| EC |
4.1.1.82 |
| Accepted name: |
phosphonopyruvate decarboxylase |
| Reaction: |
3-phosphonopyruvate = 2-phosphonoacetaldehyde + CO2 |
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For diagram of phosphonate metabolism, click here |
| Other name(s): |
3-phosphonopyruvate carboxy-lyase |
| Systematic name: |
3-phosphonopyruvate carboxy-lyase (2-phosphonoacetaldehyde-forming) |
| Comments: |
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]. |
| Links to other databases: |
BRENDA, EXPASY, Gene, KEGG, MetaCyc, CAS registry number: 151662-34-9 |
| References: |
| 1. |
Zhang, G., Dai, J., Lu, Z. and Dunaway-Mariano, D. The phosphonopyruvate decarboxylase from Bacteroides fragilis. J. Biol. Chem. 278 (2003) 41302–41308. [DOI] [PMID: 12904299] |
| 2. |
Seidel, H.M. and Knowles, J.R. Interaction of inhibitors with phosphoenolpyruvate mutase: implications for the reaction mechanism and the nature of the active site. Biochemistry 33 (1994) 5641–5646. [PMID: 8180189] |
| 3. |
Nakashita, H., Watanabe, K., Hara, O., Hidaka, T. and 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) 212–219. [PMID: 9127192] |
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| [EC 4.1.1.82 created 2005] |
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