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
ec00791  Atrazine degradation
ec01100  Metabolic pathways
ec01120  Microbial metabolism in diverse environments
Orthology
K19837  biuret amidohydrolase
Genes
HNA: Hneap_0846
BUO: BRPE64_CCDS07460
BCAI: K788_0005134
PHS: C2L64_35110
PTER: C2L65_31040
BAV: BAV2584
BHO: D560_0088
BHM: D558_0086
BHZ: ACR54_01203(atzE_1)
BGM: CAL15_12200
AXX: ERS451415_04465(gatA_6)
HYB: Q5W_18935
MPT: Mpe_A0772
LCH: Lcho_3028
THI: THI_3642
BJA: blr1041
BRA: BRADO6818
BBT: BBta_0721
BRS: S23_67650
AOL: S58_06460
RPA: RPA1469(gatA1)
RPB: RPB_4054
RPT: Rpal_1654
XAU: Xaut_4656
AZC: AZC_1515
SNO: Snov_0644
MEX: Mext_1693
MDI: METDI2366
MCH: Mchl_2012
MPO: Mpop_1125
MET: M446_2141
MOR: MOC_0819
META: Y590_08125
MAQU: Maq22A_1p30080(gatA)
HDI: HDIA_3392(atzE)
RBM: TEF_15430
CCR: CC_2613
CAK: Caul_3713
CSE: Cseg_1082
AZL: AZL_a09080(gatA)
AFR: AFE_0782
ACU: Atc_m027
 » 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 231:25-30 (1985)
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 71:4437-45 (2005)
DOI:10.1128/AEM.71.8.4437-4445.2005
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 187:3731-8 (2005)
DOI:10.1128/JB.187.11.3731-3738.2005
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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