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Information on EC 2.4.1.50 - procollagen galactosyltransferase and Organism(s) Homo sapiens and UniProt Accession Q8IYK4
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2.4.1.50 procollagen galactosyltransferaseIUBMB Comments
Involved in the synthesis of carbohydrate units in the complement system (cf. EC 2.4.1.66 procollagen glucosyltransferase).
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Word Map
- 2.4.1.50
-
glucosyltransferase
- laxity
- ehlers-danlos
-
spondyloepimetaphyseal
- b4galt7
-
chick-embryo
-
galactosylhydroxylysyl
-
b3gat3
-
linkeropathies
- hypermobility
-
hypermobl
-
spondylodysplastic
-
beighton
-
progeroid
- medicine
The taxonomic range for the selected organisms is: Homo sapiens
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Reaction Schemes
Synonyms
glt25d1, b3galt6, colgalt2, glt25d2, collagen galactosyltransferase, colgalt1, galactosyltransferase ii, hydroxylysyl galactosyltransferase, beta3galt6, hydroxylysine galactosyltransferase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
collagen galactosyltransferase
collagen hydroxylysyl galactosyltransferase
-
-
-
-
collagen hydroxylysyl glycosylsyltransferase
-
-
-
-
galactosyltransferase, uridine diphosphogalactose-collagen
-
-
-
-
hydroxylysine galactosyltransferase
-
-
-
-
LH3
lysyl hydroxylase 3
UDP galactose-collagen galactosyltransferase
-
-
-
-
UDPgalactose:5-hydroxylysine-collagen galactosyltransferase
-
-
-
-
uridine diphosphogalactose-collagen galactosyltransferase
-
-
-
-
collagen galactosyltransferase
-
-
-
-
lysyl hydroxylase 3
-
a multifunctional protein with lysyl hydroxylase, collagen galactosyltransferase and glucosyltransferase activities
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hexosyl group transfer
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
UDP-galactose:procollagen-5-hydroxy-L-lysine D-galactosyltransferase
Involved in the synthesis of carbohydrate units in the complement system (cf. EC 2.4.1.66 procollagen glucosyltransferase).
CAS REGISTRY NUMBER
COMMENTARY
9028-07-3
-
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
UDP-galactose + bovine collagen type I (deglycosylated)
UDP + ?
-
-
-
?
denatured collagen type I + UDP-alpha-D-galactose
UDP + galactosylated collagen type I
-
-
-
?
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 + 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
?
-
bovine submaxillary glycoprotein with sialic acid removed, 9.5% of activity with achilles tendon collagen with glucose and galactose residues removed
-
-
?
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
-
-
-
?
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
-
-
?
additional information
?
-
-
no sugar donors: ADP-glucose, UDP-N-acetylglucosamine, UDP-N-acetylgalactosamine
-
-
?
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
-
-
?
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-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
-
-
-
?
UDPgalactose + procollagen 5-hydroxy-L-lysine
UDP + procollagen 5-(D-galactosyloxy)-L-lysine
additional information
?
-
-
intracellular post-translational modification in collagen biosynthesis
-
-
?
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
-
-
-
?
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
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
Fe2+
contributes to the overall enzyme stabilization, enzymatic activity peaks at 25 microM Fe2+
Mg2+
Mn2+
additional information
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
not inhibited by Hg2+, acetylsalicylic acid, D-glucosamine, glutathione, ADP
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.028
calf skin collagen
-
value based on actual amount of galactosylhydroxylysyl-residues in calf skin collagen
-
0.28
ichthyocol
-
value based on actual amount of galactosylhydroxylysyl-residues in ichthyocol
-
additional information
additional information
KM-value 9.8 g/l for substrate bovine collagen type I (deglycosylated)
-
additional information
additional information
KM-value 9.8 g/l for substrate bovine collagen type I (deglycosylated)
-
additional information
additional information
-
KM-value 9.8 g/l for substrate bovine collagen type I (deglycosylated)
-
additional information
additional information
KM-value 13.6 g/l for substrate bovine collagen type I (deglycosylated)
-
additional information
additional information
KM-value 13.6 g/l for substrate bovine collagen type I (deglycosylated)
-
additional information
additional information
-
KM-value 13.6 g/l for substrate bovine collagen type I (deglycosylated)
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
blood platelet plasma membrane, may be buried in the interior of the membrane or located on its inner surface
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
loss of GLT25D2 has no effect on collagen secretion. Inactivation of the GLT25D1 gene results in a compensatory induction of isoform GLT25D2 expression. Cells harboring individually inactivated GLT25D1 and GLT25D2 genes can be recovered and maintained in culture, cell clones with simultaneously inactive GLT25D1 and GLT25D2 genes cannot be grown
malfunction
metabolism
physiological function
malfunction
-
disorders of LH3 with a unique phenotype causing severe morbidity as a result of feauters that overlap with collagen disorders
malfunction
enzyme knockdown in breast cancer cells inhibits local tissue invasion
metabolism
