Any feedback?
Information on EC 2.4.1.66 - procollagen glucosyltransferase
for references in articles please use BRENDA:EC2.4.1.66Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
2.4.1.66 procollagen glucosyltransferaseIUBMB Comments
Involved in the synthesis of carbohydrate units in the complement system (cf. EC 2.4.1.50 procollagen galactosyltransferase).
Specify your search results
Word Map
- 2.4.1.66
-
prolyl
- gg
-
4-hydroxylase
-
galactosyltransferase
- propeptide
- soleus
-
aminoterminal
- hyp
- tibialis
- 4-hydroxyproline
-
chick-embryo
The enzyme appears in viruses and cellular organisms
Reaction Schemes
Synonyms
galactosylhydroxylysyl glucosyltransferase, collagen glucosyltransferase, galactosylhydroxylysine glucosyltransferase, 
more
topPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
collagen glucosyltransferase
-
-
-
-
collagen hydroxylysyl glucosyltransferase
-
-
-
-
galactosylhydroxylysyl glucosyltransferase
GGT
-
-
-
-
glucosyltransferase, uridine diphosphoglucose-collagen
-
-
-
-
LH3
lysyl hydroxylase 3
PLOD3
UDP-glucose-collagen glucosyltransferase
-
-
-
-
UDP-glucose:galactosylhydroxylysine-collagen glucosyltransferase
-
-
-
-
uridine diphosphoglucose-collagen glucosyltransferase
-
-
-
-
additional information
galactosylhydroxylysyl glucosyltransferase
-
-
-
-
lysyl hydroxylase 3
-
a multifunctional protein with lysyl hydroxylase, collagen galactosyltransferase and glucosyltransferase activities
lysyl hydroxylase 3
-
(LH3) is a multifunctional enzyme possessing lysyl hydroxylase (LH), hydroxylysyl galactosyltransferase (GT) and galactosylhydroxylysyl glucosyltransferase (GGT) activities in vitro
lysyl hydroxylase 3
-
a multifunctional collagen-modifying enzyme possessing lysyl hydroxylase, hydroxylysine galactosyltransferase, and galactosylhydroxylysine-glucosyltransferase activities
lysyl hydroxylase 3
-
multifunctional enzyme that possesses galactosylhydroxylysine glucosyltransferase activity
additional information
-
GGT activity is associated with lysyl hydroxylase, LH
additional information
-
GGT activity is associated with lysyl hydroxylase, LH
additional information
-
GGT activity is associated with lysyl hydroxylase isoform 3, LH3, EC 1.14.11.4
additional information
-
GGT activity is associated with lysyl hydroxylase isoform 3, LH3, EC 1.14.11.4
additional information
-
GGT activity is associated with lysyl hydroxylase isoform 3, LH3, EC 1.14.11.4
additional information
GGT activity is associated with lysyl hydroxylase isoform 3, LH3, EC 1.14.11.4
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
UDP-alpha-D-glucose + [procollagen]-(5R)-5-O-(beta-D-galactosyl)-5-hydroxy-L-lysine = UDP + [procollagen]-(5R)-5-O-[alpha-D-glucosyl-(1->2)-beta-D-galactosyl]-5-hydroxy-L-lysine
UDP-alpha-D-glucose + [procollagen]-(5R)-5-O-(beta-D-galactosyl)-5-hydroxy-L-lysine = UDP + [procollagen]-(5R)-5-O-[alpha-D-glucosyl-(1->2)-beta-D-galactosyl]-5-hydroxy-L-lysine
sequential ordered mechanism
-
UDP-alpha-D-glucose + [procollagen]-(5R)-5-O-(beta-D-galactosyl)-5-hydroxy-L-lysine = UDP + [procollagen]-(5R)-5-O-[alpha-D-glucosyl-(1->2)-beta-D-galactosyl]-5-hydroxy-L-lysine
reaction mechanism
-
UDP-alpha-D-glucose + [procollagen]-(5R)-5-O-(beta-D-galactosyl)-5-hydroxy-L-lysine = UDP + [procollagen]-(5R)-5-O-[alpha-D-glucosyl-(1->2)-beta-D-galactosyl]-5-hydroxy-L-lysine
reaction mechanism
-
UDP-alpha-D-glucose + [procollagen]-(5R)-5-O-(beta-D-galactosyl)-5-hydroxy-L-lysine = UDP + [procollagen]-(5R)-5-O-[alpha-D-glucosyl-(1->2)-beta-D-galactosyl]-5-hydroxy-L-lysine
ordered mechanism
-
UDP-alpha-D-glucose + [procollagen]-(5R)-5-O-(beta-D-galactosyl)-5-hydroxy-L-lysine = UDP + [procollagen]-(5R)-5-O-[alpha-D-glucosyl-(1->2)-beta-D-galactosyl]-5-hydroxy-L-lysine
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hexosyl group transfer
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PATHWAY SOURCE
PATHWAYS
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYSTEMATIC NAME
IUBMB Comments
UDP-glucose:(2S,5R)-5-O-(beta-D-galactosyl)-5-hydroxy-L-lysine-[procollagen] D-glucosyltransferase
Involved in the synthesis of carbohydrate units in the complement system (cf. EC 2.4.1.50 procollagen galactosyltransferase).
