EC number:4.1.1.82
| ID: | 4.1.1.82 | ||
|---|---|---|---|
| Description: | Phosphonopyruvate decarboxylase. | ||
| Alternative Name: |
3-phosphonopyruvate carboxy-lyase. | ||
| Prosite: | PDOC00166; | ||
| PDB: |
|
3D structure
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External Links
| UniProtKB Enzyme Link: | UniProtKB 4.1.1.82 |
| BRENDA Enzyme Link: | BRENDA 4.1.1.82 |
| KEGG Enzyme Link: | KEGG4.1.1.82 |
| BioCyc Enzyme Link: | BioCyc 4.1.1.82 |
| ExPASy Enzyme Link: | ExPASy4.1.1.82 |
| EC2PDB Enzyme Link: | EC2PDB 4.1.1.82 |
| ExplorEnz Enzyme Link: | ExplorEnz 4.1.1.82 |
| PRIAM enzyme-specific profiles Link: | PRIAM 4.1.1.82 |
| IntEnz Enzyme Link: | IntEnz 4.1.1.82 |
| MEDLINE Enzyme Link: | MEDLINE 4.1.1.82 |
| RHEA:20768 | 3-phosphonopyruvate + H(+) = CO2 + phosphonoacetaldehyde |
| RULE(radius=1) | [*:1]=[C;H0;+0:2](-[OH;+0:3])-[C;H0;+0:4](=[*:5])-[*:6].[H+;H0:7]>>[*:1]=[C;H0;+0:2]=[O;H0;+0:3].[*:5]=[CH;+0:4]-[*:6] |
| Reaction |  |
| Core-to-Core | No scaffolds atoms were exchanged as a result of the reaction |
References
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| 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. | Nakashita H, Watanabe K, Hara O, Hidaka T, Seto H | 1997 Mar | 9127192 |
| Interaction of inhibitors with phosphoenolpyruvate mutase: implications for the reaction mechanism and the nature of the active site. | Seidel HM, Knowles JR | 1994 May 10 | 8180189 |
| The phosphonopyruvate decarboxylase from Bacteroides fragilis. | Zhang G, Dai J, Lu Z, Dunaway-Mariano D | 2003 Oct 17 | 12904299 |