Entry |
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Name |
phosphonopyruvate decarboxylase;
3-phosphonopyruvate carboxy-lyase
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Class |
Lyases;
Carbon-carbon lyases;
Carboxy-lyases
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Sysname |
3-phosphonopyruvate carboxy-lyase (2-phosphonoacetaldehyde-forming)
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Reaction(IUBMB) |
3-phosphonopyruvate = 2-phosphonoacetaldehyde + CO2 [RN: R04053]
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Reaction(KEGG) |
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Substrate |
3-phosphonopyruvate [CPD: C02798]
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Product |
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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].
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History |
EC 4.1.1.82 created 2005
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Pathway |
ec00440 | Phosphonate and phosphinate metabolism |
ec00998 | Biosynthesis of various secondary metabolites - part 2 |
ec01110 | Biosynthesis of secondary metabolites |
ec01120 | Microbial metabolism in diverse environments |
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Orthology |
K09459 | phosphonopyruvate decarboxylase |
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Genes |
» show all
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Reference |
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Authors |
Zhang G, Dai J, Lu Z, Dunaway-Mariano D. |
Title |
The phosphonopyruvate decarboxylase from Bacteroides fragilis. |
Journal |
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Reference |
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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 |
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Reference |
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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 |
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Other DBs |
ExplorEnz - The Enzyme Database: | 4.1.1.82 |
ExPASy - ENZYME nomenclature database: | 4.1.1.82 |
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LinkDB |
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