Affinity, kinetic, and structural study of the interaction of 3-O-sulfotransferase isoform 1 with heparan sulfate.

Biochemistry
Eva M MuñozRobert J Linhardt

Abstract

The 3-O-sulfonation of glucosamine residues in heparan sulfate (HS) by 3-O-sulfotransferase (3-OST) is a key substitution that is present in HS sequences of biological importance, in particular HS anticoagulant activity. Six different isoforms of 3-OST have been identified that exhibit different substrate specificity. In this paper the affinity and kinetics of the interaction between 3-O-sulfotransferase isoform 1 (3-OST-1) and HS have been examined using surface plasmon resonance (SPR). 3-OST-1 binds with micomolar affinity to HS (K(D) = 2.79 microM), and this interaction is apparently independent of the presence of the coenzyme, 3'-phosphoadenosine 5'-phosphosulfate (PAPS). A conformational change in the complex has also been detected, supporting data from previous studies. Selected 3-OST-1 mutants have provided valuable information of amino acid residues that participate in 3-OST-1 interaction with HS substrate and its catalytic activity. The results from this study contribute to understanding the substrate specificity among the 3-OST isoforms and in the mechanism of 3-OST-1-catalyzed biosynthesis of anticoagulant HS.

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Citations

May 14, 2010·Journal of the American Society for Mass Spectrometry·Lieza M DananJulie A Leary
Jul 14, 2009·Journal of the American Chemical Society·Jeffrey G MartinRobert J Linhardt
Feb 4, 2009·The Journal of Biological Chemistry·Benny PachecoMarco Maccarana
Dec 13, 2007·Journal of Molecular Recognition : JMR·Rebecca L Rich, David G Myszka
Sep 29, 2015·Glycoconjugate Journal·Fuming ZhangRobert J Linhardt
Jul 19, 2012·PloS One·Eva Maria PutzEva Zebedin-Brandl
Aug 9, 2018·Scientific Reports·David F ThiekerRobert J Woods
May 19, 2017·Bioengineering & Translational Medicine·Deepika VaidyanathanRobert J Linhardt

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