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Information on EC 2.4.2.26 - protein xylosyltransferase and Organism(s) Homo sapiens and UniProt Accession Q86Y38
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2.4.2.26 protein xylosyltransferaseIUBMB Comments
Involved in the biosynthesis of the linkage region of glycosaminoglycan chains as part of proteoglycan biosynthesis (chondroitin, dermatan and heparan sulfates).
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Word Map
- 2.4.2.26
- proteoglycans
- glycosaminoglycans
- chondroitin
- heparan
-
xylosylation
-
chain-initiating
-
xylts
- medicine
- bikunin
-
laxity
-
desbuquois
- elasticum
-
pseudoxanthoma
- diagnostics
- analysis
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
xylt2, xt-ii, xylt-ii, xylosyltransferase 1, xylt-i, xylosyltransferase ii, xylosyltransferase 2, protein xylosyltransferase, peptide o-xylosyltransferase, udp-d-xylose:proteoglycan core protein beta-d-xylosyltransferase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
XT-I
xylosyltransferase I
Rumi
-
in addition to protein O-glucosyltransferase activity, both human and mouse Rumi also show protein O-xylosyltransferase activity
UDP-D-xylose:core protein beta-D-xylosyltransferase
-
-
-
-
UDP-D-xylose:core protein xylosyltransferase
-
-
-
-
UDP-D-xylose:proteoglycan core protein beta-D-xylosyltransferase
UDP-xylose-core protein beta-D-xylosyltransferase
-
-
-
-
uridine diphosphoxylose-core protein beta-xylosyltransferase
-
-
-
-
uridine diphosphoxylose-protein xylosyltransferase
-
-
-
-
XT
XT-II
xylosyltransferase II
xylosyltransferase, uridine diphosphoxylose-core protein beta-
-
-
-
-
XylT-II
additional information
-
the enzyme competes for the substrate UDP-D-xylose with glycogenin, EC 2.4.1.186, which utilizes UDP-D-xylose as an alternative substrate to UDP-D-glucose
UDP-D-xylose:proteoglycan core protein beta-D-xylosyltransferase
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
UDP-alpha-D-xylose + [protein]-L-serine = UDP + [protein]-3-O-(beta-D-xylosyl)-L-serine
chondroitin sulfate attachment site, determination of the consensus sequence for the recognition signal of the enzyme
-
UDP-alpha-D-xylose + [protein]-L-serine = UDP + [protein]-3-O-(beta-D-xylosyl)-L-serine
isoform XT-I contains the DxD motif at position 183, which has shown to be essential for binding of nucleotide sugars in glycosyltransferases
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pentosyl group transfer
-
-
-
-
PATHWAY SOURCE
PATHWAYS
KEGG
-
-
SYSTEMATIC NAME
IUBMB Comments
UDP-alpha-D-xylose:protein beta-D-xylosyltransferase (configuration-inverting)
Involved in the biosynthesis of the linkage region of glycosaminoglycan chains as part of proteoglycan biosynthesis (chondroitin, dermatan and heparan sulfates).
CAS REGISTRY NUMBER
COMMENTARY
55576-38-0
-
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-D-xylose + biotin-NHQEEEGSGGGQKK(5-fluorescein)-CONH2
UDP + biotin-NHQEEEG-(D-xylosyl)SGGGQKK(5-fluorescein)-CONH2
UDP-D-xylose + proteoglycan core protein
UDP + proteoglycan core protein with xyloserine
the xylosyltransferases I and II catalyze the transfer of xylose from UDP-xylose to selected serine residues in the proteoglycan core protein, which is the initial and rate limiting step in glycosaminoglycan biosynthesis
-
-
?
UDP-D-xylose + silk fibroin
UDP + silk fibroin with xylosylserine
-
-
-
?
UDP + human basic fibroblast growth factor
UDP + ?
-
transfer of xylose to the serine residue of the G-S-G-motif in the amino terminal end of human basic fibroblast growth factor
-
-
?
UDP-D-xylose + bikunin-derived aminoterminus homologous peptide
UDP + xylosyl-serine bikunin-derived aminoterminus homologous peptide
-
-
-
?
UDP-D-xylose + biotin-NH-QEEEGSGGGQKK(5-fluorescein)-CONH2
UDP + biotin-NH-QEEEG-(D-xylosyl)SGGGQKK(5-fluorescein)-CONH2
UDP-D-xylose + biotin-NH-QEEEGSGGGQKK(5-fluorescein)-CONH2
UDP + biotin-NH-QEEEGS(D-xylosyl)GGGQKK(5-fluorescein)-CONH2
best substrate known so far for XT-IImediated xylosylation
-
-
?
UDP-D-xylose + biotin-NHQEEEGSGGGQKK(5-fluorescein)-CONH2
UDP + biotin-NHQEEEG-(D-xylosyl)SGGGQKK(5-fluorescein)-CONH2
UDP-D-xylose + cartilage chondroitin sulfate proteoglycan
UDP + cartilage chondroitin sulfate proteoglycan with xylosylserine
-
degraded by hydrogen fluoride or trifluromethanesulfonic acid
-
-
?
UDP-D-xylose + GVEGSADFLK
UDP + GVEGS(-D-xylose)ADFLK
-
derived from collagen X
-
?
UDP-D-xylose + PLVSSGEDEPK
UDP + ?
-
derived from neurocan protein
D-xylose bound to a serine residue
?
UDP-D-xylose + proteoglycan core protein
UDP + proteoglycan core protein with xylosylserine
the xylosyltransferases I and II catalyze the transfer of xylose from UDP-xylose to selected serine residues in the proteoglycan core protein, which is the initial and rate limiting step in glycosaminoglycan biosynthesis
-
-
?
UDP-D-xylose + QEEEGSGGGQKK
UDP + QEEEG-(D-xylosyl)SGGGQKK
-
the bikunin nuclear acceptor peptide QEEEGSGGGQKK is not a differential acceptor substrate for the human XylT isoenzymes but is a good acceptor substrate for total XylT activity measurements
-
-
?
UDP-D-xylose + SENEGSGMAEQK
UDP + SENEGS(-D-xylose)GMAEQK
-
synthetic leukocyte-derived amyloid precursor-like protein homologous peptide
-
?
