Information on EC 2.4.2.26 - protein xylosyltransferase

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The expected taxonomic range for this enzyme is: Bilateria

EC NUMBER
COMMENTARY
2.4.2.26
-
RECOMMENDED NAME
GeneOntology No.
protein xylosyltransferase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
transfers a beta-D-xylosyl residue from UDP-D-xylose to the serine hydroxy group of an acceptor protein substrate
show the reaction diagram
most probable mechanism: ordered single displacement with UDPxylose as the leading substrate and the xylosylated peptide as the first product released
-
transfers a beta-D-xylosyl residue from UDP-D-xylose to the serine hydroxy group of an acceptor protein substrate
show the reaction diagram
chondroitin sulfate attachment site, determination of the consensus sequence for the recognition signal of the enzyme
-
transfers a beta-D-xylosyl residue from UDP-D-xylose to the serine hydroxy group of an acceptor protein substrate
show the reaction diagram
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
BRENDA Link
KEGG Link
MetaCyc Link
glycoaminoglycan-protein linkage region biosynthesis
-
-
Glycosaminoglycan biosynthesis - chondroitin sulfate / dermatan sulfate
-
-
Glycosaminoglycan biosynthesis - heparan sulfate / heparin
-
-
Metabolic pathways
-
-
SYSTEMATIC NAME
IUBMB Comments
UDP-D-xylose:protein beta-D-xylosyltransferase
Involved in the biosynthesis of the linkage region of glycosaminoglycan chains as part of proteoglycan biosynthesis (chondroitin, dermatan and heparan sulfates).
SYNONYMS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
peptide O-xylosyltransferase
Q965Q8
-
peptide O-xylosyltransferase
-
-
peptide O-xylosyltransferase
Q86Y38, Q9H1B5
-
peptide O-xylosyltransferase 1
Q86Y38, Q9H1B5
-
peptide-O-xylosyltransferase
Q86Y38, Q9H1B5
-
Rumi
-
in addition to protein O-glucosyltransferase activity, both human and mouse Rumi also show protein O-xylosyltransferase activity
squashed vulva protein 6
Q965Q8
-
UDP-alpha-D-xyloase:proteoglycan core protein beta-D-xylosyltransferase
-
-
UDP-alpha-D-xyloase:proteoglycan core protein beta-D-xylosyltransferase
-
-
UDP-alpha-D-xylose:proteoglycan core protein beta-D-xylosyltransferase
Q965Q8
-
UDP-alpha-D-xylose:proteoglycan core protein beta-D-xylosyltransferase
-
-
UDP-alpha-D-xylose:proteoglycan core protein beta-D-xylosyltransferase
Q86Y38
-
UDP-D-xylose:core protein beta-D-xylosyltransferase
-
-
-
-
UDP-D-xylose:core protein beta-D-xylosyltransferase
-
-
UDP-D-xylose:core protein xylosyltransferase
-
-
-
-
UDP-D-xylose:proteoglycan core protein b-d-xylosyltransferase
Q86Y38, Q9H1B5
-
UDP-D-xylose:proteoglycan core protein beta-D-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
-
2 isoforms XT-I and XT-II
XT
Rattus norvegicus Lewis1WR1
-
-
-
XT-I
Q86Y38
; isozyme
XT-II
Q9H1B5
; isozyme
xylosyltransferase
-
-
xylosyltransferase 1
Q86Y38
-
xylosyltransferase 2
Q9H1B5
-
xylosyltransferase I
Q86Y38
-
xylosyltransferase I
Q86Y38
; isozyme
xylosyltransferase I
Q86Y38
isozyme
xylosyltransferase I
-
-
xylosyltransferase II
-
-
xylosyltransferase II
Q9H1B5
-
xylosyltransferase II
Q9H1B5
isoform of xylosyltransferase I
xylosyltransferase II
Q9H1B5
isozyme
xylosyltransferase II
-
-
xylosyltransferase sqv-6
Q965Q8
-
xylosyltransferase, uridine diphosphoxylose-core protein beta-
-
-
-
-
xylosyltransferase-I
Q86Y38
-
xylosyltransferases II
Q9H1B5
isozyme
XylT-I
-
-
XylT-I
Q86Y38
-
XylT-II
Q9H1B5
-
XYLT1
Q86Y38
-
XYLT1
-
-
XYLT2
-
-
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
CAS REGISTRY NUMBER
COMMENTARY
55576-38-0
-
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
-
in Xylt2-/- mice total XylT activity is decreased ca. 99% as compared to Xylt2+/+ mice
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
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
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
UDP + fragment(1-24) of human basic fibroblast growth factor
UDP + ?
show the reaction diagram
-
-
-
-
?
