KEGG   ENZYME: 4.1.1.82Help
Entry
EC 4.1.1.82                 Enzyme                                 

Name
phosphonopyruvate decarboxylase;
3-phosphonopyruvate carboxy-lyase
Class
Lyases;
Carbon-carbon lyases;
Carboxy-lyases
BRITE hierarchy
Sysname
3-phosphonopyruvate carboxy-lyase (2-phosphonoacetaldehyde-forming)
Reaction(IUBMB)
3-phosphonopyruvate = 2-phosphonoacetaldehyde + CO2 [RN:R04053]
Reaction(KEGG)
Substrate
3-phosphonopyruvate [CPD:C02798]
Product
2-phosphonoacetaldehyde [CPD:C03167];
CO2 [CPD:C00011]
Comment
The enzyme catalyses a step in the biosynthetic pathway of 2-aminoethylphosphonate, a component of the capsular polysaccharide complex of Bacteroides fragilis. Requires thiamine diphosphate and Mg2+ as cofactors. The enzyme is activated by the divalent cations Mg2+, Ca2+ and Mn2+. Pyruvate and sulfopyruvate can also act as substrates, but more slowly. This enzyme drives the reaction catalysed by EC 5.4.2.9, phosphoenolpyruvate mutase, in the thermodynamically unfavourable direction of 3-phosphonopyruvate formation [2]. It is the initial step in all of the major biosynthetic pathways of phosphonate natural products [3].
History
EC 4.1.1.82 created 2005
Pathway
ec00440  Phosphonate and phosphinate metabolism
ec01100  Metabolic pathways
ec01120  Microbial metabolism in diverse environments
ec01130  Biosynthesis of antibiotics
Orthology
K09459  phosphonopyruvate decarboxylase
Genes
ZNE: 110841498
FCD: 110847575
LGI: LOTGIDRAFT_114966
CRG: 105334993
MYI: 110448928
OBI: 106874397 106879477
LAK: 106157387 106176585
NVE: NEMVE_v1g168076
EPA: 110243717
ADF: 107333309
HMG: 100197891
SMIN: v1.2.019412.t1(symbB.v1.2.019412.t1)
HDE: HDEF_0202
SRL: SOD_c30100(bcpC)
ECA: ECA0488(fom2)
PATR: EV46_02525
PATO: GZ59_05040(fom2)
PCT: PC1_0477
PEC: W5S_0591
PLF: PANA5342_2584(ppd)
PAJ: PAJ_2521
XVA: C7V42_03525(aepY)
SDN: Sden_1162
NOC: Noc_1316
NHL: Nhal_1305
NWA: Nwat_1198
NTT: TAO_1302
SALN: SALB1_2155
RME: Rmet_1809(ppd)
BMA: BMAA1769(ppd)
BMV: BMASAVP1_0759(ppd)
BMAL: DM55_4013(aepY)
BMAQ: DM76_4709(aepY)
BMAI: DM57_07160
BMAF: DM51_3462(aepY)
BMAZ: BM44_3973(aepY)
BMAB: BM45_4750(aepY)
BPD: BURPS668_A0779(aepY_2) BURPS668_A0909(aepY_1)
BPSE: BDL_3734(aepY) BDL_3836(aepY)
BPSM: BBQ_5586(aepY) BBQ_5688(aepY)
BPSU: BBN_3908(aepY) BBN_4008(aepY)
BPSD: BBX_5571(aepY) BBX_5673(aepY)
BPK: BBK_3882(aepY) BBK_5713(aepY)
BPSH: DR55_4743(aepY) DR55_4844(aepY)
BPSA: BBU_5437(aepY) BBU_5539(aepY)
BPSO: X996_3789(aepY) X996_4594(aepY)
BUT: X994_4010(aepY) X994_4112(aepY)
BTQ: BTQ_5191(aepY)
BTJ: BTJ_3821(aepY)
BTZ: BTL_4577(aepY) BTL_4677(aepY)
BTD: BTI_5337(aepY)
BTV: BTHA_5552(aepY)
BTHE: BTN_4316(aepY)
BTHM: BTRA_4581(aepY)
BTHL: BG87_4648(aepY)
BOK: DM82_4610(aepY) DM82_4704(aepY)
BOC: BG90_5889(aepY) BG90_5981(aepY)
BVE: AK36_4233(aepY)