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CAS REGISTRY NUMBER
COMMENTARY
9028-08-4
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
TDP-glucose + D-galactosylhydroxylysine
TDP + 1,2-D-glucosyl-D-galactosylhydroxylysine
-
soluble enzyme, glucosylation at 60% of the rate of UDP-glucose
-
?
UDP-alpha-D-glucose + galactosylhydroxylysyl residues in a calf skin gelatin
UDP + glucosylgalactosylhydroxylysyl residues in a calf skin gelatin
-
-
-
-
?
UDP-alpha-D-glucose + [procollagen]-(5R)-5-O-(beta-D-galactosyl)-5-hydroxy-L-lysine
UDP + [procollagen]-(5R)-5-O-[alpha-D-glucosyl-(1->2)-beta-D-galactosyl]-5-hydroxy-L-lysine
UDP-glucose + (2S,5R)-5-O-(beta-D-galactosyl)-5-hydroxy-L-lysine-[procollagen]
UDP + (2S,5R)-5-O-[alpha-D-glucosyl-(1->2)-beta-D-galactosyl]-5-hydroxy-L-lysine-[procollagen]
-
-
-
-
?
UDP-glucose + 5-(D-galactosyloxy)-L-lysine-procollagen
UDP + 1,2-D-glucosyl-5-D-(galactosyloxy)-L-lysine-procollagen
UDP-glucose + ichthyocol
?
-
fish collagen prepared from carp swim bladder, ichthyocol glycopeptides prepared by collagenase digestion are better substrates than native ichthyocol, better substrate than calf skin collagen
-
-
?
UDP-glucose + transferrin minus Fe3+ and sialic acid
?
-
7% as effective as glucose-free bovine Achilles tendon collagen
-
-
?
UDP-alpha-D-glucose + [procollagen]-(5R)-5-O-(beta-D-galactosyl)-5-hydroxy-L-lysine
UDP + [procollagen]-(5R)-5-O-[alpha-D-glucosyl-(1->2)-beta-D-galactosyl]-5-hydroxy-L-lysine
-
-
-
?
UDP-alpha-D-glucose + [procollagen]-(5R)-5-O-(beta-D-galactosyl)-5-hydroxy-L-lysine
UDP + [procollagen]-(5R)-5-O-[alpha-D-glucosyl-(1->2)-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
-
-
?
UDP-glucose + 5-(D-galactosyloxy)-L-lysine-procollagen
UDP + 1,2-D-glucosyl-5-D-(galactosyloxy)-L-lysine-procollagen
-
highly specific
-
-
?
UDP-glucose + 5-(D-galactosyloxy)-L-lysine-procollagen
UDP + 1,2-D-glucosyl-5-D-(galactosyloxy)-L-lysine-procollagen
-
acceptor specificity
-
-
?
UDP-glucose + 5-(D-galactosyloxy)-L-lysine-procollagen
UDP + 1,2-D-glucosyl-5-D-(galactosyloxy)-L-lysine-procollagen
-
requires UDP-glucose as glucosyl donor and acceptor protein with terminal galactose residues
-
-
?
UDP-glucose + 5-(D-galactosyloxy)-L-lysine-procollagen
UDP + 1,2-D-glucosyl-5-D-(galactosyloxy)-L-lysine-procollagen
-
acetic acid-soluble collagen from alkali-treated calf arterial tissue
-
-
?
UDP-glucose + 5-(D-galactosyloxy)-L-lysine-procollagen
UDP + 1,2-D-glucosyl-5-D-(galactosyloxy)-L-lysine-procollagen
-
absolute requirement: free epsilon-amino group in hydroxylysyl-residues
-
-
?
UDP-glucose + 5-(D-galactosyloxy)-L-lysine-procollagen
UDP + 1,2-D-glucosyl-5-D-(galactosyloxy)-L-lysine-procollagen
-
denatured citrate-soluble calf skin collagen is the best substrate, its alpha1-chain and beta12-component are also acceptors, but with lower affinity
-
-
?
UDP-glucose + 5-(D-galactosyloxy)-L-lysine-procollagen
UDP + 1,2-D-glucosyl-5-D-(galactosyloxy)-L-lysine-procollagen
-
involved in collagen biosynthesis
-
-
?
UDP-glucose + 5-(D-galactosyloxy)-L-lysine-procollagen
UDP + 1,2-D-glucosyl-5-D-(galactosyloxy)-L-lysine-procollagen
-
glycosylation in the course of procollagen and collagen biosynthesis, carbohydrate attachment is an essential step in the protocollagen biosynthesis, postribosomal modification
-
-
?
