MalA is an enzyme found in the predatory bacterium Bdellovibrio bacteriovorous that cleaves maltose, a disaccharide, into two glucose subunits. The goal of this research project is to explore the interaction of MalA with maltose by synthesizing three maltose analogs in which the 6-OH on the +1 glucose is replaced with hydrogen, fluorine, or methoxy. Also, to probe the significance of the 6-OH on the -1 glucose in the interaction with MalA, we will synthesize α-methyl-glucopyranoside analogs where the 6-OH is again replaced with hydrogen, fluorine, or methoxy. We will then test MalA’s ability to bind with and cleave each maltose and α-methyl-glucopyranoside analog.

Characterization of the malA enzyme from Bdellovibrio bacteriovorus through the synthesis and analysis of maltose and α-methyl-glucopyranoside derivatives

253rd National Meeting (2017)

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