UDP + human basic fibroblast growth factor
UDP + ?
show the reaction diagram
-
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 + acceptor protein substrate
UDP + acceptor protein substrate proteoglycan core protein
show the reaction diagram
-
-
-
-
?
UDP-D-xylose + acceptor protein substrate
UDP + acceptor protein substrate proteoglycan core protein
show the reaction diagram
-
-
-
?
UDP-D-xylose + acceptor protein substrate
UDP + acceptor protein substrate proteoglycan core protein
show the reaction diagram
-
exogenous protein acceptor obtained by Smith degradation of bovine chondroitin sulfate-protein complex
-
-
?
UDP-D-xylose + acceptor protein substrate
UDP + acceptor protein substrate proteoglycan core protein
show the reaction diagram
-
transfers a beta-D-xylosyl residue from UDP-D-xylose to the serine hydroxyl group of an acceptor protein substrate
-
-
?
UDP-D-xylose + acceptor protein substrate
UDP + acceptor protein substrate proteoglycan core protein
show the reaction diagram
-
transfers a beta-D-xylosyl residue from UDP-D-xylose to the serine hydroxyl group of an acceptor protein substrate
-
?
UDP-D-xylose + acceptor protein substrate
UDP + acceptor protein substrate proteoglycan core protein
show the reaction diagram
-
transfers a beta-D-xylosyl residue from UDP-D-xylose to the serine hydroxyl group of an acceptor protein substrate
-
?
UDP-D-xylose + acceptor protein substrate
UDP + acceptor protein substrate proteoglycan core protein
show the reaction diagram
-
transfers a beta-D-xylosyl residue from UDP-D-xylose to the serine hydroxyl group of an acceptor protein substrate
-
?
UDP-D-xylose + acceptor protein substrate
UDP + acceptor protein substrate proteoglycan core protein
show the reaction diagram
-
transfers a beta-D-xylosyl residue from UDP-D-xylose to the serine hydroxyl group of an acceptor protein substrate
-
?
UDP-D-xylose + acceptor protein substrate
UDP + acceptor protein substrate proteoglycan core protein
show the reaction diagram
-
transfers a beta-D-xylosyl residue from UDP-D-xylose to the serine hydroxyl group of an acceptor protein substrate
-
?
UDP-D-xylose + acceptor protein substrate
UDP + acceptor protein substrate proteoglycan core protein
show the reaction diagram
-
transfers a beta-D-xylosyl residue from UDP-D-xylose to the serine hydroxyl group of an acceptor protein substrate
-
?
UDP-D-xylose + acceptor protein substrate
UDP + acceptor protein substrate proteoglycan core protein
show the reaction diagram
-
transfers a beta-D-xylosyl residue from UDP-D-xylose to the serine hydroxyl group of an acceptor protein substrate
-
?
UDP-D-xylose + acceptor protein substrate
UDP + acceptor protein substrate proteoglycan core protein
show the reaction diagram
-
transfers a beta-D-xylosyl residue from UDP-D-xylose to the serine hydroxyl group of an acceptor protein substrate
-
?
UDP-D-xylose + acceptor protein substrate
UDP + acceptor protein substrate proteoglycan core protein
show the reaction diagram
-
transfers a beta-D-xylosyl residue from UDP-D-xylose to the serine hydroxyl group of an acceptor protein substrate
-
-
?
UDP-D-xylose + acceptor protein substrate
UDP + acceptor protein substrate proteoglycan core protein
show the reaction diagram
-
transfers a beta-D-xylosyl residue from UDP-D-xylose to the serine hydroxyl group of an acceptor protein substrate
-
?
UDP-D-xylose + acceptor protein substrate
UDP + acceptor protein substrate proteoglycan core protein
show the reaction diagram
-
transfers a beta-D-xylosyl residue from UDP-D-xylose to the serine hydroxyl group of an acceptor protein substrate
-
?
UDP-D-xylose + acceptor protein substrate
UDP + acceptor protein substrate proteoglycan core protein
show the reaction diagram
-
transfers a beta-D-xylosyl residue from UDP-D-xylose to the serine hydroxyl group of an acceptor protein substrate
-
?
UDP-D-xylose + acceptor protein substrate
UDP + acceptor protein substrate proteoglycan core protein
show the reaction diagram
-
transfers a beta-D-xylosyl residue from UDP-D-xylose to the serine hydroxyl group of an acceptor protein substrate
-
?