BCN: Bcen_4246
BCJ: BCAM1244
BCEN: DM39_3754(aepY)
BCEW: DM40_4162(aepY)
BCEO: I35_5093
BAM: Bamb_3534
BMU: Bmul_4472
BMK: DM80_3633(aepY)
BMUL: NP80_4147(aepY)
BCT: GEM_4496
BCED: DM42_3847(aepY)
BDL: AK34_4231(aepY)
BCON: NL30_06375
BUB: BW23_4918(aepY)
BLAT: WK25_23145
BTEI: WS51_03915
BSEM: WJ12_26080
BPSL: WS57_07795
BMEC: WJ16_24705
BSTG: WT74_25010
BGU: KS03_4594(aepY)
BGO: BM43_5002(aepY)
BUK: MYA_4543
BUL: BW21_5017(aepY)
BXE: Bxe_B2234
BXB: DR64_4565(aepY)
BPH: Bphy_3821
BFN: OI25_4535(aepY)
PARB: CJU94_32425(aepY)
PHS: C2L64_30755(aepY)
PTER: C2L65_27415(aepY)
PGP: CUJ91_19560(aepY)
PPNO: DA70_09040
PPNM: LV28_21765
PPUL: RO07_16155
PSPU: NA29_20995
PAPI: SG18_00145
AAA: Acav_2123
AZO: azo2699
AOA: dqs_2834
HCP: HCN_1059
CHYO: CHH_1592
CHW: A2J15_004810(aepY)
DAL: Dalk_1322
BSTO: C0V70_16035(aepY)
ARA: Arad_7868
AVI: Avi_3414
AOL: S58_09490
ROS: CTJ15_07645(aepY)
BSS: BSUW23_00985(rhiE) BSUW23_00990(rhiF)
BMQ: BMQ_0785(aepY)
BMD: BMD_0786(aepY)
BMH: BMWSH_4463(ppd)
BMEG: BG04_3079(aepY)
PPOL: X809_41425
PLV: ERIC2_c18350(bcpC)
CTC: CTC_01699
CBE: Cbei_4337
CBZ: Cbs_4337
CBEI: LF65_04861
CSR: Cspa_c46180(bcpC)
CSB: CLSA_c08740(bcpC)
RCH: RUM_11410
NTP: CRH09_19450(aepY)
ROP: ROP_30760
SCO: SCO6824(SC1A2.33c)
SALS: SLNWT_3224
FAL: FRAAL6378
AMYC: CU254_05885(aepY)
ALL: CRK57522
SNA: Snas_5664
OLS: Olsu_0592
OTE: Oter_2977
TDE: TDE1414
TAZ: TREAZ_2215(aepY)
TPI: TREPR_2365(aepY)
BIP: Bint_1238
FSC: FSU_1438
BTH: BT_1719
BTHO: Btheta7330_01296(ilvB)
BFS: BF9343_1815(aepY)
PARC: CI960_12855(aepY)
PROC: Ptc2401_00815(ilvB_1)
NDE: NIDE0732(comD) NIDE2902(ppd)
NMV: NITMOv2_0601(comD)
NIO: NITINOP_0317(comD)
NJA: NSJP_1713(comD)
NCT: NMSP_0155(comD)
 » show all
Taxonomy
Reference
1  [PMID:12904299]
  Authors
Zhang G, Dai J, Lu Z, Dunaway-Mariano D.
  Title
The phosphonopyruvate decarboxylase from Bacteroides fragilis.
  Journal
J Biol Chem 278:41302-8 (2003)
DOI:10.1074/jbc.M305976200
Reference
2  [PMID:8180189]
  Authors
Seidel HM, Knowles JR.
  Title
Interaction of inhibitors with phosphoenolpyruvate mutase: implications for the reaction mechanism and the nature of the active site.
  Journal
Biochemistry 33:5641-6 (1994)
Reference
3  [PMID:9127192]
  Authors
Nakashita H, Watanabe K, Hara O, Hidaka T, Seto H.
  Title
Studies on the biosynthesis of bialaphos. Biochemical mechanism of C-P bond formation: discovery of phosphonopyruvate decarboxylase which catalyzes the formation of phosphonoacetaldehyde from phosphonopyruvate.
  Journal
J Antibiot (Tokyo) 50:212-9 (1997)
Other DBs
ExplorEnz - The Enzyme Database: 4.1.1.82
IUBMB Enzyme Nomenclature: 4.1.1.82
ExPASy - ENZYME nomenclature database: 4.1.1.82
BRENDA, the Enzyme Database: 4.1.1.82
CAS: 151662-34-9

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