UDP-D-xylose + TENEGSGLTNIK
UDP + TENEG-(D-xylosyl)SGLTNIK
-
the 3-A4-amyloid protein precursor protein peptide TENEGSGLTNIK is an acceptor substrate for XylT1
-
-
?
UDP-D-xylose + TENEGSGLTNIK
UDP + TENEGS(-D-xylose)GLTNIK
-
synthetic leukocyte-derived beta-A4-amyloid protein precursor homologous peptide
-
?
UDP-D-xylose + VCRSGSGLVGK
UDP + VCRSGSGLVGK
-
derived from apolipoprotein J
D-xylose bound to a serine residue
?
UDP-D-xylose + biotin-NHQEEEGSGGGQKK(5-fluorescein)-CONH2
UDP + biotin-NHQEEEG-(D-xylosyl)SGGGQKK(5-fluorescein)-CONH2
-
-
-
?
UDP-D-xylose + biotin-NHQEEEGSGGGQKK(5-fluorescein)-CONH2
UDP + biotin-NHQEEEG-(D-xylosyl)SGGGQKK(5-fluorescein)-CONH2
-
-
-
?
UDP-D-xylose + DSISGDDLGSGDLGSGDFQR
?
the enzyme modifies the peptide with up to two xylose residues
-
-
?
UDP-alpha-D-xylose + [protein]-L-serine
UDP + [protein]-3-O-(beta-D-xylosyl)-L-serine
-
transfers a beta-D-xylosyl residue from UDP-D-xylose to the serine hydroxyl group of an acceptor protein substrate
-
?
UDP-alpha-D-xylose + [protein]-L-serine
UDP + [protein]-3-O-(beta-D-xylosyl)-L-serine
-
transfers a beta-D-xylosyl residue from UDP-D-xylose to the serine hydroxyl group of an acceptor protein substrate
-
?
UDP-alpha-D-xylose + [protein]-L-serine
UDP + [protein]-3-O-(beta-D-xylosyl)-L-serine
-
transfers a beta-D-xylosyl residue from UDP-D-xylose to the serine hydroxyl group of an acceptor protein substrate
-
?
UDP-alpha-D-xylose + [protein]-L-serine
UDP + [protein]-3-O-(beta-D-xylosyl)-L-serine
-
transfers a beta-D-xylosyl residue from UDP-D-xylose to the serine hydroxyl group of an acceptor protein substrate
-
?
UDP-alpha-D-xylose + [protein]-L-serine
UDP + [protein]-3-O-(beta-D-xylosyl)-L-serine
-
transfers a beta-D-xylosyl residue from UDP-D-xylose to the serine hydroxyl group of an acceptor protein substrate
-
?
UDP-alpha-D-xylose + [protein]-L-serine
UDP + [protein]-3-O-(beta-D-xylosyl)-L-serine
-
transfers a beta-D-xylosyl residue from UDP-D-xylose to the serine hydroxyl group of an acceptor protein substrate
-
?
UDP-alpha-D-xylose + [protein]-L-serine
UDP + [protein]-3-O-(beta-D-xylosyl)-L-serine
-
transfers a beta-D-xylosyl residue from UDP-D-xylose to the serine hydroxyl group of an acceptor protein substrate
-
?
UDP-alpha-D-xylose + [protein]-L-serine
UDP + [protein]-3-O-(beta-D-xylosyl)-L-serine
-
transfers a beta-D-xylosyl residue to specific serine residues dependent on the consensus signal sequence
-
?
UDP-alpha-D-xylose + [protein]-L-serine
UDP + [protein]-3-O-(beta-D-xylosyl)-L-serine
-
transfers a beta-D-xylosyl residue to specific serine residues dependent on the consensus signal sequence
-
?
UDP-alpha-D-xylose + [protein]-L-serine
UDP + [protein]-3-O-(beta-D-xylosyl)-L-serine
-
initiation of chondroitin sulfate biosynthesis
-
-
?
UDP-alpha-D-xylose + [protein]-L-serine
UDP + [protein]-3-O-(beta-D-xylosyl)-L-serine
-
enzyme may play a role in maintaining the haemostatic potential of the follicular fluid
-
-
?
UDP-alpha-D-xylose + [protein]-L-serine
UDP + [protein]-3-O-(beta-D-xylosyl)-L-serine
-
enzyme is associated with large chondroitin sulfate-containing proteoglycans
-
-
?
UDP-alpha-D-xylose + [protein]-L-serine
UDP + [protein]-3-O-(beta-D-xylosyl)-L-serine
-
enzyme initiates the biosynthesis of glycosaminoglycan lateral chains in proteoglycans by transfer of xylose from UDP-xylose to specific serine residues of the core protein
-
-
?
UDP-alpha-D-xylose + [protein]-L-serine
UDP + [protein]-3-O-(beta-D-xylosyl)-L-serine
-
initiates the biosynthesis of the glycosaminoglycan linkage region
-
-
?
UDP-alpha-D-xylose + [protein]-L-serine
UDP + [protein]-3-O-(beta-D-xylosyl)-L-serine
-
Rumi transfers D-xylose or D-glucose to serine 52 in the O-glucose consensus sequence (50CASSPC55) of factor VII EGF repeat. The second serine (S53) facilitates transfer of Xyl, but not glucose, to the EGF repeat by Rumi. EGF16 of mouse Notch2, which has a diserine motif in the consensus sequence (587CYSSPC592), is also modified with either O-Xyl or O-glucose glycans in cells
-
-
?
UDP-D-xylose + bikunin
UDP + D-xylosyl-bikunin
-
recombinant bikunin
bound to serine residue
?
UDP-D-xylose + bikunin
UDP + D-xylosyl-bikunin
-
recombinant wild-type from Chang liver hepatocytes and mutant, expressed in Escherichia coli
bound to serine residue
?
UDP-D-xylose + bikunin
UDP + D-xylosyl-bikunin
-
recombinant mutant bikunin
bound to serine residue
?
UDP-D-xylose + bikunin
UDP + D-xylosyl-bikunin
-
recombinant mutant bikunin
bound to serine residue
?
UDP-D-xylose + biotin-NH-QEEEGSGGGQKK(5-fluorescein)-CONH2
UDP + biotin-NH-QEEEG-(D-xylosyl)SGGGQKK(5-fluorescein)-CONH2
the bikunin-homologous peptide Bio-QEEEGSGGGQKK-F is best acceptor substrate for XT-II, 100% activity with UDP-D-xylose
-
-
?
