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|Title:||A motif rich in charged residues determines product specificity in isomaltulose synthase||Authors:||Zhang, D.
|Issue Date:||16-Jan-2003||Citation:||Zhang, D., Li, N., Swaminathan, K., Zhang, L.-H. (2003-01-16). A motif rich in charged residues determines product specificity in isomaltulose synthase. FEBS Letters 534 (1-3) : 151-155. ScholarBank@NUS Repository. https://doi.org/10.1016/S0014-5793(02)03835-8||Abstract:||Isomaltulose synthase (PalI) catalyzes hydrolysis of sucrose and formation of α-1,6 and α-1,1 bonds to produce isomaltulose (α-D-glucosylpyranosyl-1,6-D-fructofranose) and small amount of trehalulose (α-D-glucosylpyranosyl-1,1-D-fructofranose). A potential isomaltulose synthase-specific motif (325RLDRD329), that contains a 'DxD' motif conserved in many glycosyltransferases, was identified based on sequence comparison with reference to the secondary structural features of PalI and homologs. Site-directed mutagenesis analysis of the motif showed that the four charged amino acid residues (Arg325, Arg328, Asp327 and Asp329) influence the enzyme kinetics and determine the product specificity. Mutation of these four residues increased trehalulose formation by 17-61% and decreased isomaltulose by 26-67%. We conclude that the 'RLDRD' motif controls the product specificity of PalI. © 2002 Published by Elsevier Science B.V. on behalf of the Federation of European Biochemical Societies.||Source Title:||FEBS Letters||URI:||http://scholarbank.nus.edu.sg/handle/10635/99853||ISSN:||00145793||DOI:||10.1016/S0014-5793(02)03835-8|
|Appears in Collections:||Staff Publications|
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