Area of Study
Science and Mathematics
MalA is an α-glucosidase found in the bacterium Bdellovibrio bacteriovorus, a predatory bacteria that preys on gram-negative bacteria, including several plant and human pathogens. The gene for MalA was discovered while sequencing the genome of Bdellovibrio and was predicted to be a maltase based on homology. Maltase enzymes are characterized by their role in the catalysis of maltose into two glucose subunits. MalA will bind to several different disaccharides composed of a glucose α-linked to a variety of sugars (isomaltose, trehalose, turanose, sucrose, etc.), but it does not cleave them. The objective of our research was to investigate how the various components of maltose contribute to binding and cleavage by MalA. In order to do this, we developed a route to synthesize maltose analogs with specific changes to the primary alcohol at the 6th position on the +1 site. In place of the targeted alcohol, the desired analogs will contain either a fluorine atom, a methoxy group, or a hydrogen. The fluorine atom will act as an H-bond acceptor, but not an H-bond donor. The methoxy group will be a bulky replacement for the alcohol that may impact cleavage due to its size. The deoxygenation will remove the presence of the alcohol that acts as an H-bond acceptor and H-bond donor. Over the course of our research, we were able to synthesize maltose molecules with all alcohols protected except the targeted alcohol on the 6th position of the +1 site. Over this next year, we will continue the synthesis and ultimately perform spectral analysis with MalA and each synthesized maltose derivative.
Jepson, Joey R., "Characterization of the MalA Enzyme from Bdellovibrio bacteriovorus through the Synthesis and Analysis of Maltose Derivatives" (2016). Summer Research. 277.
University of Puget Sound