UDP-D-xylose + acceptor protein substrate
UDP + acceptor protein substrate proteoglycan core protein
show the reaction diagram
-
tryptic and chymotryptic fragments from fibroin
-
-
?
UDP-D-xylose + acceptor protein substrate
UDP + acceptor protein substrate proteoglycan core protein
show the reaction diagram
-
transfers a beta-D-xylosyl residue to specific serine residues dependent on the consensus signal sequence
-
?
UDP-D-xylose + acceptor protein substrate
UDP + acceptor protein substrate proteoglycan core protein
show the reaction diagram
-
transfers a beta-D-xylosyl residue to specific serine residues dependent on the consensus signal sequence
-
?
UDP-D-xylose + acceptor protein substrate
UDP + acceptor protein substrate proteoglycan core protein
show the reaction diagram
-
transfers a beta-D-xylosyl residue to specific serine residues dependent on the consensus signal sequence
-
?
UDP-D-xylose + acceptor protein substrate
UDP + acceptor protein substrate proteoglycan core protein
show the reaction diagram
Rattus norvegicus Lewis1WR1
-
transfers a beta-D-xylosyl residue from UDP-D-xylose to the serine hydroxyl group of an acceptor protein substrate, transfers a beta-D-xylosyl residue to specific serine residues dependent on the consensus signal sequence
-
?
UDP-D-xylose + acceptor protein substrate
UDP + acceptor protein substrate with xyloserine
show the reaction diagram
-
-
-
-
-
UDP-D-xylose + acceptor protein substrate
UDP + acceptor protein substrate with xyloserine
show the reaction diagram
-
-
-
-
-
UDP-D-xylose + acceptor protein substrate
UDP + acceptor protein substrate with xyloserine
show the reaction diagram
-
-
-
-
-
UDP-D-xylose + acceptor protein substrate
UDP + acceptor protein substrate with xyloserine
show the reaction diagram
-
-
-
-
-
UDP-D-xylose + acceptor protein substrate
UDP + acceptor protein substrate with xyloserine
show the reaction diagram
-
initiation of chondroitin sulfate biosynthesis
-
-
-
UDP-D-xylose + acceptor protein substrate
UDP + acceptor protein substrate with xyloserine
show the reaction diagram
-
enzyme may play a role in maintaining the haemostatic potential of the follicular fluid, enzyme is associated with large chondroitin sulfate-containing proteoglycans
-
-
-
UDP-D-xylose + acceptor protein substrate
UDP + acceptor protein substrate with xyloserine
show the reaction diagram
-
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-D-xylose + acceptor protein substrate
UDP + acceptor protein substrate with xylosylserine
show the reaction diagram
-
initiates the biosynthesis of the glycosaminoglycan linkage region
-
-
?
UDP-D-xylose + acceptor protein substrate
O-xylosyl-acceptor protein substrate
show the reaction diagram
-
Rumi transfers Xyl or 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 + acceptor protein substrate
UDP + O-xylosyl-acceptor protein substrate
show the reaction diagram
-
Rumi transfers Xyl or 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 + aggrecan
UDP + ?
show the reaction diagram
-
-
-
-
?
UDP-D-xylose + bamcan
UDP + ?
show the reaction diagram
-
-
-
-
?
UDP-D-xylose + betaglycan-1
UDP + ?
show the reaction diagram
-
-
-
-
?
UDP-D-xylose + bFGF-peptide
UDP + ?
show the reaction diagram
-
-
-
-
?
UDP-D-xylose + biglycan
UDP + D-xylosyl-biglycan
show the reaction diagram
-
-
-
-
?
UDP-D-xylose + biglycan
UDP + D-xylosyl-biglycan
show the reaction diagram
Q9H1B5
-
-
-
?
UDP-D-xylose + biglycan
UDP + xylosyl-biglycan
show the reaction diagram
Q9H1B5
-
-
-
?
UDP-D-xylose + bikunin
UDP + xylosyl-bikunin
show the reaction diagram
-
-
-
-
?
UDP-D-xylose + bikunin
UDP + xylosyl-bikunin
show the reaction diagram
Q86Y38
-
-
-
?
UDP-D-xylose + bikunin
UDP + xylosyl-bikunin
show the reaction diagram
-
-
-
-
?
UDP-D-xylose + bikunin
UDP + xylosyl-bikunin
show the reaction diagram
Q9H1B5
-
-
-
?
