Conserved residues Arg188 and Asp302 are critical for active site organization and catalysis in human ABO(H) blood group A and B glycosyltransferases†
Author:
Affiliation:
1. Department of Biochemistry & Microbiology, University of Victoria, STN CSC, Victoria, BC, Canada
2. Department of Chemistry, University of Alberta, Edmonton, AB, Canada
3. Carlsberg Laboratory, Gamle Carlsberg Vej 4-10, Copenhagen V, Denmark
Funder
Natural Sciences and Engineering Research Council (NSERC)
Alberta Ingenuity Centre for Carbohydrate Science
Canadian Institutes of Health Research
Publisher
Oxford University Press (OUP)
Subject
Biochemistry
Link
http://academic.oup.com/glycob/article-pdf/28/8/624/25181078/cwy051.pdf
Reference61 articles.
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2. ABO(H) blood group A and B glycosyltransferases recognize substrate via specific conformational changes;Alfaro;J Biol Chem,2008
3. Blood group B galactosyltransferase: Insights into substrate binding from NMR experiments;Angulo;J Am Chem Soc,2006
4. The CCP4 suite—Programs for protein crystallography;Bailey;Acta Crystallogr D Biol Crystallogr,1994
5. Glycosyltransfer in mutants of putative catalytic residue Glu303 of the human ABO(H) A and B blood group glycosyltransferases GTA and GTB proceeds through a labile active site;Blackler;Glycobiology,2017
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