UDP-glucose + 5-(D-galactosyloxy)-L-lysine-procollagen
UDP + 1,2-D-glucosyl-5-D-(galactosyloxy)-L-lysine-procollagen
-
calf skin gelatin
-
?
UDP-glucose + 5-(D-galactosyloxy)-L-lysine-procollagen
UDP + 1,2-D-glucosyl-5-D-(galactosyloxy)-L-lysine-procollagen
-
calf skin gelatin
product is glucosylgalactosylhydroxylysine-collagen
?
UDP-glucose + 5-(D-galactosyloxy)-L-lysine-procollagen
UDP + 1,2-D-glucosyl-5-D-(galactosyloxy)-L-lysine-procollagen
-
posttranslational modification of collagen
-
-
?
UDP-glucose + 5-(D-galactosyloxy)-L-lysine-procollagen
UDP + 1,2-D-glucosyl-5-D-(galactosyloxy)-L-lysine-procollagen
-
highly specific
-
-
?
UDP-glucose + 5-(D-galactosyloxy)-L-lysine-procollagen
UDP + 1,2-D-glucosyl-5-D-(galactosyloxy)-L-lysine-procollagen
-
acceptor specificity
-
-
?
UDP-glucose + 5-(D-galactosyloxy)-L-lysine-procollagen
UDP + 1,2-D-glucosyl-5-D-(galactosyloxy)-L-lysine-procollagen
-
tendon collagen
-
-
?
UDP-glucose + 5-(D-galactosyloxy)-L-lysine-procollagen
UDP + 1,2-D-glucosyl-5-D-(galactosyloxy)-L-lysine-procollagen
-
citrate-soluble guinea pig skin collagen
-
-
?
UDP-glucose + 5-(D-galactosyloxy)-L-lysine-procollagen
UDP + 1,2-D-glucosyl-5-D-(galactosyloxy)-L-lysine-procollagen
-
calf skin collagen
-
-
?
UDP-glucose + 5-(D-galactosyloxy)-L-lysine-procollagen
UDP + 1,2-D-glucosyl-5-D-(galactosyloxy)-L-lysine-procollagen
-
absolute requirement: free epsilon-amino group in hydroxylysyl-residues
-
-
?
UDP-glucose + 5-(D-galactosyloxy)-L-lysine-procollagen
UDP + 1,2-D-glucosyl-5-D-(galactosyloxy)-L-lysine-procollagen
-
non-functional substrates, such as alpha1-glycoprotein and fetuin can replace collagen to some extent
-
-
?
UDP-glucose + 5-(D-galactosyloxy)-L-lysine-procollagen
UDP + 1,2-D-glucosyl-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
-
-
?
UDP-glucose + 5-(D-galactosyloxy)-L-lysine-procollagen
UDP + 1,2-D-glucosyl-5-D-(galactosyloxy)-L-lysine-procollagen
-
involved in collagen biosynthesis
-
-
?
UDP-glucose + 5-(D-galactosyloxy)-L-lysine-procollagen
UDP + 1,2-D-glucosyl-5-D-(galactosyloxy)-L-lysine-procollagen
-
highly specific
-
?
UDP-glucose + 5-(D-galactosyloxy)-L-lysine-procollagen
UDP + 1,2-D-glucosyl-5-D-(galactosyloxy)-L-lysine-procollagen
-
acceptor specificity
-
?
UDP-glucose + 5-(D-galactosyloxy)-L-lysine-procollagen
UDP + 1,2-D-glucosyl-5-D-(galactosyloxy)-L-lysine-procollagen
-
acceptor specificity
product is glucosylgalactosylhydroxylysine-collagen
?
UDP-glucose + 5-(D-galactosyloxy)-L-lysine-procollagen
UDP + 1,2-D-glucosyl-5-D-(galactosyloxy)-L-lysine-procollagen
-
high specificity for galactosylhydroxylysine
product is glucosylgalactosylhydroxylysine-collagen
?
UDP-glucose + 5-(D-galactosyloxy)-L-lysine-procollagen
UDP + 1,2-D-glucosyl-5-D-(galactosyloxy)-L-lysine-procollagen
-
peptides prepared by collagenase-digestion from bovine Achilles tendon collagen
-
-
?
UDP-glucose + 5-(D-galactosyloxy)-L-lysine-procollagen
UDP + 1,2-D-glucosyl-5-D-(galactosyloxy)-L-lysine-procollagen
-
peptides prepared by collagenase-digestion from bovine Achilles tendon collagen
product is glucosylgalactosylhydroxylysine-collagen
?
UDP-glucose + 5-(D-galactosyloxy)-L-lysine-procollagen
UDP + 1,2-D-glucosyl-5-D-(galactosyloxy)-L-lysine-procollagen
-
peptides prepared from citrate-soluble rat skin collagen
-
-
?
UDP-glucose + 5-(D-galactosyloxy)-L-lysine-procollagen
UDP + 1,2-D-glucosyl-5-D-(galactosyloxy)-L-lysine-procollagen
-
ordered binding of Mn2+, UDP-glucose and collagen at low Mn2+ concentration and of two Mn2+, UDP-glucose and collagen at high Mn2+ concentration
-
?
