PD Dr. Lalitha Guruprasad

University of Hyderabad
School of Chemistry
500046 - Hyderabad

Prof. Dr. Lalitha's Web Site

Information on the function of a protein can often be obtained from its three dimensional structure. The specific binding of ligands to the protein’s active site, e.g. of a substrate or inhibitor in case of an enzyme, provides the molecular basis for the reactivity. Targeted alterations in the protein se-quence via introducing mutations can provide direct proof of the structure-activity correlation in proteins and will provide clues to engineer proteins with increased or decreased enzyme activities.

We are closely collaborating with Appa Rao on the chitinase D from Serratia proteamaculans. Mu-tations were proposed through altered substrate interactions in order to improve the transglyco-sylation activity of the enzyme. Some of these mutations have been validated experimentally and the project is in progress. Also, we are collaborating with Moerschbacher and Goycoolea to un-derstand the function of a chitosanase, to be able to predict the binding pattern of the chitosan oli-gomers and determine the subsites in the protein that favor the binding of acetylated and deacety-lated oligomer subunits.

In collaboration with Siva Kumar, we are working on jackbean mannosidase to get insights into its 3D structure, glycosylation sites, and the binding of chemical inhibitors such as deoxymannojirimy-cin and mannstatin.

Possible doctoral MCGS projects

We shall focus our studies to understand the structure function cor-relation of carbohydrate binding proteins and propose the necessary modification of proteins and/or substrates. The emphasis of collaborative projects will be on bacterial chitinases, α-mannosidases, 3D modeling and analysis of chitosan modifying enzymes such as chitin deacetylases and chitosan hydrolases, molecular modeling of polysaccharides and glycoconjugates, heparin sulfate, dermatan sulfate oligosaccharides and their interactions with glycosaminoglycans.

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