Procollagen galactosyltransferase

In enzymology, a procollagen galactosyltransferase is an enzyme that catalyzes the chemical reaction
Thus, the two substrates of this enzyme are UDP-galactose and procollagen 5-hydroxy-L-lysine, whereas its two products are UDP and procollagen 5-(D-galactosyloxy)-L-lysine.
This enzyme belongs to the family of glycosyltransferases, specifically the hexosyltransferases. The systematic name of this enzyme class is UDP-galactose:procollagen-5-hydroxy-L-lysine D-galactosyltransferase. Other names in common use include hydroxylysine galactosyltransferase, collagen galactosyltransferase, collagen hydroxylysyl galactosyltransferase, UDP galactose-collagen galactosyltransferase, uridine diphosphogalactose-collagen galactosyltransferase, and UDPgalactose:5-hydroxylysine-collagen galactosyltransferase. This enzyme participates in lysine degradation.

Structure and functions of procollagen galactosyltransferase 1

Procollagen galactosyltransferase 1, encoded by the COLGALT1 gene, plays a crucial role in lysyl O-linked glycosylation and the maturation of collagen. GT251 consists of two galactosyltransferase domains and is stabilized in a dimeric form. The GT251 dimer can further associate with LH3 to form a heterotetrameric complex, known as the KOGG complex. Within this complex, three key enzymatic reactions in lysine O-linked glycosylation are coordinately catalyzed by LH3 and GT251, ensuring proper collagen modification and structural integrity.