UDP-glucose + 5-(D-galactosyloxy)-L-lysine-procollagen
UDP + 1,2-D-glucosyl-5-D-(galactosyloxy)-L-lysine-procollagen
-
ordered binding of Mn2+, UDP-glucose and collagen at low Mn2+ concentration and of two Mn2+, UDP-glucose and collagen at high Mn2+ concentration
product is glucosylgalactosylhydroxylysine-collagen
?
UDP-glucose + 5-(D-galactosyloxy)-L-lysine-procollagen
UDP + 1,2-D-glucosyl-5-D-(galactosyloxy)-L-lysine-procollagen
-
heat-denatured citrate-soluble rat skin collagen
-
?
UDP-glucose + 5-(D-galactosyloxy)-L-lysine-procollagen
UDP + 1,2-D-glucosyl-5-D-(galactosyloxy)-L-lysine-procollagen
-
heat-denatured citrate-soluble rat skin collagen
-
-
?
UDP-glucose + 5-(D-galactosyloxy)-L-lysine-procollagen
UDP + 1,2-D-glucosyl-5-D-(galactosyloxy)-L-lysine-procollagen
-
heat-denatured citrate-soluble rat skin collagen
product is glucosylgalactosylhydroxylysine-collagen
?
UDP-glucose + 5-(D-galactosyloxy)-L-lysine-procollagen
UDP + 1,2-D-glucosyl-5-D-(galactosyloxy)-L-lysine-procollagen
-
heat-denatured citrate-soluble rat skin collagen
product is glucosylgalactosylhydroxylysine-collagen
?
UDP-glucose + 5-(D-galactosyloxy)-L-lysine-procollagen
UDP + 1,2-D-glucosyl-5-D-(galactosyloxy)-L-lysine-procollagen
-
heat-denatured citrate-soluble rat skin collagen
product is glucosylgalactosylhydroxylysine-collagen
?
UDP-glucose + 5-(D-galactosyloxy)-L-lysine-procollagen
UDP + 1,2-D-glucosyl-5-D-(galactosyloxy)-L-lysine-procollagen
-
heat-denatured gelatinized calf skin collagen
-
?
UDP-glucose + 5-(D-galactosyloxy)-L-lysine-procollagen
UDP + 1,2-D-glucosyl-5-D-(galactosyloxy)-L-lysine-procollagen
-
specific for collagen
-
-
?
UDP-glucose + 5-(D-galactosyloxy)-L-lysine-procollagen
UDP + 1,2-D-glucosyl-5-D-(galactosyloxy)-L-lysine-procollagen
-
specific for collagen
product is glucosylgalactosylhydroxylysine-collagen
?
UDP-glucose + 5-(D-galactosyloxy)-L-lysine-procollagen
UDP + 1,2-D-glucosyl-5-D-(galactosyloxy)-L-lysine-procollagen
-
absolute requirement: free epsilon-amino group in hydroxylysyl-residues
-
?
UDP-glucose + 5-(D-galactosyloxy)-L-lysine-procollagen
UDP + 1,2-D-glucosyl-5-D-(galactosyloxy)-L-lysine-procollagen
-
calf skin gelatin
-
-
?
UDP-glucose + 5-(D-galactosyloxy)-L-lysine-procollagen
UDP + 1,2-D-glucosyl-5-D-(galactosyloxy)-L-lysine-procollagen
-
calf skin gelatin
product is glucosylgalactosylhydroxylysine-collagen
?
UDP-glucose + 5-(D-galactosyloxy)-L-lysine-procollagen
UDP + 1,2-D-glucosyl-5-D-(galactosyloxy)-L-lysine-procollagen
-
calf skin gelatin
product is glucosylgalactosylhydroxylysine-collagen
?
UDP-glucose + 5-(D-galactosyloxy)-L-lysine-procollagen
UDP + 1,2-D-glucosyl-5-D-(galactosyloxy)-L-lysine-procollagen
-
calf skin gelatin
product is glucosylgalactosylhydroxylysine-collagen
?
UDP-glucose + 5-(D-galactosyloxy)-L-lysine-procollagen
UDP + 1,2-D-glucosyl-5-D-(galactosyloxy)-L-lysine-procollagen
-
sequential ordered mechanism, substrates are bound in the following order: Mn2+, collagen and UDP-glucose
-
-
?
UDP-glucose + 5-(D-galactosyloxy)-L-lysine-procollagen
UDP + 1,2-D-glucosyl-5-D-(galactosyloxy)-L-lysine-procollagen
-
requires enzyme-Mn2+ for the binding of the substrate and co-substrate
-
-
?
UDP-glucose + 5-(D-galactosyloxy)-L-lysine-procollagen
UDP + 1,2-D-glucosyl-5-D-(galactosyloxy)-L-lysine-procollagen
-
involved in collagen biosynthesis
-
-
?
