99 - Iron binding affinity of Entamoeba invadens alcohol dehydrogenase E (EiADHE) in two varieties of E. invadens: VK and IP1
Lauren Salerno1,2, firstname.lastname@example.org, Monichan Phay2, Avelina Espinosa2. (1) Department of Chemistry, Roger Williams University, Bristol, Rhode Island 02809, United States, (2) Department of Biology, Roger Williams University, Bristol, Rhode Island 02809, United States
Little is known about the tertiary structures of the alcohol dehydrogenase E and alcohol dehydrogenase 2 proteins in parasitic protozoans Entamoeba invadens and Entamoeba histolytica. EiADHE and EiADH2 are key metabolic enzymes in the glycolytic alcoholic fermentation pathways of each species, respectively. These enzymes catalyze the conversions of acetyl-CoA to acetaldehyde and acetaldehyde to ethanol, using iron (II) and NAD+ as cofactors. Many microorganisms have been shown to require iron for growth and survival, which has led to the proposal of iron chelators for antimicrobial treatment. We have demonstrated that iron is essential for the two EiADHE dehydrogenase activities. The goal of this study is to determine the binding affinity of Fe2+ to EiADHE, isolated from strains VK and IP1, both for its evolutionary and clinical significance. Additionally, a theoretical tertiary structure of both EhADH2 and EiADHE and their catalytic mutants will be determined using molecular modeling software.
Sunday, March 25, 2012 05:30 PM
Current Topics in Biological Chemistry (05:30 PM - 07:30 PM)
Location: San Diego Convention Center
Room: Hall E