phosphonopyruvate decarboxylase [EC:4.1.1.82]

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) 50:212-9 (1997)
DOI:10.7164/antibiotics.50.212

Lyases;
Carbon-carbon lyases;
Carboxy-lyases

3-phosphonopyruvate carboxy-lyase (2-phosphonoacetaldehyde-forming)

3-phosphonopyruvate = 2-phosphonoacetaldehyde + CO2 [RN:R04053]

R04053

3-phosphonopyruvate [CPD:C02798]

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].

EC 4.1.1.82 created 2005

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.

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.

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.