KEGG   ENZYME: 3.11.1.1Help
Entry
EC 3.11.1.1                 Enzyme                                 

Name
phosphonoacetaldehyde hydrolase;
phosphonatase;
2-phosphonoacetylaldehyde phosphonohydrolase
Class
Hydrolases;
Acting on carbon-phosphorus bonds;
Acting on carbon-phosphorus bonds (only sub-subclass identified to date)
BRITE hierarchy
Sysname
2-oxoethylphosphonate phosphonohydrolase
Reaction(IUBMB)
phosphonoacetaldehyde + H2O = acetaldehyde + phosphate [RN:R00747]
Reaction(KEGG)
Substrate
phosphonoacetaldehyde [CPD:C03167];
H2O [CPD:C00001]
Product
acetaldehyde [CPD:C00084];
phosphate [CPD:C00009]
Comment
This enzyme destabilizes the C-P bond, by forming an imine between one of its lysine residues and the carbonyl group of the substrate, thus allowing this, normally stable, bond to be broken. The mechanism is similar to that used by EC 4.1.2.13, fructose-bisphosphate aldolase, to break a C-C bond. Belongs to the haloacetate dehalogenase family.
History
EC 3.11.1.1 created 1972, modified 1976, modified 2001
Pathway
Phosphonate and phosphinate metabolism
Metabolic pathways
Microbial metabolism in diverse environments
Orthology
K05306  
phosphonoacetaldehyde hydrolase
Genes
BFO: 
CIN: 
LGI: 
NVE: 
HMG: 
STY: 
STY0471(phnX)
STT: 
t2431(phnX)
SEX: 
SENT: 
STM: 
STM0432(phnX)
SEO: 
SEV: 
SEY: 
SEM: 
SEJ: 
SEB: 
SEF: 
SETU: 
SETC: 
SEEN: 
SENR: 
SEND: 
SPT: 
SPA2291(phnX)
SEK: 
SPQ: 
SEI: 
SPC_0444(phnX)
SEC: 
SC0473(phnX)
SEH: 
SHB: 
SENH: 
SEEH: 
SEE: 
SENN: 
SEW: 
SEA: 
SENS: 
SED: 
SEG: 
SG0443(phnX)
SEL: 
SPUL_2535(phnX)
SEGA: 
SET: 
SEN0414(phnX)
SENJ: 
SEEC: 
SEEB: 
SEEP: 
SENB: 
BN855_4290(SBOV03851)
SENE: 
ESC: 
EAS: 
EAE: 
EAR: 
KPN: 
KPN_04064(phnX)
KPU: 
KP1_5437(phnX)
KPM: 
KPP: 
KPO: 
KPR: 
KPR_0042(phnX)
KPJ: 
KPI: 
KPA: 
KPS: 
KOX: 
KOE: 
KOY: 
KOK: 
SMAF: 
SMW: 
SLQ: 
SERF: 
SERS: 
PMR: 
PMI3079(phnX)
PMIB: 
ETE: 
ETEE_2729(phnX)
PSI: 
PSX: 
ROR: 
PGE: 
VCH: 
VCE: 
VCJ: 
VCO: 
VCR: 
VCM: 
VCI: 
VCL: 
VVU: 
VV2_1662(phnX)
VVY: 
VVM: 
VVL: 
VPA: 
VPB: 
VPK: 
VPF: 
VPH: 
VHA: 
VCA: 
VAG: 
VSP: 
VEX: 
VEJ: 
VFU: 
VSA: 
PAE: 
PA1311(phnX)
PAEV: 
N297_1351(phnX)
PAEI: 
N296_1351(phnX)
PAU: 
PAP: 
PAG: 
PAF: 
PNC: 
PDK: 
PSG: 
PRP: 
PAEP: 
PAER: 
PAEM: 
PAEL: 
PAES: 
PAEU: 
PAEG: 
PAEC: 
M802_1348(phnX)
PAEO: 
M801_1350(phnX)
PPU: 
PP_2208(phnX)
PPF: 
PPG: 
PPW: 
PPT: 
PPB: 
PPI: 
PPX: 
T1E_0555(phnX)
PPUH: 
PPUT: 
PPUN: 
PP4_32670(phnX) PP4_36070(phnX)
PMOS: 
PPUU: 
PFL: 
PFL_3966(phnX)
PPRC: 
PFO: 
PFS: 
PFC: 
PPZ: 
PEN: 
PSEEN3554(phnX)
PBA: 
PDR: 
PRE: 
PSV: 
PSK: 
PMON: 
PMOT: 
PKC: 
PKB_3136(phnX)
PCH: 
PALK: 
ACD: 
ACB: 
ABY: 
ABAYE2317(phnX)
ABC: 
ABN: 
AB57_1573(phnX)
ABB: 
ABX: 
ABZ: 
ABR: 
ABD: 
ABH: 
ABJ: 
ABAB: 
ABAJ: 
ABAZ: 
ACC: 
MHC: 
MARHY1154(phnX)
MBS: 
PIN: 
PSY: 
HCH: 
HCH_03084(phnX)
HCS: 
AHA: 
AHA_1940(phnX)
