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Crystal structure of a-1,3-galactosyltransferase (a3GT) in a complex with p-nitrophenyl-ß-galactoside (pNPßGal)

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

Abstract

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.

Item Type:Article
Uncontrolled Keywords:a-1,3-Galactosyltransferase, crystal structure, enzyme kinetics, glycosyltransferase, substrate binding
Subjects:Q Science > QD Chemistry
Divisions:Biosciences and Bioengineering (Formerly known)
ID Code:13294
Deposited By: Ms Zalinda Shuratman
Deposited On:03 Aug 2011 07:17
Last Modified:03 Aug 2011 07:17

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