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denatured collagen type I + UDP-alpha-D-galactose
UDP + galactosylated collagen type I
-
-
-
?
UDP-alpha-D-galactose + calf skin collagen
?
-
-
-
-
?
UDP-alpha-D-galactose + hydroxylysyl acceptor sites
?
-
-
-
-
?
UDP-alpha-D-galactose + procollagen 5-hydroxy-L-lysine
UDP + procollagen 5-(D-galactosyloxy)-L-lysine
UDP-alpha-D-galactose + [procollagen]-(5R)-5-hydroxy-L-lysine
UDP + [procollagen]-(5R)-5-O-(beta-D-galactosyl)-5-hydroxy-L-lysine
UDP-galactose + bovine collagen type I (deglycosylated)
UDP + ?
-
-
-
?
UDPgalactose + alpha1-glycoprotein with sialic acid and galactose removed
?
-
less active than with guinea pig skin collagen with sugar residues removed
-
-
?
UDPgalactose + fetuin with sialic acid and galactose removed
?
-
33% of activity with bovine achilles tendon collagen with glucose and galactose residues removed
-
-
?
UDPgalactose + ichthyocol
?
-
fish collagen ichthyocol as best substrate, peptides derived from collagenase- and pronase-digestion of ichthyocol are less effective
-
-
?
UDPgalactose + ovalbumin
?
-
17.9% of activity with bovine achilles tendon collagen with glucose and galactose residues removed
-
-
?
UDPgalactose + procollagen 5-hydroxy-L-lysine
UDP + procollagen 5-(D-galactosyloxy)-L-lysine
UDPgalactose + submaxillary glycoprotein with sialic acid removed
?
additional information
?
-
UDP-alpha-D-galactose + procollagen 5-hydroxy-L-lysine
UDP + procollagen 5-(D-galactosyloxy)-L-lysine
-
-
-
-
?
UDP-alpha-D-galactose + procollagen 5-hydroxy-L-lysine
UDP + procollagen 5-(D-galactosyloxy)-L-lysine
-
-
-
?
UDP-alpha-D-galactose + [procollagen]-(5R)-5-hydroxy-L-lysine
UDP + [procollagen]-(5R)-5-O-(beta-D-galactosyl)-5-hydroxy-L-lysine
-
-
-
?
UDP-alpha-D-galactose + [procollagen]-(5R)-5-hydroxy-L-lysine
UDP + [procollagen]-(5R)-5-O-(beta-D-galactosyl)-5-hydroxy-L-lysine
human lysyl hydroxylase 3 (LH3/PLOD3) is a multifunctional collagen lysyl hydroxylase and glycosyltransferase LH3. Two distinct catalytic sites at the N- and C-terminal boundaries of each monomer are separated by an accessory domain. Collagen glucosyltransferase (EC 2.4.1.66) and procollagen galactosyltransferase (EC 2.4.1.50) activities localize at the N-terminus of the enzyme, whereas the lysyl hydroxylase activity (EC 1.14.11.4) is segregated at the LH3 C-terminus
-
-
?
UDPgalactose + procollagen 5-hydroxy-L-lysine
UDP + procollagen 5-(D-galactosyloxy)-L-lysine
-
guinea pig skin collagen with sugar residues removed
-
-
?
UDPgalactose + procollagen 5-hydroxy-L-lysine
UDP + procollagen 5-(D-galactosyloxy)-L-lysine
-
high specificity for galactosyl acceptor
-
-
?
UDPgalactose + procollagen 5-hydroxy-L-lysine
UDP + procollagen 5-(D-galactosyloxy)-L-lysine
-
involved in collagen biosynthesis, post-translational modification, probably involved in synthesis of carbohydrate units in complement
-
-
?
UDPgalactose + procollagen 5-hydroxy-L-lysine
UDP + procollagen 5-(D-galactosyloxy)-L-lysine
-
triple helix conformation of native collagen at 30°C prevents glycosylation
-
?
UDPgalactose + procollagen 5-hydroxy-L-lysine
UDP + procollagen 5-(D-galactosyloxy)-L-lysine
-
triple helix conformation of native collagen at 30°C prevents glycosylation
-
?
