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. 2022 May 24;298(7):102067. doi: 10.1016/j.jbc.2022.102067

Figure 4.

Figure 4

Relative contribution of the different ADP1 enzymes to the alternative β-alanine biosynthesis pathway.A, comparison of wildtype and ΔpanD growth. B, growth of single-deletion mutants of candidate genes involved in the alternative pathway. C, growth of Δddc complemented with DAP (1 mM) or β-alanine (10 μM). D, growth of the ΔpanD strain additionally deleted for the various candidate genes. E, growth of the double mutants complemented with β-alanine. F, comparison of DAP content in Δddc and WT strains. Independent overnight cultures were grown in minimal medium for Acinetobacter (MA) supplemented with 1 mM DAP and 10 μM β-alanine, harvested, and washed before inoculation in MA minimal medium. Absorbance at 600 nm was recorded by an automated growth curve analysis system (Bioscreen-C; Thermo Fisher Scientific). Values correspond to the average of three replicates. Colors indicate the gene(s) deleted in each strain. LC/MS/MS data for DAP correspond to six independent metabolite extractions for each strain. Indicated values in F correspond to automatic peak integration for the mass transition m/z 283.1 → 104.9. Values of DAP in Δddc were below the detection limit (Fig. S4). ADP1, Acinetobacter baylyi ADP1; DAP, 1,3-diaminopropane.