UDP-D-xylose + bikunin
UDP + xylosyl-bikunin
show the reaction diagram
-
recombinant bikunin
bound to serine residue
?
UDP-D-xylose + bikunin
UDP + xylosyl-bikunin
show the reaction diagram
-
recombinant wild-type from Chang liver hepatocytes and mutant, expressed in Escherichia coli
bound to serine residue
?
UDP-D-xylose + bikunin
UDP + xylosyl-bikunin
show the reaction diagram
-
recombinant mutant bikunin
-
?
UDP-D-xylose + bikunin
UDP + xylosyl-bikunin
show the reaction diagram
-
recombinant mutant bikunin
bound to serine residue
?
UDP-D-xylose + bikunin
UDP + xylosyl-bikunin
show the reaction diagram
-
recombinant mutant bikunin
bound to serine residue
?
UDP-D-xylose + bikunin
UDP + xylosyl-bikunin
show the reaction diagram
Rattus norvegicus Lewis1WR1
-
recombinant mutant bikunin
-
?
UDP-D-xylose + bikunin
UDP + ?
show the reaction diagram
-
-
-
-
?
UDP-D-xylose + bikunin
UDP + ?
show the reaction diagram
-
-
-
-
?
UDP-D-xylose + bikunin
?
show the reaction diagram
-
-
-
-
?
UDP-D-xylose + bikunin
UDP + D-xylosyl-bikunin
show the reaction diagram
Q9H1B5
-
-
-
?
UDP-D-xylose + bikunin
UDP + D-xylosyl-bikunin
show the reaction diagram
-
-
-
-
?
UDP-D-xylose + bikunin-derived aminoterminus homologous peptide
UDP + xylosyl-serine bikunin-derived aminoterminus homologous peptide
show the reaction diagram
-
-
-
?
UDP-D-xylose + Bio-QEEEGSGGGQKK-F
?
show the reaction diagram
-
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-QEEEGS(D-xylosyl)GGGQKK(5-fluorescein)-CONH2
show the reaction diagram
-
best substrate known so far for XT-IImediated xylosylation
-
-
?
UDP-D-xylose + biotin-NH-QEEEGSGGGQKK(5-fluorescein)-CONH2
UDP + biotin-NH-QEEEG-(D-xylosyl)SGGGQKK(5-fluorescein)-CONH2
show the reaction diagram
-
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
show the reaction diagram
Q9H1B5
-
-
-
?
UDP-D-xylose + biotin-NHQEEEGSGGGQKK(5-fluorescein)-CONH2
UDP + biotin-NHQEEEG-(D-xylosyl)SGGGQKK(5-fluorescein)-CONH2
show the reaction diagram
-
-
-
-
?
UDP-D-xylose + biotin-NHQEEEGSGGGQKK(5-fluorescein)-CONH2
UDP + biotin-NHQEEEG-(D-xylosyl)SGGGQKK(5-fluorescein)-CONH2
show the reaction diagram
-
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
show the reaction diagram
Q9H1B5
biotin-NHQEEEGSGGGQKK(5-fluorescein)-CONH2is the best acceptor for isozyme XT-II
-
-
?
UDP-D-xylose + cartilage chondroitin sulfate proteoglycan
UDP + cartilage chondroitin sulfate proteoglycan with xylosylserine
show the reaction diagram
-
HF-deglycosylated acceptor, the consensus sequence, acidic-acidic-Xxx-Ser-Gly-Xxx-Gly, in the acceptor proteoglycan is important
-
-
?
UDP-D-xylose + cartilage chondroitin sulfate proteoglycan
UDP + cartilage chondroitin sulfate proteoglycan with xylosylserine
show the reaction diagram
-
degraded by hydrogen fluoride or trifluromethanesulfonic acid
-
-
?
UDP-D-xylose + cartilage chondroitin sulfate proteoglycan
UDP + cartilage chondroitin sulfate proteoglycan with xylosylserine
show the reaction diagram
-
deglycosylation by Staphylococcus aureus V8 protease decreases the activity with the resulting peptides
-
-
?
UDP-D-xylose + cartilage proteoglycan
UDP + cartilage proteoglycan with xylosylserine
show the reaction diagram
-
Smith-degraded or HF-treated
-
-
?
UDP-D-xylose + cartilage proteoglycan
UDP + cartilage proteoglycan with xylosylserine
show the reaction diagram
-
modified substrate degradation method
-
-
?
UDP-D-xylose + CD44
UDP + ?
show the reaction diagram
-
-
-
-
?