UDPgalactose + procollagen 5-hydroxy-L-lysine
UDP + procollagen 5-(D-galactosyloxy)-L-lysine
-
guinea pig skin collagen with sugar residues removed
-
?
UDPgalactose + procollagen 5-hydroxy-L-lysine
UDP + procollagen 5-(D-galactosyloxy)-L-lysine
-
peptides derived from citrate soluble collagen by collagenase digestion, longer peptides are better substrates
-
?
UDPgalactose + procollagen 5-hydroxy-L-lysine
UDP + procollagen 5-(D-galactosyloxy)-L-lysine
-
bovine renal glomerular basement membrane
-
?
UDPgalactose + procollagen 5-hydroxy-L-lysine
UDP + procollagen 5-(D-galactosyloxy)-L-lysine
-
bovine anterior lens capsule collagen with carbohydrate units removed
-
?
UDPgalactose + procollagen 5-hydroxy-L-lysine
UDP + procollagen 5-(D-galactosyloxy)-L-lysine
-
heat-denatured citrate-soluble rat skin collagen is a more effective substrate than gelatinized insoluble calf skin collagen
-
?
UDPgalactose + procollagen 5-hydroxy-L-lysine
UDP + procollagen 5-(D-galactosyloxy)-L-lysine
-
dialyzable peptides prepared by collagenase digestion of bovine Achilles tendon collagen
-
?
UDPgalactose + procollagen 5-hydroxy-L-lysine
UDP + procollagen 5-(D-galactosyloxy)-L-lysine
-
gelatinized insoluble calf skin collagen
-
?
UDPgalactose + procollagen 5-hydroxy-L-lysine
UDP + procollagen 5-(D-galactosyloxy)-L-lysine
-
gelatinized insoluble calf skin collagen
-
?
UDPgalactose + procollagen 5-hydroxy-L-lysine
UDP + procollagen 5-(D-galactosyloxy)-L-lysine
-
gelatinized insoluble calf skin collagen
-
?
UDPgalactose + procollagen 5-hydroxy-L-lysine
UDP + procollagen 5-(D-galactosyloxy)-L-lysine
-
gelatinized insoluble calf skin collagen
-
?
UDPgalactose + procollagen 5-hydroxy-L-lysine
UDP + procollagen 5-(D-galactosyloxy)-L-lysine
-
acceptor specificity: requires free epsilon-amino group in hydroxylysyl-residues
-
?
UDPgalactose + procollagen 5-hydroxy-L-lysine
UDP + procollagen 5-(D-galactosyloxy)-L-lysine
-
high specificity for galactosyl acceptor
-
?
UDPgalactose + procollagen 5-hydroxy-L-lysine
UDP + procollagen 5-(D-galactosyloxy)-L-lysine
-
denatured citrat-soluble rat skin collagen
-
?
UDPgalactose + procollagen 5-hydroxy-L-lysine
UDP + procollagen 5-(D-galactosyloxy)-L-lysine
-
denatured citrat-soluble rat skin collagen
beta-glycosidic bond
?
UDPgalactose + procollagen 5-hydroxy-L-lysine
UDP + procollagen 5-(D-galactosyloxy)-L-lysine
-
involved in collagen biosynthesis, post-translational modification, probably involved in synthesis of carbohydrate units in complement
-
-
?
UDPgalactose + procollagen 5-hydroxy-L-lysine
UDP + procollagen 5-(D-galactosyloxy)-L-lysine
-
-
-
?
UDPgalactose + procollagen 5-hydroxy-L-lysine
UDP + procollagen 5-(D-galactosyloxy)-L-lysine
-
acid-soluble calf skin collagen
-
?
UDPgalactose + procollagen 5-hydroxy-L-lysine
UDP + procollagen 5-(D-galactosyloxy)-L-lysine
-
fish collagen ichthyocol as best substrate, peptides derived from collagenase- and pronase-digestion of ichthyocol are less effective, native collagens from swim bladder or calf skin are more efficient substrates than collagen glycopeptides
-
?
UDPgalactose + procollagen 5-hydroxy-L-lysine
UDP + procollagen 5-(D-galactosyloxy)-L-lysine
-
bovine achilles tendon collagen with glucose and galactose residues removed
-
-
?
