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Information on EC 2.4.1.66 - procollagen glucosyltransferase and Organism(s) Homo sapiens and UniProt Accession O60568
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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).
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Word Map
- 2.4.1.66
-
prolyl
- gg
-
4-hydroxylase
-
galactosyltransferase
- propeptide
- soleus
-
aminoterminal
- hyp
- tibialis
- 4-hydroxyproline
-
chick-embryo
The taxonomic range for the selected organisms is: Homo sapiens
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
Synonyms
galactosylhydroxylysyl glucosyltransferase, collagen glucosyltransferase, galactosylhydroxylysine glucosyltransferase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
collagen glucosyltransferase
-
-
-
-
collagen hydroxylysyl glucosyltransferase
-
-
-
-
galactosylhydroxylysyl glucosyltransferase
-
-
-
-
GGT
-
-
-
-
glucosyltransferase, uridine diphosphoglucose-collagen
-
-
-
-
lysyl hydroxylase 3
UDP-glucose-collagen glucosyltransferase
-
-
-
-
UDP-glucose:galactosylhydroxylysine-collagen glucosyltransferase
-
-
-
-
uridine diphosphoglucose-collagen glucosyltransferase
-
-
-
-
additional information
lysyl hydroxylase 3
-
a multifunctional protein with lysyl hydroxylase, collagen galactosyltransferase and glucosyltransferase activities
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
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
reaction mechanism
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hexosyl group transfer
-
-
-
-
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).
CAS REGISTRY NUMBER
COMMENTARY
9028-08-4
-
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-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
TDP-glucose + D-galactosylhydroxylysine
TDP + 1,2-D-glucosyl-D-galactosylhydroxylysine
-
soluble enzyme, glucosylation at 60% of the rate of UDP-glucose
-
?
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 + fetuin minus sialic acid, galactose and N-acetylglucosamine
?
-
7% as effective as glucose-free bovine Achilles tendon collagen
-
-
?
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
-
-
-
-
?
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 + 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
-
?
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
-
-
?
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
additional information
?
-
-
there must be an additional glucosyltransferase to LH3 that is responsible for most of the collagen glucosylation in vivo
-
-
?
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
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Fe2+
contributes to the overall enzyme stabilization, enzymatic activity peaks at 25 microM Fe2+
Ca2+
Co2+
Mg2+
Mn2+
additional information
Mn2+
-
25-80 mM: optimal concentration for free galactosylhydroxylysine as acceptor, 2 mM: optimal concentration for galactosylhydroxylysine bound in purified alpha1-chain of chicken skin collagen as acceptor, soluble enzyme is inhibited above 50 mM
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
sucrose
-
membrane-bound enzyme, 0.42 M: 88% inhibition, also inhibits soluble enzyme
additional information
-
not inhibited by D-glucose, N-acetylglucosamine, N-acteylgalactosamine, Triton X-100, delta-hydroxylysine
-
additional information
-
membrane-bound enzyme: not inhibited by 100 mM D-glucosamine, 10 mM N-ethylmaleimide, 50 mM glucosylgalactosylhydroxylysine, soluble enzyme: not inhibited by 75 mM glucosylgalactosylhydroxylysine
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
enzyme activity is dependent on aging of IMR-90 cells
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.002
D-galactosylhydroxylysine
-
bound in purified alpha1-chain of chicken skin collagen, value based on actual amount of galactosylhydroxylysine-residues of alpha1-chain
additional information
additional information
-
Km: 1.5 mg/ml, alpha-chain of chicken skin collagen
-
additional information
additional information
-
Km: 4 mg/ml, denatured citrate soluble rat skin collagen
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
25 DMP/microg soluble protein, control group, activitiy in lymphoblastoid cells
additional information
-
25 DPM/microl serum, patient with mutation of the lysyl hydroxylase 3 gene
additional information
-
5 DPM/microg soluble protein, patient with mutation of the lysyl hydroxylase 3 gene, activitiy in lymphoblastoid cells
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
multifunctional, cataylzes reactions of EC 1.14.11.4, EC 2.4.1.50, EC 2.4.1.66
UniProt
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
fetal lung WI-38 and IMR-90 diploid fibroblasts, in cell suspension culture
-
fetal lung WI-38 and IMR-90 diploid fibroblasts, in cell suspension culture
-
fetal lung WI-38 and IMR-90 diploid fibroblasts, in cell suspension culture
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
5-10% of the total activity is surface-bound, the rest is of cytoplasmic origin
-
secretion of the enzyme from the endoplasmic reticulum to the extracellular space occurs via two secretory pathways, which generate two glycoforms. Enzyme molecules found in the cell medium are secreted through the Golgi complex, and the secretion is dependent on lysyl hydroxylase 3 glycosyltransferase activity. Enzyme found on the cell surface bypasses the Golgi complex
-
membrane-bound and soluble forms in platelets, lymphocytes and granulocytes
-
5-10% of the total activity is surface-bound, the rest is of cytoplasmic origin
-
membrane-bound and soluble forms in platelets, lymphocytes and granulocytes
-
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
organization of the extracellular matrix and cytoskeleton
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
-
lysyl hydroxylase 3-mediated glucosylation occurs at specific sites in collagen, including cross-linking sites, and suppression of this modification results in defective collagen and mineralization
metabolism
-
lysyl hydroxylase 3 functions as glucosyltransferase in type I 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