UDP-D-xylose + CDEASGIGPDDRD
UDP + ?
show the reaction diagram
-
-
-
-
?
UDP-D-xylose + CDEASGIGPEVPDDRD
UDP + CDEAS(-D-xylose)GIGPEVPDDRD
show the reaction diagram
-
synthetic peptide
-
-
?
UDP-D-xylose + collagen alpha2(IX)
UDP + ?
show the reaction diagram
-
-
-
-
?
UDP-D-xylose + DDDSIEGSGGR
UDP + ?
show the reaction diagram
-
-
-
-
?
UDP-D-xylose + DDDSIEGSGGR
UDP + DDDSIEG(D-xylosyl)SGGR
show the reaction diagram
-
syndecan peptide substrate
-
-
?
UDP-D-xylose + DDDSIEGSGSGGR
UDP + DDD(D-xylosyl)SIEGSGSGG
show the reaction diagram
-
-
-
-
?
UDP-D-xylose + DDDSIEGSGSGGR
UDP + DDD(D-xylosyl)SIEGSGSGG
show the reaction diagram
Q965Q8
-
-
-
?
UDP-D-xylose + DDDSIEGSGSGGR
UDP + DDD-(-D-xylosyl)SIEGSGSGG
show the reaction diagram
-
-
-
-
?
UDP-D-xylose + decorin (PG40) peptide
UDP + ?
show the reaction diagram
-
-
-
-
?
UDP-D-xylose + DSISGDDLGSGDLGSGDFQR
?
show the reaction diagram
-
-
-
-
?
UDP-D-xylose + DSISGDDLGSGDLGSGDFQR
?
show the reaction diagram
-
the enzyme modifies the peptide with up to two xylose residues
-
-
?
UDP-D-xylose + DSISGDDLGSGDLGSGDFQR
UDP + ?
show the reaction diagram
-
-
-
-
?
UDP-D-xylose + fibroblast growth factor 2
?
show the reaction diagram
-
-
-
-
?
UDP-D-xylose + fibroblast growth factor 2 fragment 1-24
?
show the reaction diagram
-
-
-
-
?
UDP-D-xylose + fibroblast growth factor 2 peptide
?
show the reaction diagram
Q9H1B5
-
-
-
?
UDP-D-xylose + FMLEDEASGIGP
UDP + FMLEDEAS(-D-xylose)GIGP
show the reaction diagram
-
synthetic peptide
-
-
?
UDP-D-xylose + Gln-Ser-Gly
UDP + Gln-(O-D-xylosyl)-Ser-Gly
show the reaction diagram
-
-
-
-
?
UDP-D-xylose + Gly-Ser-Gly
UDP + Gly-(O-D-xylosyl)Ser-Gly
show the reaction diagram
-
-
-
-
?
UDP-D-xylose + Gly-Ser-Gly-Ser-Gly-Ser-Gly-Ser-Gly-Ser
UDP + ?
show the reaction diagram
-
-
-
-
?
UDP-D-xylose + Gly-Thr-Gly
UDP + Gly-(O-D-xylosyl)-Thr-Gly
show the reaction diagram
-
-
-
-
?
UDP-D-xylose + glypican-1
UDP + ?
show the reaction diagram
-
-
-
-
?
UDP-D-xylose + GVEGSADFLK
UDP + GVEGS(-D-xylose)ADFLK
show the reaction diagram
-
derived from collagen X
-
?
UDP-D-xylose + HF-degraded chondroitin sulfate proteoglycan
UDP + ?
show the reaction diagram
-
-
-
-
?
UDP-D-xylose + HF-degraded chondroitin sulfate proteoglycan
UDP + ?
show the reaction diagram
-
-
-
-
?
UDP-D-xylose + KKDSGPY
UDP + KKDS(-D-xylose)GPY
show the reaction diagram
-
-
-
?
UDP-D-xylose + KTKGSGFFVF
UDP + KTKGS(-D-xylose)GFFVF
show the reaction diagram
-
-
-
?
UDP-D-xylose + L-APLP2
UDP + ?
show the reaction diagram
-
-
-
-
?
UDP-D-xylose + L-APP
UDP + ?
show the reaction diagram
-
-
-
-
?
UDP-D-xylose + neuroglycan C
UDP + ?
show the reaction diagram
-
-
-
-
?
UDP-D-xylose + NFDEIDRSGFGFN
UDP + NFDEIDRS(-D-xylose)GFGFN
show the reaction diagram
-
-
-
?