procollagen lysyl hydroxylase 2 is required for the biogenesis of collagen
metabolism
-
the enzyme is commonly involved in biosynthesis of collagenous proteins
physiological function
-
forms part of the many posttranslational modifications required during collagen biosynthesis
physiological function
procollagen lysyl hydroxylase 2 is essential for hypoxia-induced breast cancer metastasis. The enzyme is critical for fibrillary collagen formation by breast cancer cells, increases tumor stiffness, and is required for metastasis to lymph nodes and lungs
physiological function
knockdown of GLT25D1 HEK cells modified for the stable expression of adiponectin (Adipo-HEK cell) as well as in Simpson Golabi-Behmel-Syndrome adipocytes (SGBS) causes a significant decrease in high-molecular-weight adiponectin in Adipo-HEK cells with no change in total adiponectin. Knockdown in the SGBS cells caused an increase in lipid accumulation yet inhibits adipogenesis. Adiponectin forms a protein complex with lysyl hydroxylase 3 and GLT25D1. The intracellular retention of lysyl hydroxylase 3 is dependent on GLT25D1
physiological function
loss of GLT25D1 leads to increased expression and intracellular accumulation of collagen type I. Inactivation of the GLT25D1 gene results in a compensatory induction of isoform GLT25D2 expression. Loss of GLT25D1 decreases collagen glycosylation by up to 60% but does not alter collagen folding and thermal stability. Cells harboring individually inactivated GLT25D1 and GLT25D2 genes can be recovered and maintained in culture, cell clones with simultaneously inactive GLT25D1 and GLT25D2 genes cannot be grown
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). GT252_HUMAN
626
0
72924
Swiss-Prot
Secretory Pathway (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
two distinct catalytic sites at the N- and C-terminal boundaries of each monomer are separated by an accessory domain. Dimerization is essential for lysyl hydroxylase activity, whereas disruption of physiological dimers does not significantly perturb the N-terminal glycosyltransferase activities of LH3
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
sitting drop vapor diffusion method, crystal structures of full-length human LH3 in complex with cofactors and donor substrates provide a molecular understanding of the biochemical knowledge underlying the multiple functions of this enzyme
structures of full-length human LH3 in complex with cofactors and donor substrates. LH3 has three domains encompassing multiple catalytic sites and forms elongated tail-to-tail dimers showing two distinct catalytic sites at the N- and C-terminal boundaries of each monomer. The glycosyltransferase domain displays distinguishing features compared to other known glycosyltransferases. Known disease-related mutations map in close proximity to the catalytic sites
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
A187D/A189D
-
30 kDa His-tagged amino-terminal fragment with mutations shows 2% glycosyltransferase activity of wild type fragment
D207H
-
the mutation is associated with skin fragility, delayed wound healing, joint hyperlaxity and contractures, muscle hypotonia, intellectual disability, and a spondyloepimetaphyseal dysplasia with bone fragility and severe kyphoscoliosis
G217S
-
the mutation is associated with skin fragility, delayed wound healing, joint hyperlaxity and contractures, muscle hypotonia, intellectual disability, and a spondyloepimetaphyseal dysplasia with bone fragility and severe kyphoscoliosis
additional information
additional information
-
A668G, higher apparent molecular mass, about 90% reduced collagen galctosyltransferase activity and reduced glucosyltransferase activity, EC 2.4.1.66, about 50% decreased lysyl hydroxylase activity, EC 1.14.11.4
additional information
-
delT2071, lower apparent molecular mass, about 60% reduced collagen galctosyltransferase activity and reduced glucosyltransferase activity, EC 2.4.1.66, complete loss of lysyl hydroxylase activity, EC 1.14.11.4
additional information
-
LH-deficient mutant, deficiency of LH3 glycosyltransferase activity decreases cell growth and increases lethality
additional information
-
overexpression of LH3, increased hydroxylation of lysyl residues and increased galactosylation and glucosylation of hydroxylysyl residues
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant baculoviruses are produced in Spodoptera frugiperda Sf9 cells
chimeric proteins (GLT25D1-cerebral endothelial cell adhesion molecule (CEECAM1)) expressed in SF-9 cell
recombinant baculoviruses are produced in Spodoptera frugiperda Sf9 cells
wild-type protein and His-tagged version expressed in fibrosarcoma cells HT-1080, 30 kDa His-tagged amino-terminal fragment (amino acid residue 25-290) with glycosyltransferase activity expressed in Escherichia coli
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
PLOD2 mRNA is induced greater than 4fold by hypoxia within 12 h and remains elevated for 72 hours of continuous hypoxia
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
high enzyme expression in breast cancer biopsies is associated with increased risk of mortality
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Kivirikko, K.I.; Myllyl, R.
Posttranslational enzymes in the biosynthesis of collagen: intracellular enzymes
Methods Enzymol.
82
245-304
1982
Cavia porcellus, Gallus gallus, Homo sapiens, Rattus norvegicus
Barber, A.J.; Jamieson, G.A.
