| Entry |
|
|---|
| Name |
allophanate hydrolase;
allophanate lyase;
AtzF;
TrzF |
|---|
| Class |
Hydrolases;
Acting on carbon-nitrogen bonds, other than peptide bonds;
In linear amides
 |
|---|
| Sysname |
urea-1-carboxylate amidohydrolase |
|---|
| Reaction(IUBMB) |
urea-1-carboxylate + H2O = 2 CO2 + 2 NH3 [RN:R00005] |
|---|
| Reaction(KEGG) |
R00005
 |
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| Substrate |
urea-1-carboxylate [CPD:C01010];
H2O [CPD:C00001] |
|---|
| Product |
CO2 [CPD:C00011];
NH3 [CPD:C00014] |
|---|
| Comment |
Along with EC 3.5.2.15 (cyanuric acid amidohydrolase) and EC
3.5.1.84 (biuret amidohydrolase), 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. The yeast enzyme (but not that from green algae) also
catalyses the reaction of EC 6.3.4.6, urea carboxylase, thus
bringing about the hydrolysis of urea to CO2 and NH3 in the presence
of ATP and bicarbonate. The enzyme from Pseudomonas sp. strain ADP
has a narrow substrate specificity, being unable to use the
structurally analogous compounds urea, hydroxyurea or
methylcarbamate as substrate [6]. |
|---|
| Pathway |
PATH: ec00330 Arginine and proline metabolism
PATH: ec00791 Atrazine degradation
PATH: ec01100 Metabolic pathways |
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| Orthology |
KO: K01457 allophanate hydrolase |
|---|
| Genes |
SCE: YBR208C(DUR1)
AGO: AGOS_ADR051C
KLA: KLLA0E08107g
DHA: DEHA0D07777g
PIC: PICST_28452(DUR1)
VPO: Kpol_299p2
CAL: CaO19.780(DUR1)
CGR: CAGL0M05533g
YLI: YALI0E07271g
MGR: MGG_04386
FGR: FG10913.1
ECA: ECA1917
HSO: HS_0025 HS_0026
PSB: Psyr_2720
PEN: PSEEN4016
ACI: ACIAD2518
ACB: A1S_1269
ABM: ABSDF2256
ABY: ABAYE2439
PHA: PSHAa1442
PIN: Ping_3549
TCX: Tcr_1792
AEH: Mlg_1917
ABO: ABO_1892(uahA)
CVI: CV_3170
RSO: RSc2170
RPI: Rpic_2373
RPF: Rpic12D_1973
REU: Reut_A0088 Reut_A2450
REH: H16_A0125 H16_B1758(alpH)
RME: Rmet_0063
CTI: RALTA_A0067
BMA: BMA3310
BMV: BMASAVP1_A2980
BML: BMA10229_A2112
BMN: BMA10247_3368
BPS: BPSL0258
BPM: BURPS1710b_0448
BPL: BURPS1106A_0265
BPD: BURPS668_0253
BPR: GBP346_A0168
BTE: BTH_I0229
BVI: Bcep1808_3123 Bcep1808_3855
BUR: Bcep18194_A6284 Bcep18194_A6385
BCN: Bcen_2424
BCH: Bcen2424_3038
BCM: Bcenmc03_3057
BCJ: BCAL0551
BAM: Bamb_3083
BAC: BamMC406_2949
BMU: Bmul_3033
BMJ: BMULJ_00199
BXE: Bxe_A0194
BPH: Bphy_2904
BPY: Bphyt_3742
BGL: bglu_1g33280
RFR: Rfer_0126
VAP: Vapar_4366
NET: Neut_2470
AZO: azo0044
RET: RHE_PC00188(yhc00046) RHE_PE00118(ype00056)
RLE: RL2460 pRL100433
RPE: RPE_3038
RSP: RSP_3449
JAN: Jann_2804
RDE: RD1_0244
HNE: HNE_2123 HNE_2124
GBE: GbCGDNIH1_1744
RRU: Rru_A1505
SAJ: SaurJH9_1665
SAH: SaurJH1_1699
LME: LEUM_0989
MSM: MSMEG_2187 MSMEG_2189(atzF)
MMC: Mmcs_1840
MKM: Mkms_1887
MJL: Mjls_1821
RHA: RHA1_ro06922
CMI: CMM_0564
AAU: AAur_0053 AAur_0186(atzF)
TFU: Tfu_1968
FRA: Francci3_2975
SEN: SACE_1551(alpH) SACE_1552
SUS: Acid_0062
GFO: GFO_2121 GFO_2122
TTH: TTC0624
 |
|---|
Reference
Authors
Title
Journal
|
1
Maitz, G.S., Haas, E.M. and Castric, P.A.
Purification and properties of the allophanate hydrolase from
Chlamydomonas reinhardii.
Biochim. Biophys. Acta 714 (1982) 486-491. |
|---|
Reference
Authors
Title
Journal
Organism
|
2 [PMID:4556303]
Roon RJ, Levenberg B.
Urea amidolyase. I. Properties of the enzyme from Candida utilis.
J. Biol. Chem. 247 (1972) 4107-13.
Candida utilis |
|---|
Reference
Authors
Title
Journal
Organism
|
3 [PMID:6124544]
Sumrada RA, Cooper TG.
Urea carboxylase and allophanate hydrolase are components of a
multifunctional protein in yeast.
J. Biol. Chem. 257 (1982) 9119-27.
Saccharomyces cerevisiae [GN:sce] |
|---|
Reference
Authors
Title
Journal
Organism
|
4 [PMID:15796980]
Kanamori T, Kanou N, Kusakabe S, Atomi H, Imanaka T.
Allophanate hydrolase of Oleomonas sagaranensis involved in an
ATP-dependent degradation pathway specific to urea.
FEMS. Microbiol. Lett. 245 (2005) 61-5.
Oleomonas sagaranensis |
|---|
Reference
Authors
Title
Journal
Organism
|
5 [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.
Enterobacter cloacae, Pseudomonas huttiensis, Pseudomonas sp. |
|---|
Reference
Authors
Title
Journal
Organism
|
6 [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.
Pseudomonas sp. |
|---|
Reference
Authors
Title
Journal
Organism
|
7 [PMID:16597948]
Shapir N, Cheng G, Sadowsky MJ, Wackett LP.
Purification and characterization of TrzF: biuret hydrolysis by
allophanate hydrolase supports growth.
Appl. Environ. Microbiol. 72 (2006) 2491-5.
Enterobacter cloacae |
|---|
| Other DBs |
ExplorEnz - The Enzyme Database: 3.5.1.54
IUBMB Enzyme Nomenclature: 3.5.1.54
ExPASy - ENZYME nomenclature database: 3.5.1.54
UM-BBD (Biocatalysis/Biodegradation Database): 3.5.1.54
BRENDA, the Enzyme Database: 3.5.1.54
CAS: 9076-72-6 |
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