EC Number |
Natural Substrates |
---|
2.4.1.66 | more |
there must be an additional glucosyltransferase to LH3 that is responsible for most of the collagen glucosylation in vivo |
2.4.1.66 | more |
the reduction of the galactosylhydroxylysyl glucosyltransferase activity of LH3 disrupts the localization of type IV collagen, and thus the formation of basement membranes during mouse embryogenesis leading to lethality at embryonic day 9.5-14.5. Survival of hypomorphic embryos and the formation of the basement membrane are directly correlated with the level of galactosylhydroxylysyl glucosyltransferase activity. An LH3-knockout mouse lacks galactosylhydroxylysyl glucosyltransferase. Lysyl hydroxylase 3 is the main molecule responsible for galactosylhydroxylysyl glucosyltransferase activity. Galactosylhydroxylysyl glucosyltransferase is essential for the formation of the basement membrane |
2.4.1.66 | UDP-alpha-D-glucose + [procollagen]-(5R)-5-O-(beta-D-galactosyl)-5-hydroxy-L-lysine |
- |
2.4.1.66 | UDP-glucose + (2S,5R)-5-O-(beta-D-galactosyl)-5-hydroxy-L-lysine-[procollagen] |
- |
2.4.1.66 | UDP-glucose + 5-(D-galactosyloxy)-L-lysine-procollagen |
probably postribosomal, attachment of galactose and glucose to hydroxylysine in collagen could conceivably function as part of the control mechanism signaling completion of the molecule and initiating its release |
2.4.1.66 | UDP-glucose + 5-(D-galactosyloxy)-L-lysine-procollagen |
involved in collagen biosynthesis |
2.4.1.66 | UDP-glucose + 5-(D-galactosyloxy)-L-lysine-procollagen |
may play a major role in the mechanism of platelet:collagen adhesion |
2.4.1.66 | UDP-glucose + 5-(D-galactosyloxy)-L-lysine-procollagen |
posttranslational modification of collagen |
2.4.1.66 | UDP-glucose + 5-(D-galactosyloxy)-L-lysine-procollagen |
marker enzyme of collagen biosynthesis |
2.4.1.66 | UDP-glucose + 5-(D-galactosyloxy)-L-lysine-procollagen |
intracellular enzyme of collagen biosynthesis |