-
the lysyl hydroxylase 3-mediated glucosylation occurs at the specific molecular loci in the type I collagen molecule and plays critical roles in controlling collagen cross-linking, fibrillogenesis, and mineralization
physiological function
-
fibroblast cell surface recruitment of matrix metalloproteinase-9 via its fibronectin-like domain by lysyl hydroxylase 3 induces transforming growth factor-beta activation and myofibroblast differentiation
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). PLOD3_HUMAN
738
0
84785
Swiss-Prot
Secretory Pathway (Reliability: 2)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
80000
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
additional information
-
structural domain fragment A of LH3 with GGT activity contains 2 N-glycosylation sites
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
D187A/D189A/D190A/D191A
-
the mutant shows unreduced lysyl hydroxylase 3 activity
additional information
additional information
A195G/A434G/C882T/A1011G, reduced amount of LH3 in humans with epidermolysis bullosa simplex, only 30% GGT activity in cell lysate, only 40% GGT activity in the culture medium
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
additional information
-
mutagenesis of aspartates of the DXD-like motif in LH3 eliminates GGT activity
additional information
-
mutation of aspartates in the positions 187-191 significantly reduces GGT activity of LH3
additional information
-
A668G, higher apparent molecular mass, reduced collagen galctosyltransferase, EC 2.4.1.50, and about 80% reduced glucosyltransferase activity, about 50% decreased lysyl hydroxylase activity, EC 1.14.11.4
additional information
-
delT2071, lower apparent molecular mass, reduced collagen galctosyltransferase, EC 2.4.1.50, and about 50% reduced glucosyltransferase activity, complete loss of lysyl hydroxylase activity, EC 1.14.11.4
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
20
-
10% loss of activity within 18 h, soluble enzyme, after DEAE-ion exchange chromatography
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
room temperature, soluble enzyme after DEAE-cellulose column, 18 h, 10% loss of activity
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
His-tagged recombinant LH3/GGT/GT and N-terminal 30kDa fragment A of LH3 with GGT activity expressed in High Five insect cells
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
overexpression in HT-1080 cells, expression of fragments in Escherichia coli
full-length LH3 and the N-terminal 30 kDa fragment A with GGT activity is cloned, sequenced and expressed in High Five insect cells
-
LH3 cDNA with GGT activity is cloned and expressed in Sf9 insect cells and in Escherichia coli XL1-Blue
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
enzyme levels are reduced in patients with recessive dystrophic epidermolysis bullosa
-
exogenous type VII collagen do not alter enzyme expression in cultured recessive dystrophic epidermolysis bullosa keratinocytes
-
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
Bos taurus, Cavia porcellus, Gallus gallus, Homo sapiens, Rattus norvegicus
Rautavuoma, K.; Takaluoma, K.; Passoja, K.; Pirskanen, A.; Kvist, A.P.; Kivirikko, K.I.; Myllyharju, J.
Characterization of three fragments that constitute the monomers of the human lysyl hydroxylase isoenzymes 1-3: The 30-kDa N-terminal fragment is not required for lysyl hydroxylase activity
J. Biol. Chem.
277
23084-23091
2002
Homo sapiens
Wang, C.; Risteli, M.; Heikkinen, J.; Hussa, A.K.; Uitto, L.; Myllyla, R.
Identification of amino acids important for the catalytic activity of the collagen glucosyltransferase associated with the multifunctional lysyl hydroxylase 3 (LH3)
J. Biol. Chem.
277
18568-18573
2002
Caenorhabditis elegans, Homo sapiens
Carnicero, H.H.; Adamany, A.M.; Englard, S.
Collagen glucosyl- and galactosyltransferases of cultured human fetal lung fibroblasts
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Homo sapiens
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Platelet collagen adhesion characterization of collagen glucosyltransferase of plasma membranes of human blood platelets
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Homo sapiens
Leunis, J.C.; Smith, D.F.; Nwokoro, N.; Fishback, B.L.; Wu, C.; Jamieson, G.A.
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Homo sapiens
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Characterization of human platelet UDPglucose-collagen glucosyltransferase using a new rapid assay
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Homo sapiens
Wang, C.; Luosujrvi, H.; Heikkinen, J.; Risteli, M.; Uitto, L.; Myllyl, R.
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Caenorhabditis elegans, Homo sapiens
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Homo sapiens
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Homo sapiens (O60568), Mus musculus
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Homo sapiens (O60568)
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Homo sapiens, Mus musculus
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Homo sapiens
Dayer, C.; Stamenkovic, I.
Recruitment of matrix metalloproteinase-9 (MMP-9) to the fibroblast cell surface by lysyl hydroxylase 3 (lh3) triggers transforming growth factor-beta (TGF-beta) activation and fibroblast differentiation
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Homo sapiens
Watt, S.A.; Dayal, J.H.; Wright, S.; Riddle, M.; Pourreyron, C.; McMillan, J.R.; Kimble, R.M.; Prisco, M.; Gartner, U.; Warbrick, E.; McLean, W.H.; Leigh, I.M.; McGrath, J.A.; Salas-Alanis, J.C.; Tolar, J.; South, A.P.
Lysyl hydroxylase 3 localizes to epidermal basement membrane and is reduced in patients with recessive dystrophic epidermolysis bullosa
PLoS ONE
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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
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Homo sapiens
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
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Homo sapiens (O60568)
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