
KPX: 
KPB: 
KPNU: 
KVA: 
KVD: 
KVQ: 
KOX: 
KOE: 
KOY: 
KOK: 
KOM: 
KMI: 
EAE: 
EAR: 
SPE: 
SRR: 
SRL: 
SRY: 
SRS: 
SRA: 
SMAF: 
SLQ: 
SERR: 
SERS: 
DDA: 
DDD: 
DZE: 
DDC: 
DZC: 
PAM: 
PANA_0856(gatA)
PLF: 
PAJ: 
PAJ_0192(gatA)
PAQ: 
PVA: 
Pvag_0250(gata1)
PAO: 
KLN: 
PANT: 
PANP: 
HHS: 
HHS_08200(gatA)
PCK: 
PAGG: 
RAH: 
RAQ: 
RAA: 
ROR: 
RON: 
CNT: 
CEM: 
CEN: 
CED: 
PGE: 
KSA: 
KIN: 
ICP: 
SBW: 
PSTS: 
PSES: 
HNA: 
CBW: 
BGO: 
BUO: 
BCAI: 
BAV: 
BHO: 
BHM: 
BHZ: 
ACR54_01203(atzE_1)
AXO: 
AXN: 
AXS: 
ADT: 
AFA: 
MPT: 
LCH: 
THI: 
MEU: 
SHZ: 
BJA: 
BJU: 
BJP: 
BRA: 
BBT: 
BRS: 
AOL: 
BRC: 
RPA: 
RPA1469(gatA1)
RPB: 
RPT: 
RPX: 
BOP: 
XAU: 
AZC: 
SNO: 
MEX: 
MDI: 
MCH: 
MRD: 
MET: 
MPO: 
MOR: 
META: 
MAQU: 
HNI: 
RHZ: 
CCR: 
CCS: 
CAK: 
CSE: 
CHQ: 
LAP: 
NPP: 
AZL: 
PGV: 
AFE: 
AFR: 
ACU: 
AFI: 
LET: 
 » show all
Taxonomy
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.
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.
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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