Polyamine acetyltransferases

We study polyamine N-acetyltransferases across all domains of life to determine why some are allosteric and others are not, why some adopt diverse oligomeric states, and why their structures and substrate specificity are not conserved within and across domains of life.

Polyamines are polycationic molecules that control a variety of cellular processes. During times of stress in bacteria these molecules become acetylated. Although many bacterial polyamine acetyltransferases have been studied in the past, there is still a lot to learn and explore regarding their structure/function relationships. One enzyme we are currently studying in detail is the polyamine acetyltransferase SpeG, which adopts a unique dodecameric structure and has an allosteric site. This unusual oligomeric state and allosteric behavior of this enzyme presents many opportunities to explore how these properties contribute to the function of this enzyme and other GNATs that exhibit similar characteristics.

We are currently using site-directed mutagenesis, enzyme kinetics assays, and protein crystallography to study these enzymes in more detail. We are in the process of adding new technologies to our repertoire.