| Entry |
|
|---|
| Name |
phosphonopyruvate decarboxylase;
3-phosphonopyruvate carboxy-lyase |
|---|
| Class |
Lyases;
Carbon-carbon lyases;
Carboxy-lyases
 |
|---|
| Sysname |
3-phosphonopyruvate carboxy-lyase (2-phosphonoacetaldehyde-forming) |
|---|
| Reaction(IUBMB) |
3-phosphonopyruvate = 2-phosphonoacetaldehyde + CO2 [RN:R04053] |
|---|
| Reaction(KEGG) |
R04053
 |
|---|
| 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]. |
|---|
| Pathway |
PATH: ec00440 Phosphonate and phosphinate metabolism
PATH: ec01100 Metabolic pathways |
|---|
| Orthology |
KO: K09459 phosphonopyruvate decarboxylase |
|---|
| Genes |
NVE: NEMVE_v1g168076
ECA: ECA0488(fom2)
PCT: PC1_0477
EIC: NT01EI_2702
BPS: BPSS0609
BPM: BURPS1710b_A2172(fom2)
BPL: BURPS1106A_A0817(ppd)
BPD: BURPS668_A0909(ppd)
AZO: azo2699
DAL: Dalk_1322
CBE: Cbei_4337
ROP: ROP_30760
TDE: TDE1414
BTH: BT_1719
BFR: BF1833 BF2577
BFS: BF1898(aepY)
 |
|---|
Reference
Authors
Title
Journal
Organism
|
1 [PMID:12904299]
Zhang G, Dai J, Lu Z, Dunaway-Mariano D.
The phosphonopyruvate decarboxylase from Bacteroides fragilis.
J. Biol. Chem. 278 (2003) 41302-8.
Bacteroides fragilis |
|---|
Reference
Authors
Title
Journal
Organism
|
2 [PMID:8180189]
Seidel HM, Knowles JR.
Interaction of inhibitors with phosphoenolpyruvate mutase:
implications for the reaction mechanism and the nature of the active
site.
Biochemistry. 33 (1994) 5641-6.
Tetrahymena pyriformis, Streptomyces hygroscopicus |
|---|
Reference
Authors
Title
Journal
Organism
|
3 [PMID:9127192]
Nakashita H, Watanabe K, Hara O, Hidaka T, Seto H.
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.
J. Antibiot. (Tokyo). 50 (1997) 212-9.
Streptomyces hygroscopicus |
|---|
| 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 |
|---|
