Evidence that a deferrioxamine B degrading enzyme is a serine protease.

Siderophores are organic biomolecules synthesized by a wide variety of microbes. The molecules sequester ferric ion from environments where it is present at extremely low concentrations. Siderophores are of consequence with respect to microbial nutrition, pathogenicity, virulence, and microbe-plant interactions. How siderophores are degraded and returned to the carbon and nitrogen cycles is not well understood. The catalytic activity of an enzyme from a bacterium that degrades the siderophore deferrioxamine B has been examined. While the degradation of deferrioxamine B is sensitive to sulfhydryl and metal moiety inhibitors, the data presented is most consistent with the hypothesis that the enzyme uses a hydroxyl moiety (serine peptidase) to catalyze the degradation of deferrioxamine B. If sulfhydryl and metal inhibitors are simultaneously present at concentrations that when alone only partially inhibit the enzyme, the enzyme is unable to catalyze deferrioxamine B dissimilation. Analysis of the inhibitor experiments conducted led to the conclusion that the deferrioxamine B degrading enzyme is a serine-peptidase-like enzyme that needs calcium ions and sulfhydryl groups to be fully activated or stabilized. The knowledge of the catalytic moieties of the enzyme will be exploited to purify the enzyme.