Literature summary for 2.4.1.37 extracted from

Fluegge, F.; Peters, T.
Insights into allosteric control of human blood group A and B glycosyltransferases from dynamic NMR (2019), ChemistryOpen, 8, 760-769 .

Crystallization (Commentary)

Crystallization (Comment)	Organism
Methyl-TROSY-based titration experiments in combination with zz-exchange experiments show dramatic changes of binding kinetics associated with allosteric interactions between donor-type and acceptor-type ligands. Binding of the acceptor substrates H-disaccharide, H-type II trisaccharide, and H-type VI trisaccharide affects the chemical shifts of the 13C-methyl groups of Met 266, Val 299, Leu 324, and Leu 329, which belong to the acceptor substrate binding pocket	Homo sapiens

Crystallization (Comment)

Organism

Methyl-TROSY-based titration experiments in combination with zz-exchange experiments show dramatic changes of binding kinetics associated with allosteric interactions between donor-type and acceptor-type ligands. Binding of the acceptor substrates H-disaccharide, H-type II trisaccharide, and H-type VI trisaccharide affects the chemical shifts of the 13C-methyl groups of Met 266, Val 299, Leu 324, and Leu 329, which belong to the acceptor substrate binding pocket

Homo sapiens

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	P16442	-	-

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)