AHY: 
AHD: 
AHR: 
AHP: 
AVR: 
OCE: 
RSN: 
RPI: 
RPF: 
BCEN: 
DM39_4565(phnX)
BXE: 
BXB: 
DR64_4272(phnX)
BPY: 
BGL: 
BUG: 
BGE: 
BGD: 
BPX: 
BPE: 
BPC: 
BPER: 
BPA: 
BBR: 
BBM: 
BBH: 
BAV: 
BAV1192(phnX)
BHO: 
AXY: 
AXO: 
AXN: 
DAC: 
DEL: 
CTT: 
CTES: 
HSE: 
RGE: 
RGE_31440(phnX)
SBA: 
SMUL: 
DVM: 
DGG: 
SFU: 
SNO: 
CAK: 
CSE: 
RCP: 
OAR: 
SSY: 
SLG_17040(phnX)
GXL: 
RPM: 
AZL: 
ALI: 
PGV: 
BAN: 
BA_1340(phnX)
BAR: 
GBAA_1340(phnX)
BAT: 
BAH: 
BAI: 
BAA_1407(phnX)
BAX: 
BANT: 
BANR: 
BANS: 
BAL: 
BCE: 
BCA: 
BCE_1439(phnX)
BCZ: 
BCZK1217(phnX)
BCR: 
BCB: 
BCU: 
BCG: 
BCQ: 
BCQ_1398(phnX)
BCX: 
BCA_1378(phnX)
BNC: 
BCF: 
BCER: 
BCY: 
BTK: 
BTL: 
BTB: 
BTT: 
BTC: 
BTF: 
BTM: 
BTG: 
BTI: 
BTN: 
BTHT: 
BTHU: 
BWE: 
BTY: 
BMQ: 
BMQ_3213(phnX)
BMD: 
BMD_3231(phnX)
LSP: 
Bsph_1361(phnX)
LGY: 
HHD: 
SCA: 
BBE: 
PJD: 
GYM: 
PPY: 
PPE_00475(phnX)
PPM: 
PPO: 
PPM_0474(phnX)
PPOL: 
PPQ: 
PMS: 
PMQ: 
PMW: 
PTA: 
LPL: 
lp_0711(phnX)
LPJ: 
JDM1_0587(phnX)
LPT: 
LPS: 
LPR: 
LPZ: 
LSA: 
LSA1665(phnX)
EFC: 
EFAU: 
EFU: 
EFM: 
EFT: 
EMU: 
CBL: 
CSO: 
ELM: 
EAC: 
BPRM: 
ELE: 
GMA: 
STR: 
PSL: 
PLM: 
PBS: 
IPA: 
SACI: 
BFR: 
BFS: 
BFG: 
BVU: 
BSA: 
BDO: 
BDH: 
PDI: 
OSP: 
RRS: 
RCA: 
CAP: 
 » show all
Taxonomy
Reference
1  [PMID:4982500]
  Authors
La Nauze JM, Rosenberg H.
  Title
The identification of 2-phosphonoacetaldehyde as an intermediate in the degradation of 2-aminoethylphosphonate by Bacillus cereus.
  Journal
Biochim. Biophys. Acta. 165 (1968) 438-47.
Reference
2  [PMID:4989158]
  Authors
La Nauze JM, Rosenberg H, Shaw DC.
  Title
The enzymic cleavage of the carbon-phosphorus bond: purification and properties of phosphonatase.
  Journal
Biochim. Biophys. Acta. 212 (1970) 332-50.
Reference
3  [PMID:200222]
  Authors
La Nauze JM, Coggins JR, Dixon HB.
  Title
Aldolase-like imine formation in the mechanism of action of phosphonoacetaldehyde hydrolase.
  Journal
Biochem. J. 165 (1977) 409-11.
Reference
4  [PMID:3132206]
  Authors
Olsen DB, Hepburn TW, Moos M, Mariano PS, Dunaway-Mariano D.
  Title
Investigation of the Bacillus cereus phosphonoacetaldehyde hydrolase. Evidence for a Schiff base mechanism and sequence analysis of an active-site peptide containing the catalytic lysine residue.
  Journal
Biochemistry. 27 (1988) 2229-34.
Reference
5  [PMID:9649311]
  Authors
Baker AS, Ciocci MJ, Metcalf WW, Kim J, Babbitt PC, Wanner BL, Martin BM, Dunaway-Mariano D.
  Title
Insights into the mechanism of catalysis by the P-C bond-cleaving enzyme phosphonoacetaldehyde hydrolase derived from gene sequence analysis and mutagenesis.
  Journal
Biochemistry. 37 (1998) 9305-15.
  Sequence
[stm:STM0432] [bal:BACI_c13600]
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
BRENDA, the Enzyme Database: 
CAS: 
37289-42-2

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