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Kinetic characterization of Staphylococcus aureus SpeG polyamine N‐ acetyltransferase
Author(s) -
Boeck Paloma,
Renolo Rossellini,
Forwood Jade,
Kuhn Misty L.
Publication year - 2018
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.2018.32.1_supplement.655.27
Subject(s) - polyamine , acetyltransferase , bacteria , acetyltransferases , biochemistry , staphylococcus aureus , biofilm , biology , microbiology and biotechnology , archaea , enzyme , chemistry , genetics , acetylation , gene
SpeG is a bacterial polyamine N ‐acetyltransferase that belongs to the Gcn5‐related N‐ acetyltransferase (GNAT) superfamily. Members of this family have a diverse set of functions and are present in all domains of life. Polyamines are cationic molecules present in all organisms, with roles in nucleic acid and protein synthesis, the cell cycle, stress responses, and biofilm regulation. While SpeGs from Gram‐negative bacteria have been studied previously, SpeGs from Gram‐positive bacteria have not been kinetically characterized. Here, we present the kinetic characterization of SpeG from Staphylococcus aureus and compare our results with those of other bacterial polyamine acetyltransferases. Additionally, we present a structural comparison of all SpeG proteins that have been deposited into the Protein Data Bank from both Gram‐positive and Gram‐negative bacteria. An understanding of the structure/function relationships of these enzymes is critical to advancing our understanding of how polyamine concentrations are regulated across both Gram‐positive and Gram‐negative bacteria. This may lead to a deeper understanding of the evolution of polyamine acetyltransferases across domains of life and offer opportunities to apply this knowledge toward production of effective pharmaceuticals for infectious bacteria in the future. This abstract is from the Experimental Biology 2018 Meeting. There is no full text article associated with this abstract published in The FASEB Journal .