Jamaluddin, Haryati and Tumbale, Percy and Ferns, Tyrone A. and Thiyagarajan, Nethaji and Brew, Keith and Acharya, K. Ravi (2009) Crystal structure of a-1,3-galactosyltransferase (a3GT) in a complex with p-nitrophenyl-ß-galactoside (pNPßGal). Biochemical and Biophysical Research Communications, 385 (4). pp. 601-604. ISSN 0006291X
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Official URL: http://dx.doi.org/10.1016/j.bbrc.2009.05.111
The specificities of glycosyltransferases make them useful for the synthesis of biologically active oligosaccharides, but also restrict their range of products. In substrate engineering, substrate promiscuity is enhanced by attaching removable interactive groups to weak substrates. Thus, the attachment of ß p-nitrophenyl converts galactose from a poor into a good substrate of a-1,3-galactosyltransferase. The crystallographic structure of a complex of a3GT containing p-nitrophenyl-ß-galactoside shows that the p-nitrophenyl binds similarly to the N-acetylglucosamine of the substrate, N-acetyllactosamine, interacting with the indole of Trp249. p-Nitrophenyl, unlike N-acetylglucosamine, makes no H-bonds but has more non-polar interactions, making it an effective monosaccharide mimetic.
|Uncontrolled Keywords:||a-1,3-Galactosyltransferase, crystal structure, enzyme kinetics, glycosyltransferase, substrate binding|
|Subjects:||Q Science > QD Chemistry|
|Divisions:||Biosciences and Bioengineering (Formerly known)|
|Deposited By:||Ms Zalinda Shuratman|
|Deposited On:||03 Aug 2011 07:17|
|Last Modified:||08 Feb 2017 03:19|
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