UDP-D-xylose + biotin-NH-QEEEGSGGGQKK(5-fluorescein)-CONH2
UDP + biotin-NH-QEEEG-(D-xylosyl)SGGGQKK(5-fluorescein)-CONH2
-
catalytic efficiency of XylT-I is more than 2.4fold higher than for XylT-II
-
-
?
UDP-D-xylose + biotin-NHQEEEGSGGGQKK(5-fluorescein)-CONH2
UDP + biotin-NHQEEEG-(D-xylosyl)SGGGQKK(5-fluorescein)-CONH2
biotin-NHQEEEGSGGGQKK(5-fluorescein)-CONH2is the best acceptor for isozyme XT-II
-
-
?
UDP-D-xylose + biotin-NHQEEEGSGGGQKK(5-fluorescein)-CONH2
UDP + biotin-NHQEEEG-(D-xylosyl)SGGGQKK(5-fluorescein)-CONH2
biotin-NHQEEEGSGGGQKK(5-fluorescein)-CONH2is the best acceptor for isozyme XT-II
-
-
?
UDP-D-xylose + DDDSIEGSGGR
UDP + DDDSIEG(D-xylosyl)SGGR
syndecan peptide substrate
-
-
?
UDP-D-xylose + QEEEGSGGGOK
UDP + QEEEGS(-D-xylose)GGGOK
-
best substrate
-
?
UDP-D-xylose + QEEEGSGGGOK
UDP + QEEEGS(-D-xylose)GGGOK
-
peptide derived from bikunin
-
?
UDP-D-xylose + silk fibroin
UDP + silk fibroin with xylosylserine
-
-
-
?
UDP-D-xylose + silk fibroin
UDP + silk fibroin with xylosylserine
-
-
-
?
UDP-D-xylose + silk fibroin
UDP + silk fibroin with xylosylserine
-
acceptor substrate contains repetitive sequence Gly-Ser-Gly-Ala-Gly-Ala
-
-
?
UDP-D-xylose + silk fibroin
UDP + silk fibroin with xylosylserine
silk fibroin is a low affinity acceptor for XT-II
-
-
?
additional information
?
-
first enzyme required for the generation of chondroitin and heparan sulfate glycosaminoglycan chains of proteoglycans
-
-
?
additional information
?
-
first enzyme required for the generation of chondroitin and heparan sulfate glycosaminoglycan chains of proteoglycans
-
-
?
additional information
?
-
-
first enzyme required for the generation of chondroitin and heparan sulfate glycosaminoglycan chains of proteoglycans
-
-
?
additional information
?
-
synthesis of chondrioitin and heparan sulphates is initiated by UDP-alpha-D-xylose:proteoglycan core protein beta-D-xylosyltransferase
-
-
?
additional information
?
-
-
synthesis of chondrioitin and heparan sulphates is initiated by UDP-alpha-D-xylose:proteoglycan core protein beta-D-xylosyltransferase
-
-
?
additional information
?
-
-
very low activity with tripeptide SGG and peptide LNFSTGW
-
-
?
additional information
?
-
-
enzyme activity in seminal plasma of infertile men is significantly reduced
-
-
?
additional information
?
-
first enzyme required for the generation of chondroitin and heparan sulfate glycosaminoglycan chains of proteoglycans
-
-
?
additional information
?
-
first enzyme required for the generation of chondroitin and heparan sulfate glycosaminoglycan chains of proteoglycans
-
-
?
additional information
?
-
-
first enzyme required for the generation of chondroitin and heparan sulfate glycosaminoglycan chains of proteoglycans
-
-
?
additional information
?
-
-
xylosyltransferase II is involved in the biosynthesis of the uniform tetrasaccharide linkage region in chondroitin sulfate and heparan sulfate proteoglycans
-
-
?
additional information
?
-
xylosyltransferase II is involved in the biosynthesis of the uniform tetrasaccharide linkage region in chondroitin sulfate and heparan sulfate proteoglycans
-
-
?
additional information
?
-
-
XT-II initiates the biosynthesis of both heparan sulfate and chondroitin sulfate
-
-
?
additional information
?
-
XT-II initiates the biosynthesis of both heparan sulfate and chondroitin sulfate
-
-
?
additional information
?
-
TENEGSGLTNIK, SENEGSGMAEQK, orcokinin (NFDEIDRSGFGFN), melittin (GIGAVLKVLTTGLPALISWIKRKRQQ), fibrinopeptide A (ADSGEGDFLAEGGGVR), IgE C4 domain (KTKGSGFFVF), C-type natriuretic peptide (GLSKGCFGLKLDRIGSMSGLGC), and calcitonin (VLGKLSQELHKLQTYPRTNTGSGTP) are no substrates for XT-II
-
-
?
additional information
?
-
-
TENEGSGLTNIK, SENEGSGMAEQK, orcokinin (NFDEIDRSGFGFN), melittin (GIGAVLKVLTTGLPALISWIKRKRQQ), fibrinopeptide A (ADSGEGDFLAEGGGVR), IgE C4 domain (KTKGSGFFVF), C-type natriuretic peptide (GLSKGCFGLKLDRIGSMSGLGC), and calcitonin (VLGKLSQELHKLQTYPRTNTGSGTP) are no substrates for XT-II
-
-
?
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-D-xylose + proteoglycan core protein
UDP + proteoglycan core protein with xyloserine
the xylosyltransferases I and II catalyze the transfer of xylose from UDP-xylose to selected serine residues in the proteoglycan core protein, which is the initial and rate limiting step in glycosaminoglycan biosynthesis
-
-
?
UDP-D-xylose + proteoglycan core protein
UDP + proteoglycan core protein with xylosylserine
the xylosyltransferases I and II catalyze the transfer of xylose from UDP-xylose to selected serine residues in the proteoglycan core protein, which is the initial and rate limiting step in glycosaminoglycan biosynthesis
-
-
?
UDP-alpha-D-xylose + [protein]-L-serine
UDP + [protein]-3-O-(beta-D-xylosyl)-L-serine
-
initiation of chondroitin sulfate biosynthesis
-
-
?
UDP-alpha-D-xylose + [protein]-L-serine
UDP + [protein]-3-O-(beta-D-xylosyl)-L-serine
-
enzyme may play a role in maintaining the haemostatic potential of the follicular fluid
-
-
?