UDPgalactose + procollagen 5-hydroxy-L-lysine
UDP + procollagen 5-(D-galactosyloxy)-L-lysine
-
bovine glomerular basement membranes with carbohydrate units removed, native less effective
-
?
UDPgalactose + procollagen 5-hydroxy-L-lysine
UDP + procollagen 5-(D-galactosyloxy)-L-lysine
-
high specificity for specific hydroxylysine residues in collagen
-
-
?
UDPgalactose + procollagen 5-hydroxy-L-lysine
UDP + procollagen 5-(D-galactosyloxy)-L-lysine
-
high specificity for specific hydroxylysine residues in collagen
-
?
UDPgalactose + procollagen 5-hydroxy-L-lysine
UDP + procollagen 5-(D-galactosyloxy)-L-lysine
-
incorporation of monosaccharide precursors into the heterosaccharide chains of collagen
-
-
?
UDPgalactose + procollagen 5-hydroxy-L-lysine
UDP + procollagen 5-(D-galactosyloxy)-L-lysine
-
involved in collagen biosynthesis, post-translational modification, probably involved in synthesis of carbohydrate units in complement
-
-
?
UDPgalactose + procollagen 5-hydroxy-L-lysine
UDP + procollagen 5-(D-galactosyloxy)-L-lysine
-
-
-
-
?
UDPgalactose + procollagen 5-hydroxy-L-lysine
UDP + procollagen 5-(D-galactosyloxy)-L-lysine
-
involved in collagen biosynthesis, post-translational modification, probably involved in synthesis of carbohydrate units in complement
-
-
?
UDPgalactose + submaxillary glycoprotein with sialic acid removed
?
-
not porcine
-
-
?
UDPgalactose + submaxillary glycoprotein with sialic acid removed
?
-
bovine submaxillary glycoprotein with sialic acid removed, 9.5% of activity with achilles tendon collagen with glucose and galactose residues removed
-
-
?
additional information
?
-
-
no sugar donor: UDPglucose
-
-
?
additional information
?
-
-
no acceptors: galactose, glucose, glucosamine, N-acetylgalactosamine, lysine, hydroxyproline, threonine, serine, fetuin, native guinea pig collagen, glucose-free guinea pig skin collagen, native alpha1-glycoprotein
-
-
?
additional information
?
-
-
no acceptor: free hydroxylysine
-
-
?
additional information
?
-
-
no acceptor: free hydroxylysine
-
-
?
additional information
?
-
-
no sugar donors: UDPxylose, GDPmannose, GDPfucose
-
-
?
additional information
?
-
-
no acceptor: native collagen
-
-
?
additional information
?
-
-
free thiol groups in the active centre
-
-
?
additional information
?
-
-
no acceptor: galactosylhydroxylysine
-
-
?
additional information
?
-
-
no acceptor: free hydroxylysine
-
-
?
additional information
?
-
-
no acceptor: free hydroxylysine
-
-
?
additional information
?
-
-
no acceptor: free hydroxylysine
-
-
?
additional information
?
-
-
intracellular post-translational modification in collagen biosynthesis
-
-
?
additional information
?
-
-
collagen biosynthesis
-
-
?
additional information
?
-
-
no sugar donors: ADP-glucose, UDP-N-acetylglucosamine, UDP-N-acetylgalactosamine
-
-
?
additional information
?
-
-
no sugar donor: UDPglucose
-
-
?
additional information
?
-
-
no acceptor: thyroglobulin unit B
-
-
?
additional information
?
-
-
no acceptors: transferrin, native fetuin
-
-
?
additional information
?
-
-
no acceptor: free hydroxylysine
-
-
?
additional information
?
-
-
no acceptor: free hydroxylysine
-
-
?
additional information
?
-
-
intracellular post-translational modification in collagen biosynthesis
-
-
?
additional information
?
-
-
LH3 is the only enzyme capable of glucosylating the galactosylhydroxylysine residues in proteins with a collagenous domain
-
-
?
additional information
?
-
-
no acceptor: free hydroxylysine
-
-
?