@phdthesis{b627685afa264548b87d674261de276f,
title = "Enzymatic Study of Two Phospholipid-Catalysing Enzymes: Lipid A Phosphoethanolamine Transferase from Pathogenic Neisseria and Phospholipase D from Streptomyces antibioticus",
abstract = "Lipid A phosphoethanolamine transferase (EptA) is an enzyme that modifies the lipid A portion of LPS/LOS of pathogenic Gram-negative bacteria by addition of phosphoethanolamine. The modification confers bacterial resistance to defensins and polymyxin. EptA is an important target enzyme for the development of novel therapeutic agents. In this study, the in vitro interactions of EptA and its substrates, phosphatidylethanolamine (PE) and LOS, were investigated through biophysical and structural studies as well as enzyme assays. Structural investigations on phospholipase D from Streptomyces antibioticus were carried out as a mini project within this thesis to understand the enzyme{\textquoteright}s acyl group recognition.",
keywords = "EptA, Neisseria, lipooligosaccharide, antibiotic resistance, PLD, enzyme, crystalography",
author = "Ariela Samantha",
year = "2022",
doi = "10.26182/ek26-v943",
language = "English",
school = "The University of Western Australia",
}