Glycosyltransferase

The phosphate(s) of these donor molecules are usually coordinated by divalent cations such as manganese, however metal independent enzymes exist.

Many glycosyltransferases are single-pass transmembrane proteins, and they are usually anchored to membranes of Golgi apparatus[3] Glycosyltransferases can be segregated into "retaining" or "inverting" enzymes according to whether the stereochemistry of the donor's anomeric bond is retained (α→α) or inverted (α→β) during the transfer.

An "orthogonal associative" mechanism has been proposed which, akin to the inverting enzymes, requires only a single nucleophilic attack from an acceptor from a non-linear angle (as observed in many crystal structures) to achieve anomer retention.

[4] The recent discovery of the reversibility of many reactions catalyzed by inverting glycosyltransferases served as a paradigm shift in the field and raises questions regarding the designation of sugar nucleotides as 'activated' donors.

[16] The ABO blood group system is determined by what type of glycosyltransferases are expressed in the body.

The deletion causes a frameshift and results in translation of an almost entirely different protein that lacks enzymatic activity.

The combination of glycosyltransferases by both alleles present in each person determines whether there is an AB, A, B or O blood type.

In cell-free approaches, the large-scale application of glycosyltransferases for glycoconjugate synthesis has required access to large quantities of the glycosyl donors.