Characterization of membrane-bound collagen galactosyltransferase of human blood platelets
Biochim. Biophys. Acta
252
546-552
1971
Homo sapiens
Carnicero, H.H.; Adamany, A.M.; Englard, S.
Collagen glucosyl- and galactosyltransferases of cultured human fetal lung fibroblasts
Arch. Biochem. Biophys.
210
678-690
1981
Homo sapiens
Salo, A.M.; Cox, H.; Farndon, P.; Moss, C.; Grindulis, H.; Risteli, M.; Robins, S.P.; Myllylae, R.
A connective tissue disorder caused by mutations of the lysyl hydroxylase 3 gene
Am. J. Hum. Genet.
83
495-503
2008
Homo sapiens
Risteli, M.; Ruotsalainen, H.; Salo, A.M.; Sormunen, R.; Sipilae, L.; Baker, N.L.; Lamande, S.R.; Vimpari-Kauppinen, L.; Myllylae, R.
Reduction of lysyl hydroxylase 3 causes deleterious changes in the deposition and organization of extracellular matrix
J. Biol. Chem.
284
28204-28211
2009
Homo sapiens (O60568), Mus musculus
Wang, C.; Kovanen, V.; Raudasoja, P.; Eskelinen, S.; Pospiech, H.; Myllylae, R.
The glycosyltransferase activities of lysyl hydroxylase 3 (LH3) in the extracellular space are important for cell growth and viability
J. Cell. Mol. Med.
13
508-521
2009
Homo sapiens
Schegg, B.; Huelsmeier, A.J.; Rutschmann, C.; Maag, C.; Hennet, T.
Core glycosylation of collagen is initiated by two beta(1-O)galactosyltransferases
Mol. Cell. Biol.
29
943-952
2009
Gallus gallus, Homo sapiens (Q8IYK4), Homo sapiens (Q8NBJ5), Homo sapiens
Liefhebber, J.; Punt, S.; Spaan, W.; van Leeuwen, H.
The human collagen beta(1-O)galactosyltransferase, GLT25D1, is a soluble endoplasmic reticulum localized protein
BMC Cell Biol.
11
33
2010
Homo sapiens (Q8NBJ5), Homo sapiens
Perrin-Tricaud, C.; Rutschmann, C.; Hennet, T.
Identification of domains and amino acids essential to the collagen galactosyltransferase activity of GLT25D1
PLoS ONE
6
e29390
2011
Homo sapiens (Q8NBJ5), Homo sapiens
Gilkes, D.M.; Bajpai, S.; Wong, C.C.; Chaturvedi, P.; Hubbi, M.E.; Wirtz, D.; Semenza, G.L.
Procollagen lysyl hydroxylase 2 is essential for hypoxia-induced breast cancer metastasis
Mol. Cancer Res.
11
456-466
2013
Homo sapiens (O00469)
Malfait,F.; Kariminejad, A.; Van Damme,T.; Gauche, C.; Syx, D.; Merhi-Soussi, F.; Gulberti, S.; Symoens, S.; Vanhauwaert, S.; Willaert, A.; Bozorgmehr, B.; Kariminejad, M.H.; Ebrahimiadib, N.; Hausser, I.; Huysseune, A.; Fournel-Gigleux, S.; De Paepe, A.
Defective initiation of glycosaminoglycan synthesis due to B3GALT6 mutations causes a pleiotropic Ehlers-Danlos-Syndrome-like connective tissue disorder
Am. J. Hum. Genet.
92
935-945
2013
Homo sapiens
Risteli, M.; Ruotsalainen, H.; Bergmann, U.; Venkatraman Girija, U.; Wallis, R.; Myllylae, R.
Lysyl hydroxylase 3 modifies lysine residues to facilitate oligomerization of mannan-binding lectin
PLoS ONE
9
e113498
2014
Homo sapiens
Webster, J.A.; Yang, Z.; Kim, Y.H.; Loo, D.; Mosa, R.M.; Li, H.; Chen, C.
Collagen beta (1-O) galactosyltransferase 1 (GLT25D1) is required for the secretion of high molecular weight adiponectin and affects lipid accumulation
Biosci. Rep.
37
BSR20170105
2017
Homo sapiens (Q8NBJ5), Homo sapiens, Mus musculus (Q8K297)
Baumann, S.; Hennet, T.
Collagen accumulation in osteosarcoma cells lacking GLT25D1 collagen galactosyltransferase
J. Biol. Chem.
291
18514-18524
2016
Homo sapiens (Q8IYK4), Homo sapiens (Q8NBJ5)
Scietti, L.; Chiapparino, A.; De Giorgi, F.; Fumagalli, M.; Khoriauli, L.; Nergadze, S.; Basu, S.; Olieric, V.; Cucca, L.; Banushi, B.; Profumo, A.; Giulotto, E.; Gissen, P.; Forneris, F.
Molecular architecture of the multifunctional collagen lysyl hydroxylase and glycosyltransferase LH3
Nat. Commun.
9
3163
2018
Homo sapiens (O60568)
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