Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Ca2+ | 0.1 mM, significant increase in activity, more significant acceleration at 10 mM | Homo sapiens | |
Mg2+ | 0.1 mM, significant increase in activity, more significant acceleration at 10 mM | Homo sapiens | |
Mn2+ | 0.1 mM, significant increase in activity | Homo sapiens |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Homo sapiens | - |
recombinantly expressed in Escherichia coli | - |
Source Tissue | Comment | Organism | Textmining |
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Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | fragment-based screening of the donor substrate specificity. Enzyme binds several UDP-activated sugars, including UDP-Glc, UDP-GlcNAc, and UDP-GalNAc. In all cases, UDP is the dominant binding epitope. The binding of donor substrate to GTB is essentially controlled by the base as a molecular anchor. Uracil represents the smallest fragment that is recognized. CDP, AMP, and GDP do not exhibit any significant binding affinity for the enzyme. The ribose and beta-phosphate moieties increase the affinity of the ligands. The pyranose sugar weakens the binding, although this part of the molecule controls the specificity of the enzyme. UDP represents the best binder. The binding affinities of UDP-Gal, UDP-Glc, and UMP are about the same, but lower than that of UDP. beta-D-Galactose and alpha-D-galactose bind weakly to GTB. Whereas beta-D-galactose binds to the acceptor and donor sites, it is suggested that alpha-D-galactose occupies a third hitherto unknown binding pocket | Homo sapiens | ? | - |
? |
Synonyms | Comment | Organism |
---|---|---|
blood group B alpha-(1,3)-galactosyltransferase | - |
Homo sapiens |
blood group B galactosyltransferase | - |
Homo sapiens |