UDP-alpha-D-xylose + [protein]-L-serine
UDP + [protein]-3-O-(beta-D-xylosyl)-L-serine
-
enzyme is associated with large chondroitin sulfate-containing proteoglycans
-
-
?
UDP-alpha-D-xylose + [protein]-L-serine
UDP + [protein]-3-O-(beta-D-xylosyl)-L-serine
-
enzyme initiates the biosynthesis of glycosaminoglycan lateral chains in proteoglycans by transfer of xylose from UDP-xylose to specific serine residues of the core protein
-
-
?
UDP-alpha-D-xylose + [protein]-L-serine
UDP + [protein]-3-O-(beta-D-xylosyl)-L-serine
-
initiates the biosynthesis of the glycosaminoglycan linkage region
-
-
?
additional information
?
-
first enzyme required for the generation of chondroitin and heparan sulfate glycosaminoglycan chains of proteoglycans
-
-
?
additional information
?
-
first enzyme required for the generation of chondroitin and heparan sulfate glycosaminoglycan chains of proteoglycans
-
-
?
additional information
?
-
-
first enzyme required for the generation of chondroitin and heparan sulfate glycosaminoglycan chains of proteoglycans
-
-
?
additional information
?
-
synthesis of chondrioitin and heparan sulphates is initiated by UDP-alpha-D-xylose:proteoglycan core protein beta-D-xylosyltransferase
-
-
?
additional information
?
-
-
synthesis of chondrioitin and heparan sulphates is initiated by UDP-alpha-D-xylose:proteoglycan core protein beta-D-xylosyltransferase
-
-
?
additional information
?
-
-
enzyme activity in seminal plasma of infertile men is significantly reduced
-
-
?
additional information
?
-
first enzyme required for the generation of chondroitin and heparan sulfate glycosaminoglycan chains of proteoglycans
-
-
?
additional information
?
-
first enzyme required for the generation of chondroitin and heparan sulfate glycosaminoglycan chains of proteoglycans
-
-
?
additional information
?
-
-
first enzyme required for the generation of chondroitin and heparan sulfate glycosaminoglycan chains of proteoglycans
-
-
?
additional information
?
-
-
xylosyltransferase II is involved in the biosynthesis of the uniform tetrasaccharide linkage region in chondroitin sulfate and heparan sulfate proteoglycans
-
-
?
additional information
?
-
xylosyltransferase II is involved in the biosynthesis of the uniform tetrasaccharide linkage region in chondroitin sulfate and heparan sulfate proteoglycans
-
-
?
additional information
?
-
-
XT-II initiates the biosynthesis of both heparan sulfate and chondroitin sulfate
-
-
?
additional information
?
-
XT-II initiates the biosynthesis of both heparan sulfate and chondroitin sulfate
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
N-Phenylmaleimide
treatment shows no effect on wild-type XT-I but strongly inactivaets the cysteine mutants C461A and C574A
beta-mercaptoethanol
XT-II activity is completely abolished at a concentration 1% (v/v) beta-mercaptoethanol
dithiothreitol
XT-II activity is completely abolished at a concentration of 1 mM dithiothreitol
protamine
adding protamine to a final concentration of 10 mg/ml decreases XT-II activity 4fold
UDP
inhibition on the XT-I activity of C561A mutant enzyme is significantly reduced compared with all other tested cysteine mutants
heparin
-
non-competitive inhibitor using fragment(1-24) of human basic fibroblast growth factor as xylose acceptor
additional information
lysozyme does not change the activity of XT-II at any concentration
-
additional information
-
lysozyme does not change the activity of XT-II at any concentration
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
transforming growth factor beta1
0.5-10 ng/ml transforming growth factor beta1 induce expression of isozyme XT-I
-
histone protein
activity gains 1.5fold when histone protein is added at a concentration of 0.1 mg/ml
-
protamine
adding protamine to a final concentration of 0.1 mg/ml stimulates XT-II activity at least 2fold
additional information
0.5-10 ng/ml transforming growth factor beta1 does not induce expression of isozyme XT-II
-
additional information
0.5-10 ng/ml transforming growth factor beta1 does not induce expression of isozyme XT-II
-
additional information
-
0.5-10 ng/ml transforming growth factor beta1 does not induce expression of isozyme XT-II
-
additional information
-
the c-Jun/activator protein-1 transcription factor is essential for full XYLT1 promoter activity in SW1353 cells
-
additional information
-
unactivated platelets harbor significant XylT activity that is released upon activation with thrombin. Diseases affecting platelet activation may alter serum total XylT activity. In vivo liver cells may contribute significant XylT activity to circulating levels
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0274
bikunin
-
isoenzyme XT-I with wild-type bikunin (sequence QEEEGSGGGQLV)
-
0.0462
bikunin
-
isoenzyme XT-II with wild-type bikunin (sequence QEEEGSGGGQLV)
-
0.155
cartilage chondroitin sulfate proteoglycan
-
trifluoromethanesulfonic acid-degraded substrate
-
0.19
cartilage chondroitin sulfate proteoglycan
-
hydrogen fluoride-degraded substrate
-
0.0223
fragment(1-24) of human basic fibroblast growth factor
-
recombinant XT-I
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.5 - 9
pH 6.5: about 60% of maximal activity, pH 9.0: about 60% of maximal activity
6.5 - 8.5
pH 6.5: about 70% of maximal activity, pH 8.5: about 60% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
15 - 37
15Ā°C: about 40% of maximal activity, 37Ā°C: maximal activity
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
mesenchymal stem cell. Xylosyltransferase 1 is the predominant xylosyltransferase in the early phase of chondrogenic stem cell differentiation and xylosyltransferase 2 is upregulated 7 days after induction
-
XT-II mRNA expression is higher than for XT-I. Very low XT-I mRNA expression
-
unactivated platelets harbor significant XylT activity that is released upon activation with thrombin
-
XT-II mRNA expression is higher than for XT-I. Very low XT-I mRNA expression
-
XT-II mRNA expression is higher than for XT-I. Very low XT-I mRNA expression
-
XT-II mRNA expression is higher than for XT-I. Very low XT-I mRNA expression
-
XT-II mRNA expression is higher than for XT-I. Very low XT-I mRNA expression
