Conserved residues Arg188 and Asp302 are critical for active site organization and catalysis in human ABO(H) blood group A and B glycosyltransferases†

Author:

Gagnon Susannah M L1,Legg Max S G1,Polakowski Robert2,Letts James A1,Persson Mattias3,Lin Shuangjun2,Zheng Ruixiang Blake2,Rempel Brian2,Schuman Brock1,Haji-Ghassemi Omid1,Borisova Svetlana N1,Palcic Monica M123,Evans Stephen V1

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

Reference61 articles.

1. Structural snapshots of alpha-1,3-galactosyltransferase with native substrates: Insight into the catalytic mechanism of retaining glycosyltransferases;Albesa-Jove;Angew Chem Int Ed Engl,2017

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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