UDP-glucose + 5-(D-galactosyloxy)-L-lysine-procollagen
UDP + 1,2-D-glucosyl-5-D-(galactosyloxy)-L-lysine-procollagen
-
intracellular enzyme of collagen biosynthesis
-
-
?
UDP-glucose + 5-(D-galactosyloxy)-L-lysine-procollagen
UDP + 1,2-D-glucosyl-5-D-(galactosyloxy)-L-lysine-procollagen
-
-
-
-
?
UDP-glucose + 5-(D-galactosyloxy)-L-lysine-procollagen
UDP + 1,2-D-glucosyl-5-D-(galactosyloxy)-L-lysine-procollagen
-
highly specific
-
?
UDP-glucose + 5-(D-galactosyloxy)-L-lysine-procollagen
UDP + 1,2-D-glucosyl-5-D-(galactosyloxy)-L-lysine-procollagen
-
acceptor specificity
-
?
UDP-glucose + 5-(D-galactosyloxy)-L-lysine-procollagen
UDP + 1,2-D-glucosyl-5-D-(galactosyloxy)-L-lysine-procollagen
-
acetic acid-soluble bovine tendon collagen
product is glucosylgalactosylhydroxylysine-collagen
?
UDP-glucose + 5-(D-galactosyloxy)-L-lysine-procollagen
UDP + 1,2-D-glucosyl-5-D-(galactosyloxy)-L-lysine-procollagen
-
galactosylhydroxylysine bound in purified alpha1-chain of chicken skin collagen
product is glucosylgalactosylhydroxylysine-collagen
?
UDP-glucose + 5-(D-galactosyloxy)-L-lysine-procollagen
UDP + 1,2-D-glucosyl-5-D-(galactosyloxy)-L-lysine-procollagen
-
calf skin collagen
product is glucosylgalactosylhydroxylysine-collagen
?
UDP-glucose + 5-(D-galactosyloxy)-L-lysine-procollagen
UDP + 1,2-D-glucosyl-5-D-(galactosyloxy)-L-lysine-procollagen
-
heat-denatured citrate-soluble rat skin collagen
-
?
UDP-glucose + 5-(D-galactosyloxy)-L-lysine-procollagen
UDP + 1,2-D-glucosyl-5-D-(galactosyloxy)-L-lysine-procollagen
-
heat-denatured citrate-soluble rat skin collagen
-
-
?
UDP-glucose + 5-(D-galactosyloxy)-L-lysine-procollagen
UDP + 1,2-D-glucosyl-5-D-(galactosyloxy)-L-lysine-procollagen
-
specific for collagen
product is glucosylgalactosylhydroxylysine-collagen
?
UDP-glucose + 5-(D-galactosyloxy)-L-lysine-procollagen
UDP + 1,2-D-glucosyl-5-D-(galactosyloxy)-L-lysine-procollagen
-
absolute requirement: free epsilon-amino group in hydroxylysyl-residues
-
?
UDP-glucose + 5-(D-galactosyloxy)-L-lysine-procollagen
UDP + 1,2-D-glucosyl-5-D-(galactosyloxy)-L-lysine-procollagen
-
enzyme recognizes probably not only the carbohydrate side chains but also the primary structure of collagen
product is glucosylgalactosylhydroxylysine-collagen
?
UDP-glucose + 5-(D-galactosyloxy)-L-lysine-procollagen
UDP + 1,2-D-glucosyl-5-D-(galactosyloxy)-L-lysine-procollagen
-
calf skin gelatin
-
?
UDP-glucose + 5-(D-galactosyloxy)-L-lysine-procollagen
UDP + 1,2-D-glucosyl-5-D-(galactosyloxy)-L-lysine-procollagen
-
calf skin gelatin
product is glucosylgalactosylhydroxylysine-collagen
?
UDP-glucose + 5-(D-galactosyloxy)-L-lysine-procollagen
UDP + 1,2-D-glucosyl-5-D-(galactosyloxy)-L-lysine-procollagen
-
calf skin gelatin
product is glucosylgalactosylhydroxylysine-collagen
?
UDP-glucose + 5-(D-galactosyloxy)-L-lysine-procollagen
UDP + 1,2-D-glucosyl-5-D-(galactosyloxy)-L-lysine-procollagen
-
glucosyl-acceptors: ichthyocol, ichthyocol glycopeptides obtained by collagenase digestion, bovine glomerular basement membrane
product is glucosylgalactosylhydroxylysine-collagen
?
UDP-glucose + 5-(D-galactosyloxy)-L-lysine-procollagen
UDP + 1,2-D-glucosyl-5-D-(galactosyloxy)-L-lysine-procollagen
-
incomplete hexasaccharide chains of bovine Achilles tendon collagen, glucosyl residues removed by mild acid hydrolysis
product is glucosylgalactosylhydroxylysine-collagen
?