mesenchymal stem cell. Xylosyltransferase 1 is the predominant xylosyltransferase in the early phase of chondrogenic stem cell differentiation and xylosyltransferase 2 is upregulated 7 days after induction
mesenchymal stem cell. Xylosyltransferase 1 is the predominant xylosyltransferase in the early phase of chondrogenic stem cell differentiation and xylosyltransferase 2 is upregulated 7 days after induction
-
XT-II mRNA expression is higher than for XT-I. Very low XT-I mRNA expression
-
of healthy and infertile men with oligo-, astheno- or teratozoospermia, and of men after vasectomy
additional information
elevated xylosyltransferase I activities in Pseudoxanthoma elasticum patients
increased activity of xylosyltransferase I in the blood serum of patients with connective tissue diseases
-
of JAR choriocarcinoma cells secrete six times more XT-I than the osteogenic sarcoma cell line SAOS-2 and 40times more XT-I than the fibroblast cell line hTERT-BJ1
-
XT-II mRNA expression is higher than for XT-I. Low XT-I mRNA expression
expresson of xylosyltransferase 2, no expression of xylosyltransferase 1
XT-II is exclusively expressed in liver tissues, in the HeLa cervical carcinoma cell line, and in K-562 erythroleukemia cells
-
XT-II mRNA expression is higher than for XT-I. Very low XT-I mRNA expression
expresson of xylosyltransferase 2, no expression of xylosyltransferase 1
expresson of xylosyltransferase 2, no expression of xylosyltransferase 1
XT-II is exclusively expressed in liver tissues, in the HeLa cervical carcinoma cell line, and in K-562 erythroleukemia cells
XT-II is highly expressed in liver, no XT-I mRNA is detectable in liver
-
of healthy and infertile men with oligo-, astheno- or teratozoospermia, and of men after vasectomy
additional information
-
activity in several human cell lines, culture supernatant, overview
additional information
-
enzyme activity in seminal plasma of infertile men is significantly reduced
additional information
-
equal expression levels of XT-I and XT-II in 1301 cells, WERI-RB-1 cells and HS-27 cells. In 3051/80 cells, SW-982 cells, MHH-ES-1 cells, hTERT-BJ1 cells and EFO-21 cells, XT-II mRNA expression is higher than for XT-I. In 23132/87 cells, XT-I mRNA expression is higher than for XT-II. In NCI-H510A cells, highest XT-I expression levels, XT-I mRNA expression is higher than for XT-II
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
for its complete Golgi retention, XT-I requires the N-terminal 214 amino acids
for its complete Golgi retention, XT-II requires the N-terminal 45 amino acids
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
the role of XT-I in osteoarthritis disease is examined. XT-I regulates glycosaminoglycan synthesis in human cartilage during early onset and late stage of osteoarthritis disease. Expression of XT-I gene is regulated by IL-1beta and by TGF-beta1. Forced expression of this enzyme by gene transfer in late stage osteoarthritis cartilage enhances glycosaminoglycan synthesis and stimulates cartilage repair
malfunction
-
LARGE gene silencing in Hep-G2 and HEK-EBNA cells does not affect SERPINC1 mRNA levels but significantly reduces the secretion of antithrombin with moderate intracellular retention
physiological function
physiological function
-
the single nucleotide polymorphism c.343G-T in XYLT1 exon 1 correlates with a significantly decreased glycosaminoglycan content in the serum of healthy blood donors. The two XYLT2 variations (c.166G-A in exon 2 and c.1253C-T in exon 6) reveal no changes in the serum glycosaminoglycan amount
physiological function
-
XylT-II fragments bind with low affinity to heparin. Prolonging of XylT-II fragments does not account for a cooperative effect of multiple heparin-binding motifs and in turn for a stronger heparin-binding. Two high polarity surface regions in the stem region with the sequence [-K-G-R-Q-R-K-P-R-P-] and [-G-R-R-H-G-R-W-], both representing Cardin-Weintraub motifs
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). XYLT1_HUMAN
959
1
107569
Swiss-Prot
Secretory Pathway (Reliability: 4)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
120000
97000
additional information
-
enzyme activity is also detected in a peak of MW 500000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C257A
2.3fold decrease in the ratio of Vmax to KM-value as compared to wild-type enzyme
C285A
5.4fold decrease in the ratio of Vmax to KM-value as compared to wild-type enzyme
C301A
2.3fold decrease in the ratio of Vmax to KM-value as compared to wild-type enzyme
C471A
complete loss of catalytic activity. N-phenylmaleimide treatment shows no effect on wild-type XT-I but strongly inactivates the cysteine mutant
C542A
2.9fold decrease in the ratio of Vmax to KM-value as compared to wild-type enzyme
C563A
2fold decrease in the ratio of Vmax to KM-value as compared to wild-type enzyme
C574A
complete loss of catalytic activity. N-phenylmaleimide treatment shows no effect on wild-type XT-I but strongly inactivates the cysteine mutant
C675A
1.5fold increase in the ratio of Vmax to KM-value as compared to wild-type enzyme
C902A
1.5fold increase in the ratio of Vmax to KM-value as compared to wild-type enzyme
C927A
1.4fold decrease in the ratio of Vmax to KM-value as compared to wild-type enzyme
C933A
1.36fold increase in the ratio of Vmax to KM-value as compared to wild-type enzyme
D314G
80% of the activity of wild-type enzyme,Km-value for bikunin is 1.2fold higher than wild-type value
D316G
as active as wild-type enzyme, Km-value for bikunin is identical to wild-type value
D745E
mutant retains full activity, Km-value for bikunin is 1.2fold higher than wild-type value
D747E
reduced substrate affinity, about 35% of the wild-type activity, Km-value for bikunin is 4.4fold higher than wild-type value
D747G
reduced substrate affinity, about 35% of the wild-type activity, Km-value for bikunin is 7.7fold higher than wild-type value
W746D
about 25% of wild-type activity, Km-value for bikunin is 1.3fold higher than wild-type value
W746G
about 25% of wild-type activity, Km-value for bikunin is 1.3fold higher than wild-type value
W746N
about 25% of wild-type activity, Km-value for bikunin is 1.4fold higher than wild-type value
DELTA1-184
-
