pH-induced conformational changes in human ABO(H) blood group glycosyltransferases confirm the importance of electrostatic interactions in the formation of the semi-closed state
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High Resolution Structures of the Human ABO(H) Blood Group Enzymes in Complex with Donor Analogs Reveal That the Enzymes Utilize Multiple Donor Conformations to Bind Substrates in a Stepwise MannerGlycosyltransfer 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.
P2860
pH-induced conformational changes in human ABO(H) blood group glycosyltransferases confirm the importance of electrostatic interactions in the formation of the semi-closed state
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pH-induced conformational chan ...... ation of the semi-closed state
@ast
pH-induced conformational chan ...... ation of the semi-closed state
@en
pH-induced conformational chan ...... ation of the semi-closed state
@nl
type
label
pH-induced conformational chan ...... ation of the semi-closed state
@ast
pH-induced conformational chan ...... ation of the semi-closed state
@en
pH-induced conformational chan ...... ation of the semi-closed state
@nl
prefLabel
pH-induced conformational chan ...... ation of the semi-closed state
@ast
pH-induced conformational chan ...... ation of the semi-closed state
@en
pH-induced conformational chan ...... ation of the semi-closed state
@nl
P2093
P50
P356
P1433
P1476
pH-induced conformational chan ...... ation of the semi-closed state
@en
P2093
Asha R Johal
Javier A Alfaro
Svetlana Borisova
P304
P356
10.1093/GLYCOB/CWT098
P577
2013-11-20T00:00:00Z