UDP-glucose + 5-(D-galactosyloxy)-L-lysine-procollagen
UDP + 1,2-D-glucosyl-5-D-(galactosyloxy)-L-lysine-procollagen
-
involved in collagen biosynthesis
-
-
?
UDP-glucose + 5-(D-galactosyloxy)-L-lysine-procollagen
UDP + 1,2-D-glucosyl-5-D-(galactosyloxy)-L-lysine-procollagen
-
may play a major role in the mechanism of platelet:collagen adhesion
-
-
?
UDP-glucose + 5-(D-galactosyloxy)-L-lysine-procollagen
UDP + 1,2-D-glucosyl-5-D-(galactosyloxy)-L-lysine-procollagen
-
posttranslational modification of collagen
-
-
?
UDP-glucose + 5-(D-galactosyloxy)-L-lysine-procollagen
UDP + 1,2-D-glucosyl-5-D-(galactosyloxy)-L-lysine-procollagen
-
together with EC 2.4.1.50 involved in biosynthesis of glucosylgalactosylhydroxylysine units in collagens, basement membranes and certain serum glycoproteins
-
-
?
UDP-glucose + 5-(D-galactosyloxy)-L-lysine-procollagen
UDP + 1,2-D-glucosyl-5-D-(galactosyloxy)-L-lysine-procollagen
-
-
-
-
?
UDP-glucose + 5-(D-galactosyloxy)-L-lysine-procollagen
UDP + 1,2-D-glucosyl-5-D-(galactosyloxy)-L-lysine-procollagen
-
highly specific
-
?
UDP-glucose + 5-(D-galactosyloxy)-L-lysine-procollagen
UDP + 1,2-D-glucosyl-5-D-(galactosyloxy)-L-lysine-procollagen
-
acceptor specificity
-
?
UDP-glucose + 5-(D-galactosyloxy)-L-lysine-procollagen
UDP + 1,2-D-glucosyl-5-D-(galactosyloxy)-L-lysine-procollagen
-
heat-denatured gelatinized calf skin collagen
-
?
UDP-glucose + 5-(D-galactosyloxy)-L-lysine-procollagen
UDP + 1,2-D-glucosyl-5-D-(galactosyloxy)-L-lysine-procollagen
-
heat-denatured gelatinized calf skin collagen
product is glucosylgalactosylhydroxylysine-collagen
?
UDP-glucose + 5-(D-galactosyloxy)-L-lysine-procollagen
UDP + 1,2-D-glucosyl-5-D-(galactosyloxy)-L-lysine-procollagen
-
absolute requirement: free epsilon-amino group in hydroxylysyl-residues
-
?
UDP-glucose + 5-(D-galactosyloxy)-L-lysine-procollagen
UDP + 1,2-D-glucosyl-5-D-(galactosyloxy)-L-lysine-procollagen
-
calf skin gelatin
-
-
?
UDP-glucose + 5-(D-galactosyloxy)-L-lysine-procollagen
UDP + 1,2-D-glucosyl-5-D-(galactosyloxy)-L-lysine-procollagen
-
involved in collagen biosynthesis
-
-
?
UDP-glucose + 5-(D-galactosyloxy)-L-lysine-procollagen
UDP + 1,2-D-glucosyl-5-D-(galactosyloxy)-L-lysine-procollagen
-
posttranslational modification of collagen
-
-
?
UDP-glucose + 5-(D-galactosyloxy)-L-lysine-procollagen
UDP + 1,2-D-glucosyl-5-D-(galactosyloxy)-L-lysine-procollagen
-
marker enzyme of collagen biosynthesis
-
-
?
UDP-glucose + asialo alpha 1-glycoprotein
?
-
sialic acid-free alpha1-acid glycoprotein of human serum, 1/50 of affinity of citrate-soluble calf skin collagen
-
-
?
UDP-glucose + asialo alpha 1-glycoprotein
?
-
non-functional substrates, such as alpha1-glycoprotein and fetuin can replace collagen to some extent, poor substrate
-
-
?
UDP-glucose + D-galactosylhydroxylysine
UDP + 1,2-D-glucosyl-D-galactosylhydroxylysine
-
in vitro
-
-
?
UDP-glucose + D-galactosylhydroxylysine
UDP + 1,2-D-glucosyl-D-galactosylhydroxylysine
-
in vitro
-
?
UDP-glucose + D-galactosylhydroxylysine
UDP + 1,2-D-glucosyl-D-galactosylhydroxylysine
-
good substrate
-
?
UDP-glucose + D-galactosylhydroxylysine
UDP + 1,2-D-glucosyl-D-galactosylhydroxylysine
-
in vitro
-
-
?
UDP-glucose + D-galactosylhydroxylysine
UDP + 1,2-D-glucosyl-D-galactosylhydroxylysine
-
in vitro
-
?
UDP-glucose + D-galactosylhydroxylysine
UDP + 1,2-D-glucosyl-D-galactosylhydroxylysine
-
in vitro
-
?
UDP-glucose + D-galactosylhydroxylysine
UDP + 1,2-D-glucosyl-D-galactosylhydroxylysine
-
in vitro
-
?
