Microbial degradation plays a critical role in determining the environmental fate of steroid hormones, such as 17β-estradiol (E2). The molecular mechanisms governing the microbial transformation of E2 and its primary degradation intermediate, estrone (E1), are largely unknown. The objective of this study was to identify metabolism pathways that might be involved in microbial estrogen degradation. To achieve the objective, Stenotrophomonas maltophilia strain ZL1 was used as a model estrogen degrading bacterium and its protein expression level during E2/E1 degradation was studied using quantitative proteomics. During an E2 degradation experiment, strain ZL1 first converted E2 to E1 stoichiometrically. At 16 h E1 reached its peak concentration, and microbial growth started. At the same time, enzymes involved in certain catabolic and anabolic pathways were most highly expressed compared to the other time points tested. Among those enzymes, the ones involved in protein and lipid biosyntheses were observed to be particularly active. Based on the metabolite information from a previous study and the proteomic data from this study, we hypothesized that S. maltophilia strain ZL1 was able to convert E1 to amino acid tyrosine through ring cleavage on a saturated ring of the E1 molecule and then utilize tyrosine in protein biosynthesis.
Available at: http://works.bepress.com/zhongtian_li/3/