PMID:15026039

Citation	Banks, J and Cane, DE (2004) Biosynthesis of vitamin B6: direct identification of the product of the PdxA-catalyzed oxidation of 4-hydroxy-l-threonine-4-phosphate using electrospray ionization mass spectrometry. Bioorg. Med. Chem. Lett. 14:1633-6
Abstract	PdxA (E.C. 1.1.1.262) catalyzes a key step in the biosynthesis of vitamin B(6): the nicotinamide-dependent oxidation of 4-hydroxy-l-threonine-4-phosphate (HTP) to a product tentatively identified as 3-amino-1-hydroxyacetone 1-phosphate (AHAP). To date, the evidence for the formation of AHAP, while self-consistent, has been largely circumstantial, and does not exclude the possibility that the actual product of the enzyme-catalyzed oxidation of HTP might be 2-amino-3-oxo-4-hydroxybutyric acid 4-phosphate which could undergo rapid, non-enzyme-catalyzed decarboxylation once released from the protein. Use of negative ion electrospray ionization mass spectrometry (ESI-MS) and tandem mass spectrometric analysis (MS-MS) confirms that AHAP is the product of the PdxA-catalyzed reaction.
Links	PubMed Online version:10.1016/j.bmcl.2004.01.065
Keywords	Catalysis; Escherichia coli Proteins/analysis; Escherichia coli Proteins/metabolism; Oxidation-Reduction; Oxidoreductases/analysis; Oxidoreductases/metabolism; Phosphothreonine/analysis; Phosphothreonine/metabolism; Spectrometry, Mass, Electrospray Ionization/methods; Vitamin B 6/analysis; Vitamin B 6/biosynthesis
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