KM-value for bikunin is identical to wild-type value, Vmax is 1.2fold higher than wild-type value
DELTA1-213
-
KM-value for bikunin is 1.6fold higher than wild-type value, Vmax is 1.1fold higher than wild-type value
DELTA1-260
-
KM-value for bikunin is 1.6fold higher than wild-type value, Vmax is identical to wild-type value
DELTA1-266
-
KM-value for bikunin is 5.6fold higher than wild-type value, Vmax is 1.6fold lower than wild-type value
DELTA1-272
-
KM-value for bikunin is 6fold higher than wild-type value, Vmax is 1.3fold lower than wild-type value
E263A
-
KM-value for bikunin is 1.4fold higher than wild-type value, Vmax is 2fold higher than wild-type value
K262A
-
KM-value for bikunin is 1.2fold higher than wild-type value, Vmax is 1.7fold higher than wild-type value
K272A
-
KM-value for bikunin is 1.4fold higher than wild-type value, Vmax is 1.7fold higher than wild-type value
R270A
-
KM-value for bikunin is 1.2fold higher than wild-type value, Vmax is 1.4fold higher than wild-type value
S266A
-
KM-value for bikunin is 1.4fold higher than wild-type value, Vmax is 1.3fold higher than wild-type value
S269A
-
KM-value for bikunin is 1.3fold higher than wild-type value, Vmax is 1.1fold higher than wild-type value
additional information
-
truncation of 266, 272 and 273 amino acids in the N-terminal region results in a 70, 90 and above 98% loss in catalytic activity. Deletion of the single 12 amino acid motif G261KEAISALSRAK272 leads to a loss-of-function xylosyltransferase I mutant. Heparin binding is slightly altered in mutants lacking 289 or 568 amino acids, but deletion of the potential heparin-binding motif P721KKVFKI727 does not lead to a loss of heparin binding capacity
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
reaching a temperature of 37Ā°C, XT-II has 66% of the activity compared with 30Ā°C
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
full-length XylT-II purified to homogeneity as inclusion bodies, by maltose binding protein affinity chromatography and heparin affinity chromatography
-
XylT-II purified by fractionated ammonium sulfate precipitation, heparin affinity and ion exchange chromatography, 7087fold with a final yield of 2.6%
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in CHO cells, high five insect cells, HEK293 cells, and SaOS-2 cells, and in Pichia pastoris
expressed in the xylosyltransferase-deficient pgsA-745 (S745) CHO cell line and in Pichia pastoris
expression in Pichia pastoris. Soluble form of human XT-II is expressed in the xylosyltransferase-deficient pgsA-745 (S745) Chinese hamster ovary cell line
expression of XT-I-GFP and various GFP-tagged XT-I mutants with C-terminal truncations and deletions in HEK-293 and SaOS-2 cells
soluble active form of human XT-I is expressed in High Five insect cells, Trichoplusia ni
DNA sequence determination and analysis, chromosome mapping, functional expression of isoforms XT-I and XT-II in CHO-K1 cells, no activity when XT-II is expressed fused to the aminoterminal peptide tag, 8% of the recombinant activity is located in the cytosol and membranes, 92% recombinant activity is secreted into the medium
-
expressed as glutathione-S-transferase fusion proteins containing putative or known GAG attachment sites of in vivo proteoglycans. Cloned into the XhoI and EcoRI digested pGEX-6P-1 vector and ligated by T4 DNA ligase. Expressed in Escherichia coli BL21 DE3 cells
-
expressed in CHO cells, high five insect cells, HEK293 cells, and SaOS-2 cells, and in Pichia pastoris
expressed in the xylosyltransferase-deficient pgsA-745 (S745) CHO cell line and in Pichia pastoris
expression in Pichia pastoris. Soluble form of human XT-II is expressed in the xylosyltransferase-deficient pgsA-745 (S745) Chinese hamster ovary cell line
expression in Pichia pastoris. Transfection of the xylosyltransferase-deficient Chinese hamster ovary mutant pgsA-745 with XT-II coding cDNA completely restores glycosaminoglycan biosynthesis
expression of various GFP-tagged XT-II mutants with C-terminal truncations and deletions in HEK-293 and SaOS-2 cells
into pGEX-6P-1, ligated into the multiple cloning site of the BamHI-digested and shrimp alkaline phosphatase-dephosphorylated pMAL-c4E expression vector, in frame with the N-terminal located maltose binding protein, expressed in Escherichia coli strain BL21(DE3) under the control of the IPTG inducible tac promoter. MBP/XylT-II fusion protein expressed in ER2507 that contains prolonged XylT-II fragments (MBP/XylT-IIF1-3 and MBP/XylT-IIF4-6)
-
soluble mutant enzymes of human XT-I with deletions at the N-terminal domain are expressed in insect cells
-
XylT-II cloned into the multiple cloning site of the pPICZ alphaA expression vector, in frame with the alpha-factor signal sequence and with a C-terminal located myc-epitope and hexa-histidine tag, expressed in Pichia pastoris strain X-33
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
members of the activator protein 1 and specificity protein 1 family of transcription factors are necessary for the transcriptional regulation of the XYLT1 gene. Transcription factors of the specificity protein 1 family, especially specificity protein 3, are very likely involved in the regulation of the XT-I mRNA expression. A 531-bp core promoter element is able to drive the transcription on a basal level. A binding site for transcription factors of the activator protein 1 family, which is essential for full promoter activity is located 730 bp 5' of the translation initiation site. A promoter element containing this binding site is able to drive the transcription to about 79fold above control in SW1353 chondrosarcoma cells
-
SW1353 cells treated with curcumin (0.02 mM) and tanshinone IIA (0.1 mM), respectively, for 6 h show significantly reduced XT-I mRNA expression to 41.8% and 13.8%, respectively. SW1353 cells treated with different concentrations (10 nM to 0.001 mM) of mithramycin A for 24 h show a highly significant decrease of XT-I mRNA levels compared with nontreated cells. mRNA level of both specificity protein 1 and specificity protein 3 is significantly reduced to less than 30% compared with controls treated with a scrambled siRNA for a total of 96 h after transfection. The siRNA-mediated knockdown of specificity protein 1 has no detectable effect on the XT-I mRNA levels, whereas the knockdown of specificity protein 3 leads to a highly significant reduction to ca. 40% compared with controls. Decrease of 51% in the enzyme xylosyltransferase activity in the cell culture supernatant of specificity protein 3 siRNA-transfected cells compared with controls 96 h after transfection