UDP-glucose + D-galactosylhydroxylysine
UDP + 1,2-D-glucosyl-D-galactosylhydroxylysine
-
galactosylhydroxylysine purified from marine sponge collagen
-
?
UDP-glucose + D-galactosylsphingosine
UDP + 1,2-D-glucosyl-D-galactosylsphingosine
-
in vitro
-
-
?
UDP-glucose + D-galactosylsphingosine
UDP + 1,2-D-glucosyl-D-galactosylsphingosine
-
in vitro
-
?
UDP-glucose + D-galactosylsphingosine
UDP + 1,2-D-glucosyl-D-galactosylsphingosine
-
good acceptor
-
-
?
UDP-glucose + fetuin minus sialic acid, galactose and N-acetylglucosamine
?
-
non-functional substrates, such as alpha1-glycoprotein minus sialic acid and fetuin can replace collagen to some extent, poor substrate, fetuin minus sialic acid and galactose is a better substrate than fetuin
-
-
?
UDP-glucose + fetuin minus sialic acid, galactose and N-acetylglucosamine
?
-
7% as effective as glucose-free bovine Achilles tendon collagen
-
-
?
additional information
?
-
-
lysyl hydroxylase and collagen glucosyltransferase activities are associated with the same gene product, the amino acids important for the GGT activity are located in the N-terminal part of LH/GGT protein separate from the C-terminal LH active site, C-132 and L-196 are important for the catalytic activity of GGT
-
-
?
additional information
?
-
-
multifunctional lysyl hydroxylase possesses lysyl hydroxylase, collagen glucosyltransferase and galactosyltransferase activities
-
-
?
additional information
?
-
-
not: porcine submaxillary glycoprotein, galactose, galactosamine, N-acetylgalactosamine
-
-
?
additional information
?
-
-
not: UDP-N-acetylglucosamine and UDP-N-acetylgalactosamine
-
-
?
additional information
?
-
-
not: casein, chondroitin sulfate, ovomucoid, alpha1-glycoprotein, alpha-lactalbumin, thyroglobulin
-
-
?
additional information
?
-
-
no substrates: hydroxylysyl- or glucosylgalactosyl hydroxylysyl-residues
-
-
?
additional information
?
-
-
the amino acids important for the GGT activity are located in the N-terminal part of LH3/GGT protein separate from the C-terminal LH active site
-
-
?
additional information
?
-
-
the amino acids important for the GGT activity are located in the N-terminal part of LH3/GGT protein separate from the C-terminal LH active site
-
-
?
additional information
?
-
-
multifunctional lysyl hydroxylase isoform 3, LH3 protein, possesses lysyl hydroxylase, collagen glucosyltransferase and galactosyltransferase activities
-
-
?
additional information
?
-
-
multifunctional lysyl hydroxylase isoform 3, LH3 protein, possesses lysyl hydroxylase, collagen glucosyltransferase and galactosyltransferase activities
-
-
?
additional information
?
-
-
multifunctional lysyl hydroxylase isoform 3, LH3 protein, possesses lysyl hydroxylase and collagen glucosyltransferase activities
-
-
?
additional information
?
-
-
GGT and GT activities reside in the N-terminal 30.4 kDa structural domain fragment A of LH3, which plays no role in hydroxylase activity, only trace amounts of GT activity of LH3
-
-
?
additional information
?
-
-
C-144 and L-208 are important for the catalytic activity of GGT, DXD-like motif is required for activity, no GGT activity in LH1 and LH2
-
-
?
additional information
?
-
-
not: glucose free bovine glomerular basement membranes, calf thyroglobulin, galactose
-
-
?
additional information
?
-
-
not: bovine and ovine submaxillary glycoprotein, ovalbumin, ceruloplasmin, human albumin, fibrinogen, haptoglobin, deaminated collagen, very poor glucosyl donors: UDPgalactose, ADPglucose
-
-
?
additional information
?
-
-
there must be an additional glucosyltransferase to LH3 that is responsible for most of the collagen glucosylation in vivo
-
-
?
additional information
?
-
-
lysyl hydroxylase 3 is a post-translational modification enzyme with lysyl hydroxylase collagen galactosyltransferase, and glucosyltransferase activities
-
-
?
additional information
?
-
-
the enzyme displays lysyl hydroxylase as well as galactosyl- and glucosyltransferase activity
-
-
?
additional information
?
-
multifunctional lysyl hydroxylase isoform 3, LH3 protein, possesses lysyl hydroxylase and collagen glucosyltransferase activities
-
-
?
additional information
?
-
-
multifunctional lysyl hydroxylase isoform 3, LH3 protein, possesses lysyl hydroxylase and collagen glucosyltransferase activities
-
-
?
additional information
?
-
-
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
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
UDP-alpha-D-glucose + [procollagen]-(5R)-5-O-(beta-D-galactosyl)-5-hydroxy-L-lysine
UDP + [procollagen]-(5R)-5-O-[alpha-D-glucosyl-(1->2)-beta-D-galactosyl]-5-hydroxy-L-lysine
-
-
-
?
