Pyridoxal-5’-phosphate (PLP), one of the active forms of vitamin B6, is a prosthetic group of many enzymes. Depending on the fold type, PLP-bound proteins are classified into five families: aspartate aminotransferase family, tryptophan synthase family, D-amino acid aminotransferase family, alanine racemase family (TIM-barrel) and glycogen phosphorylase family. Study of PLP enzymes are of great importance: it can help us understand enzyme functions and mechanisms as well as design drugs for certain diseases such as Alzheimer’s disease1 and Parkinson’s disease2. Up to date, however, most research focused on individual PLP-dependent enzymes and there lacks a study on PLP proteomics (PLPome), especially on the targeting and isolating PLP enzymes. In this research, we developed a method to probe and identify PLP proteins. By feeding cells with a designed PLP analog molecule, we were able to label PLP proteins in bacterial proteome and enrich them using affinity chromatography. Five PLP proteins were identified by trypsin digestion followed by mass spectrometry method. And this method was also used to study PLP proteins under certain stress conditions.

PLP proteomics: Probing and identifying of PLP-dependent proteins in bacteria

249th National Meeting (2015)

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