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1	Effects of Amino Acid Insertion on the Substrate and Regiospecificity of a Citrus paradisi Glucosyltransferase Tolliver, Benjamin M., Shivakumar, Devaiah P., McIntosh, Cecelia A. 03 April 2014 (has links) Glucosyltransferases, or GTs, are enzymes which perform glucosylation reactions. These glucosylation reactions involve attaching a UDP-activated glucose molecule to acceptor molecules specific to the enzyme. The products of these reactions are observed to have a myriad of effects on metabolic processes, including stabilization of structures, solubility modification, and regulation of compound bioavailability. The enzyme which our lab focuses its research on is a flavonol-specific 3-O-GT found in Citrus paradisi, or grapefruit. This enzyme is part of the class of enzymes known as flavonoid GTs, which are responsible for, among other things, the formation of compounds which can affect the taste of citrus. Our lab focuses its research on performing site-directed mutagenesis on Citrus paradisi 3-O-GT in an attempt to modify its substrate specificity and regiospecificity. In this poster, we report our findings thus far concerning the addition of specific residues to the 3-O-GT's amino acid sequence based on an alignment with the sequence of a putative flavonoid GT found in Citrus sinensis. effects amino acid insertion substrate regiospecificity citrus paradisi glucosyltransferase GTs enzymes glucosylation reactions UDP-activated glucose molecule metabolic processes Biological Sciences School of Graduate Studies Biochemistry Molecular Biology Plant Biology
2	Effects of Amino Acid Sequence Insertion on the Substrate Preference of a Citrus Paradisi Glucosyltransferase Tolliver, Benjamin M., Shivakumar, Devaiah P., McIntosh, Cecelia A. 09 August 2013 (has links) Glucosyltransferases (GTs) are enzymes which perform glucosylation reactions, which involve attaching a UDP-activated glucose molecule to acceptor molecules specifi c to the enzyme. The enzyme which our lab focuses its research on is a fl avonol-specifi c 3-OGT found in Citrus paradisi, or grapefruit (Cp3GT). This enzyme is part of the class of enzymes known as fl avonoid GTs, which are responsible for, among other things, the formation of compounds which can affect the taste of citrus. Our lab focuses its research on performing site-directed mutagenesis on Cp3GT in an attempt to discover the residues important for substrate and regiospecifi city. In this study, we are testing the basis of substrate septicity of Cp3GT. We hypothesize that incorporation of fi ve amino acids specifi c to Citrus sinensis GT (CsGT) into Cp3GT at 308th position may facilitate mCp3GT to use anthocyanidins as one of the substrates. We report our fi ndings thus far concerning the addition of specifi c residues to the Cp3GT’s amino acid sequence based on an alignment with the sequence of a putative fl avonoid GT found in Citrus sinensis. effects amino acid insertion substrate regiospecificity citrus paradisi glucosyltransferase GTs enzymes glucosylation reactions UDP-activated glucose molecule metabolic processes amino acid sequence insertion Biological Sciences School of Graduate Studies Biochemistry Molecular Biology Plant Biology

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Effects of Amino Acid Insertion on the Substrate and Regiospecificity of a Citrus paradisi Glucosyltransferase

Effects of Amino Acid Sequence Insertion on the Substrate Preference of a Citrus Paradisi Glucosyltransferase