UDP-glucose + (2S,5R)-5-O-(beta-D-galactosyl)-5-hydroxy-L-lysine-[procollagen]
UDP + (2S,5R)-5-O-[alpha-D-glucosyl-(1->2)-beta-D-galactosyl]-5-hydroxy-L-lysine-[procollagen]
-
-
-
-
?
UDP-glucose + 5-(D-galactosyloxy)-L-lysine-procollagen
UDP + 1,2-D-glucosyl-5-D-(galactosyloxy)-L-lysine-procollagen
UDP-glucose + 5-(D-galactosyloxy)-L-lysine-procollagen
UDP + 1,2-D-glucosyl-5-D-(galactosyloxy)-L-lysine-procollagen
-
involved in collagen biosynthesis
-
-
?
UDP-glucose + 5-(D-galactosyloxy)-L-lysine-procollagen
UDP + 1,2-D-glucosyl-5-D-(galactosyloxy)-L-lysine-procollagen
-
glycosylation in the course of procollagen and collagen biosynthesis, carbohydrate attachment is an essential step in the protocollagen biosynthesis, postribosomal modification
-
-
?
UDP-glucose + 5-(D-galactosyloxy)-L-lysine-procollagen
UDP + 1,2-D-glucosyl-5-D-(galactosyloxy)-L-lysine-procollagen
-
posttranslational modification of collagen
-
-
?
UDP-glucose + 5-(D-galactosyloxy)-L-lysine-procollagen
UDP + 1,2-D-glucosyl-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
-
-
?
UDP-glucose + 5-(D-galactosyloxy)-L-lysine-procollagen
UDP + 1,2-D-glucosyl-5-D-(galactosyloxy)-L-lysine-procollagen
-
involved in collagen biosynthesis
-
-
?
UDP-glucose + 5-(D-galactosyloxy)-L-lysine-procollagen
UDP + 1,2-D-glucosyl-5-D-(galactosyloxy)-L-lysine-procollagen
-
involved in collagen biosynthesis
-
-
?
UDP-glucose + 5-(D-galactosyloxy)-L-lysine-procollagen
UDP + 1,2-D-glucosyl-5-D-(galactosyloxy)-L-lysine-procollagen
-
intracellular enzyme of collagen biosynthesis
-
-
?
UDP-glucose + 5-(D-galactosyloxy)-L-lysine-procollagen
UDP + 1,2-D-glucosyl-5-D-(galactosyloxy)-L-lysine-procollagen
-
involved in collagen biosynthesis
-
-
?
UDP-glucose + 5-(D-galactosyloxy)-L-lysine-procollagen
UDP + 1,2-D-glucosyl-5-D-(galactosyloxy)-L-lysine-procollagen
-
may play a major role in the mechanism of platelet:collagen adhesion
-
-
?
UDP-glucose + 5-(D-galactosyloxy)-L-lysine-procollagen
UDP + 1,2-D-glucosyl-5-D-(galactosyloxy)-L-lysine-procollagen
-
posttranslational modification of collagen
-
-
?
UDP-glucose + 5-(D-galactosyloxy)-L-lysine-procollagen
UDP + 1,2-D-glucosyl-5-D-(galactosyloxy)-L-lysine-procollagen
-
together with EC 2.4.1.50 involved in biosynthesis of glucosylgalactosylhydroxylysine units in collagens, basement membranes and certain serum glycoproteins
-
-
?
UDP-glucose + 5-(D-galactosyloxy)-L-lysine-procollagen
UDP + 1,2-D-glucosyl-5-D-(galactosyloxy)-L-lysine-procollagen
-
involved in collagen biosynthesis
-
-
?
UDP-glucose + 5-(D-galactosyloxy)-L-lysine-procollagen
UDP + 1,2-D-glucosyl-5-D-(galactosyloxy)-L-lysine-procollagen
-
posttranslational modification of collagen
-
-
?
UDP-glucose + 5-(D-galactosyloxy)-L-lysine-procollagen
UDP + 1,2-D-glucosyl-5-D-(galactosyloxy)-L-lysine-procollagen
-
marker enzyme of collagen biosynthesis
-
-
?
additional information
?
-
-
there must be an additional glucosyltransferase to LH3 that is responsible for most of the collagen glucosylation in vivo
-
-
?
additional information
?
-
-
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
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
Co2+
Fe2+
Mg2+
Mn2+
additional information
Ca2+
-
Mn2+ is the most effective metal cofactor, partial replacement with Co2+, Mg2+ and Ca2+
Co2+
-
activates at low but inhibits at high concentrations, optimal concentration: 0.3 mM, 80% as effective as 0.01 mM Mn2+
Co2+
-
Mn2+ is the most effective metal cofactor, partial replacement with Co2+, Mg2+ and Ca2+, optimal concentration: 2.5 mM