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
Phosphonate and phosphinate metabolism
Metabolic pathways
Microbial metabolism in diverse environments
Biosynthesis of antibiotics
Orthology
K09459  
phosphonopyruvate decarboxylase
Genes
LGI: 
CRG: 
OBI: 
NVE: 
ADF: 
HMG: 
TET: 
PTM: 
SMIN: 
v1.2.019412.t1(symbB.v1.2.019412.t1)
HDE: 
SRL: 
SRY: 
ECA: 
ECA0488(fom2)
PATR: 
PATO: 
PCT: 
PCC: 
PWA: 
PPAR: 
PEC: 
PLF: 
PAJ: 
PAQ: 
EIC: 
PPZ: 
SDN: 
NOC: 
NHL: 
NWA: 
RPJ: 
RME: 
CBW: 
BMA: 
BMV: 
BMAL: 
DM55_4013(aepY)
BMAQ: 
DM76_4709(aepY)
BMAI: 
BMAF: 
DM51_3462(aepY)
BMAZ: 
BM44_3973(aepY)
BMAB: 
BM45_4750(aepY)
BPS: 
BPM: 
BPL: 
BPD: 
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)
BPZ: 
BPQ: 
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)
BTE: 
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)
BTHA: 
BTHL: 
BG87_4648(aepY)
BOK: 
DM82_4610(aepY) DM82_4704(aepY)
BOC: 
BG90_5889(aepY) BG90_5981(aepY)
BVI: 
BVE: 
AK36_4233(aepY)
BUR: 
BCN: 
BCH: 
BCM: 
BCJ: 
BCEN: 
DM39_3754(aepY)
BCEW: 
DM40_4162(aepY)
BCEO: 
BAM: 
BAC: 
BMU: 
BMK: 
DM80_3633(aepY)
BMUL: 
NP80_4147(aepY)
BCT: 
BCED: 
DM42_3847(aepY)
BDL: 
AK34_4231(aepY)
BPYR: 
BCON: 
BGL: 
BGP: 
BGU: 
KS03_4594(aepY)
BUG: 
BGE: 
BGF: 
BGD: 
BGO: 
BM43_5002(aepY)
BYI: 
BUK: 
BUO: 
BUE: 
BUL: 
BW21_5017(aepY)
BUB: 
BW23_4918(aepY)
BUQ: 
BPLA: 
BUD: 
BXE: 
BXB: 
DR64_4565(aepY)
BPH: 
BPX: 
BPY: 
BFN: 
OI25_4535(aepY)
BCAI: 
PPK: 
PPNO: 
PPNM: 
PRB: 
PPUL: 
PSPU: 
PAPI: 
PVE: 
POX: 
PFG: 
PNR: 
AAA: 
AZO: 
SHD: 
MEU: 
HCP: 
HCB: 
ANT: 
DHY: 
DAK: 
DAL: 
SCU: 
LLU: 
DAO: 
ARA: 
AVI: 
REP: 
AOL: 
MAGX: 
BSS: 
BMQ: 
BMQ_0785(aepY)
BMD: 
BMD_0786(aepY)
BMH: 
BMEG: 
BG04_3079(aepY)
BACI: 
BLR: 
PPY: 
PPOL: 
PTA: 
PLV: 
PIH: 
PPEO: 
SNX: 
SPNE: 
SPNU: 
SPNM: 
SPNO: 
CTC: 
CTET: 
CBJ: 
CBE: 
CBZ: 
CSR: 
CSB: 
CBUT: 
RAL: 
RCH: 
CLE: 
HAS: 
SSG: 
SELE: 
MBJ: 
NBR: 
ROP: 
SCO: 
SCO6824(SC1A2.33c)
SDV: 
SALS: 
STRC: 
KSK: 
RTX: 
RTC: 
ARH: 
FAL: 
ALL: 
SNA: 
ARD: 
AYM: 
OLS: 
ARP: 
MPRO: 
OTE: 
TDE: 
TBE: 
TAZ: 
TPI: 
SCD: 
TPK: 
SSM: 
STA: 
SBU: 
SGP: 
TPX: 
BIP: 
FSU: 
FSC: 
BTH: 
BFR: 
BFS: 
BFG: 
BDO: 
PCM: 
PROC: 
NDE: 
NMV: 
NIO: 
TAR: 
ARG: 
 » 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 (2003) 41302-8.
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 (1994) 5641-6.
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 (1997) 212-9.
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
BRENDA, the Enzyme Database: 
CAS: 
151662-34-9

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