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
measurement of fibrosis marker xylosyltransferase I activity by HPLC electrospray ionization tandem mass spectrometry. The simple and robust LC-MS/MS assay permits the rapid and accurate determination of XT-I activity in human serum
medicine
diagnostics
-
the enzyme is a diagnostic marker of an enhanced proteoglycan biosynthesis
medicine
medicine
serum xylosyltransferase activity is a biochemical marker for the assessment of disease activity in systemic sclerosis and for the diagnosis of fibrotic remodeling processes. Sequence variations in the XT-I and XT-II coding genes are identified as risk factors for diabetic nephropathy, osteoarthritis or pseudoxanthoma elasticum. Important role of the xylosyltransferases as disease modifiers in pathologies which are characterized by an altered proteoglycan metabolism
medicine
serum xylosyltransferase I, the novel fibrosis marker, may be useful for the assessment of extracellular matrix alterations and disease activity in Pseudoxanthoma elasticum
medicine
serum xylosyltransferase activity is a biochemical marker for the assessment of disease activity in systemic sclerosis and for the diagnosis of fibrotic remodeling processes, sequence variations in the XT-I coding gene are identified as risk factors for diabetic nephropathy, osteoarthritis or pseudoxanthoma elasticum
medicine
serum xylosyltransferase activity is a biochemical marker for the assessment of disease activity in systemic sclerosis and for the diagnosis of fibrotic remodeling processes, sequence variations in the XT-II coding gene are identified as risk factors for diabetic nephropathy, osteoarthritis or pseudoxanthoma elasticum
medicine
-
monitoring of the seminal plasma for enzyme activity is proposed to be an advantegeous additional biochemical parameter to improve in vitro fertilization methods, because the activity is reduced in seminal plasma of infertile men
medicine
serum xylosyltransferase activity is a biochemical marker for the assessment of disease activity in systemic sclerosis and for the diagnosis of fibrotic remodeling processes. Sequence variations in the XT-I and XT-II coding genes are identified as risk factors for diabetic nephropathy, osteoarthritis or pseudoxanthoma elasticum. Important role of the xylosyltransferases as disease modifiers in pathologies which are characterized by an altered proteoglycan metabolism
medicine
-
serum XylT levels may be an informative biomarker in patients who suffer from diseases affecting platelet and/or liver homeostasis
medicine
-
ways of modulating the XYLT1 gene expression, especially in the development of therapeutic strategies for the treatment of fibrotic remodeling processes or cartilage repair
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Brinkmann, T.; Weilke, C.; Kleesiek, K.
Recognition of acceptor proteins by UDP-D-xylose proteoglycan core protein beta-D-xylosyltransferase
J. Biol. Chem.
272
11171-11175
1997
Homo sapiens
Götting, C.; Kuhn, J.; Brinkmann, T.; Kleesiek, K.
Xylosylation of alternatively spliced isoforms of Alzheimer APP by xylosyltransferase
J. Protein Chem.
17
295-302
1998
Homo sapiens, Rattus norvegicus, Rattus norvegicus Lewis1WR1
Kuhn, J.; Götting, C.; Schnolzer, M.; Kempf, T.; Brinkmann, T.; Kleesiek, K.
First isolation of human UDP-D-xylose:proteoglycan core protein beta-D-xylosyltransferase secreted from cultured JAR choriocarcinoma cells
J. Biol. Chem.
276
4940-4947
2001
Homo sapiens
Götting, C.; Kuhn, J.; Zahn, R.; Brinkmann, T.; Kleesiek, K.
Molecular cloning and expression of human UDP-D-xylose:proteoglycan core protein beta-D-xylosyltransferase and its first isoform XT-II
J. Mol. Biol.
304
517-528
2000
Homo sapiens, Rattus norvegicus
Götting, C.; Kuhn, J.; Brinkmann, T.; Kleesiek, K.
Xylosyltransferase activity in seminal plasma of infertile men
Clin. Chim. Acta
317
199-202
2002
Homo sapiens
Götting, C.; Kuhn, J.; Tinneberg, H.R.; Brinkmann, T.; Kleesiek, K.
High xylosyltransferase activities in human follicular fluid and cultured granulosa-lutein cells
Mol. Hum. Reprod.
8
1079-1086
2002
Homo sapiens
Meezan, E.; Manzella, S.; Roden, L.
Menage a trois: glycogenin, proteoglycan core protein xylosyltransferase and UDP-xylose
Trends Glycosci. Glycotechnol.
7
303-332
1995
Bos taurus, Gallus gallus, Homo sapiens, Mus musculus, Rattus norvegicus
-
Kuhn, J.; Muller, S.; Schnolzer, M.; Kempf, T.; Schon, S.; Brinkmann, T.; Schottler, M.; Gotting, C.; Kleesiek, K.
High-level expression and purification of human xylosyltransferase I in High Five insect cells as biochemically active form
Biochem. Biophys. Res. Commun.
312
537-544
2003
Homo sapiens
Kuhn, J.; Schnolzer, M.; Schon, S.; Muller, S.; Prante, C.; Gotting, C.; Kleesiek, K.
Xylosyltransferase I acceptor properties of fibroblast growth factor and its fragment bFGF (1-24)
Biochem. Biophys. Res. Commun.
333
156-166
2005
Homo sapiens
Müller, S.; Schöttler, M.; Schön, S.; Prante, C.; Brinkmann, T.; Kuhn, J.; Götting, C.; Kleesiek, K.
Human xylosyltransferase I: functional and biochemical characterization of cysteine residues required for enzymic activity
Biochem. J.
386
227-236
2005
Homo sapiens (Q86Y38)
Götting, C.; Müller, S.; Schöttler, M.; Schön, S.; Prante, C.; Brinkmann, T.; Kuhn, J.; Kleesiek, K.
Analysis of the DXD motifs in human xylosyltransferase I required for enzyme activity
J. Biol. Chem.
279
42566-42573
2004
Homo sapiens (Q86Y38)
Mueller, S.; Disse, J.; Schoettler, M.; Schoen, S.; Prante, C.; Brinkmann, T.; Kuhn, J.; Kleesiek, K.; Goetting, C.
Human xylosyltransferase I and N-terminal truncated forms: functional characterization of the core enzyme
Biochem. J.
394
163-171
2006
Homo sapiens
Goetting, C.; Kuhn, J.; Kleesiek, K.
Human xylosyltransferases in health and disease
Cell. Mol. Life Sci.
