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thiamine pyrophosphate-dependent enzyme
thiamine pyrophosphate-binding protein
thiamine pyrophosphate enzyme family protein
thiamine pyrophosphate (TPP) enzyme family protein which requires TPP, and may be a phosphonopyruvate (PnPy) decarboxylase which catalyzes the decarboxylation of PnPy to form phosphonoacetaldehyde (PnAA) in the biosynthesis of phosphonate-containing compounds, similar to Streptomyces fradiae putative PnPy decarboxylase Fom2 which may produce PnAA in the fosfomycin biosynthetic pathway
phosphonopyruvate decarboxylase
This family consists of examples of phosphonopyruvate an decarboxylase enzyme that produces phosphonoacetaldehyde (Pald), the second step in the biosynthesis phosphonate-containing compounds. Since the preceding enzymate step, PEP phosphomutase (AepX, TIGR02320) favors the substrate PEP energetically, the decarboxylase is required to drive the reaction in the direction of phosphonate production. Pald is a precursor of natural products including antibiotics like bialaphos [1] and phosphonothricin [2] in Streptomyces species, phosphonate-modified molecules such as the polysaccharide B of Bacteroides fragilis [3], the phosphonolipids of Tetrahymena pyroformis [4], the glycosylinositolphospholipids of Trypanosoma cruzi [5]. This gene generally occurs in prokaryotic organisms adjacent to the gene for AepX. Most often an aminotansferase (aepZ) is also present which leads to the production of the most common phosphonate compound, 2-aminoethylphosphonate (AEP).
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