Fig. 2From: Gut bacterial deamination of residual levodopa medication for Parkinson’s diseaseIdentification of the aromatic amino transferase initiating the deamination pathway. In order to identify which aminotransferase is responsible for the initial transaminase reaction, all class I/II aminotransferases were cloned and purified to test the activity against (N)PAAAs. a Transaminase activity (production of glutamate) for all substrates is depicted. EDU38870 (CLOSPO_01732) was involved in all transaminase reactions. EDU37030 showed similar activity as EDU38870, for phenylalanine. Experiment was performed in technical duplicates to screen for candidate genes for mutagenesis in C. sporogenes. b Targeted metabolic quantification of deamination products from CSWT, CSΩfldC, and CSΩCLOSPO_01732 reveals that EDU38870 is involved in the transamination of all for all tested (N)PAAAs. All quantified deamination products are normalized to their initial substrate concentration, and the data represents 3 independent biological replicates. Corresponding values are reported, and metabolite concentration differences between WT and ΩfldC or ΩCLOSPO_01732 were tested for significance using Student’s t test, in Additional File 1: Table S1. Black squares indicate that quantification was not possible because of a coeluting HPLC-ED peak. As no commercial standards are available for 5-HILA and 5-HIPA, the peaks were quantified assuming a similar ED-detector response as for 5-HTPBack to article page