64
1498-1517
2007
Homo sapiens (Q86Y38), Homo sapiens (Q9H1B5), Homo sapiens
Kuhn, J.; Prante, C.; Schoen, S.; Goetting, C.; Kleesiek, K.
Measurement of fibrosis marker xylosyltransferase I activity by HPLC electrospray ionization tandem mass spectrometry
Clin. Chem.
52
2243-2249
2006
Homo sapiens (Q86Y38)
Brunner, A.; Kolarich, D.; Voglmeir, J.; Paschinger, K.; Wilson, I.B.
Comparative characterisation of recombinant invertebrate and vertebrate peptide O-xylosyltransferases
Glycoconj. J.
23
543-554
2006
Caenorhabditis elegans (Q965Q8), Caenorhabditis elegans, Drosophila melanogaster, Homo sapiens (Q86Y38), Homo sapiens
Schoen, S.; Prante, C.; Bahr, C.; Kuhn, J.; Kleesiek, K.; Goetting, C.
Cloning and recombinant expression of active full-length xylosyltransferase I (XT-I) and characterization of subcellular localization of XT-I and XT-II
J. Biol. Chem.
281
14224-14231
2006
Homo sapiens (Q86Y38), Homo sapiens (Q9H1B5), Homo sapiens
Poenighaus, C.; Ambrosius, M.; Casanova, J.C.; Prante, C.; Kuhn, J.; Esko, J.D.; Kleesiek, K.; Goetting, C.
Human xylosyltransferase II is involved in the biosynthesis of the uniform tetrasaccharide linkage region in chondroitin sulfate and heparan sulfate proteoglycans
J. Biol. Chem.
282
5201-5206
2007
Homo sapiens, Homo sapiens (Q9H1B5)
Voglmeir, J.; Voglauer, R.; Wilson, I.B.
XT-II, the second isoform of human peptide-O-xylosyltransferase, displays enzymatic activity
J. Biol. Chem.
282
5984-5990
2007
Homo sapiens (Q86Y38), Homo sapiens (Q9H1B5), Homo sapiens
Goetting, C.; Hendig, D.; Adam, A.; Schoen, S.; Schulz, V.; Szliska, C.; Kuhn, J.; Kleesiek, K.
Elevated xylosyltransferase I activities in Pseudoxanthoma elasticum (PXE) patients as a marker of stimulated proteoglycan biosynthesis
J. Mol. Med.
83
984-992
2005
Homo sapiens (Q86Y38), Homo sapiens
Casanova, J.C.; Kuhn, J.; Kleesiek, K.; Goetting, C.
Heterologous expression and biochemical characterization of soluble human xylosyltransferase II
Biochem. Biophys. Res. Commun.
365
678-684
2008
Homo sapiens (Q9H1B5), Homo sapiens
Prante, C.; Milting, H.; Kassner, A.; Farr, M.; Ambrosius, M.; Schoen, S.; Seidler, D.G.; Banayosy, A.E.; Koerfer, R.; Kuhn, J.; Kleesiek, K.; Goetting, C.
Transforming growth factor beta1-regulated xylosyltransferase I activity in human cardiac fibroblasts and its impact for myocardial remodeling
J. Biol. Chem.
282
26441-26449
2007
Homo sapiens (Q86Y38), Homo sapiens (Q9H1B5), Homo sapiens
Casanova, J.C.; Roch, C.; Kuhn, J.; Kleesiek, K.; Goetting, C.
First in-gel detection and purification of human xylosyltransferase II
Biochem. Biophys. Res. Commun.
379
243-248
2009
Homo sapiens
Casanova, J.C.; Ambrosius, M.; Kuhn, J.; Kleesiek, K.; Goetting, C.
Analysis of xylosyltransferase II binding to the anticoagulant heparin
Biochem. Biophys. Res. Commun.
383
4-10
2009
Homo sapiens
Roch, C.; Kuhn, J.; Kleesiek, K.; Goetting, C.
Differences in gene expression of human xylosyltransferases and determination of acceptor specificities for various proteoglycans
Biochem. Biophys. Res. Commun.
391
685-691
2010
Homo sapiens
Ambrosius, M.; Kleesiek, K.; Goetting, C.
The xylosyltransferase I gene polymorphism c.343G-T (p.A115S) is associated with decreased serum glycosaminoglycan levels
Clin. Biochem.
42
1-4
2009
Homo sapiens
Condac, E.; Dale, G.L.; Bender-Neal, D.; Ferencz, B.; Towner, R.; Hinsdale, M.E.
Xylosyltransferase II is a significant contributor of circulating xylosyltransferase levels and platelets constitute an important source of xylosyltransferase in serum
Glycobiology
19
829-833
2009
Homo sapiens, Mus musculus
Mueller, B.; Prante, C.; Kleesiek, K.; Goetting, C.
Identification and characterization of the human xylosyltransferase I gene promoter region
J. Biol. Chem.
284
30775-30782
2009
Homo sapiens
Venkatesan, N.; Barre, L.; Bourhim, M.; Magdalou, J.; Mainard, D.; Netter, P.; Fournel-Gigleux, S.; Ouzzine, M.
Xylosyltransferase-I regulates glycosaminoglycan synthesis during the pathogenic process of human osteoarthritis
PLoS ONE
7
e34020
2012
Homo sapiens (Q86Y38)
Takeuchi, H.; Fernandez-Valdivia, R.C.; Caswell, D.S.; Nita-Lazar, A.; Rana, N.A.; Garner, T.P.; Weldeghiorghis, T.K.; Macnaughtan, M.A.; Jafar-Nejad, H.; Haltiwanger, R.S.
Rumi functions as both a protein O-glucosyltransferase and a protein O-xylosyltransferase
Proc. Natl. Acad. Sci. USA
108
16600-16605
2011
Homo sapiens, Mus musculus
de la Morena-Barrio, M.; Buil, A.; Anton, A.; Martinez-Martinez, I.; Minano, A.; Gutierrez-Gallego, R.; Navarro-Fernandez, J.; Aguila, S.; Souto, J.; Vicente, V.; Soria, J.; Corral, J.
Identification of antithrombin-modulating genes. Role of LARGE, a gene encoding a bifunctional glycosyltransferase, in the secretion of proteins?
PLoS ONE
8
e64998
2013
Homo sapiens
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