UDP-D-xylose + perlecan-1
UDP + ?
show the reaction diagram
-
-
-
-
?
UDP-D-xylose + perlecan-2
UDP + ?
show the reaction diagram
-
-
-
-
?
UDP-D-xylose + perlecan-3
UDP + ?
show the reaction diagram
-
-
-
-
?
UDP-D-xylose + phosphacan
UDP + ?
show the reaction diagram
-
-
-
-
?
UDP-D-xylose + PLVSSGEDEPK
UDP + ?
show the reaction diagram
-
derived from neurocan protein
D-xylose bound to a serine residue
?
UDP-D-xylose + proteoglycan core protein
UDP + proteoglycan core protein with xyloserine
show the reaction diagram
Q9H1B5
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
show the reaction diagram
Q9H1B5
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 + QEEEGSGGGGQR
UDP + QEEEG(-D-xylosyl)SGGGGQR
show the reaction diagram
Q965Q8
-
-
-
?
UDP-D-xylose + QEEEGSGGGGQR
UDP + QEEEG(D-xylosyl)SGGGGQR
show the reaction diagram
-
-
-
-
?
UDP-D-xylose + QEEEGSGGGGQR
UDP + QEEEG(D-xylosyl)SGGGGQR
show the reaction diagram
-
-
-
-
?
UDP-D-xylose + QEEEGSGGGGQR
UDP + QEEEG-(D-xylosyl)-S-GGGGQR
show the reaction diagram
-
-
-
-
?
UDP-D-xylose + QEEEGSGGGOK
UDP + QEEEGS(-D-xylose)GGGOK
show the reaction diagram
-
best substrate, peptide derived from bikunin
-
?
UDP-D-xylose + QEEEGSGGGQGG
UDP + QEEEGS(-D-xylose)GGGQGG
show the reaction diagram
-
peptide derived from bikunin
-
?
UDP-D-xylose + QEEEGSGGGQGG
UDP + ?
show the reaction diagram
-
bikunin-type peptide
-
-
?
UDP-D-xylose + QEEEGSGGGQK
UDP + ?
show the reaction diagram
-
-
-
-
?
UDP-D-xylose + QEEEGSGGGQKK
UDP + QEEEGS(-D-xylose)GGGQKK
show the reaction diagram
-
peptide derived from bikunin
-
?
UDP-D-xylose + QEEEGSGGGQKK
UDP + QEEEG-(D-xylosyl)SGGGQKK
show the reaction diagram
-
QEEEGSGGGQKK is a better acceptor substrate than TENEGSGLTNIK
-
-
?
UDP-D-xylose + QEEEGSGGGQKK
UDP + QEEEG-(D-xylosyl)SGGGQKK
show the reaction diagram
-
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 + QEEEGTGGGQGG
UDP + ?
show the reaction diagram
-
-
-
-
?
UDP-D-xylose + QGGGGSGGGQGG
UDP + ?
show the reaction diagram
-
-
-
-
?
UDP-D-xylose + rat L2 chondroitin sulfate
UDP + ?
show the reaction diagram
-
-
-
-
?
UDP-D-xylose + SAAYSGSGSG
UDP + ?
show the reaction diagram
-
-
-
-
?
UDP-D-xylose + SDDYSGSGSG
UDP + SDDYS(-D-xylose)GSGSG
show the reaction diagram
-
synthetic peptide
-
-
?
UDP-D-xylose + SDDYSGSGSG
UDP + ?
show the reaction diagram
-
-
-
-
?
UDP-D-xylose + SENEGSGMAEQK
UDP + SENEGS(-D-xylose)GMAEQK
show the reaction diagram
-
synthetic leukocyte-derived amyloid precursor-like protein homologous peptide
-
?
UDP-D-xylose + SENEGSGMAQQK
UDP + ?
show the reaction diagram
-
-
-
-
?
UDP-D-xylose + Ser-Gly-Ala-Gly-Ala-Gly
UDP + xylosyl-Ser-Gly-Ala-Gly-Ala-Gly
show the reaction diagram
-
silk sequence hexapeptide
-
-
?
UDP-D-xylose + Ser-Gly-Gly
UDP + O-D-xylosyl-Ser-Gly-Gly
show the reaction diagram
-
-
-
-
?
UDP-D-xylose + serglycin
UDP + ?
show the reaction diagram
-
-
-
-
?
UDP-D-xylose + SIEGSGGR
UDP + (D-xylosyl)SIEGSGGR
show the reaction diagram
Q965Q8
-
-
-
?
UDP-D-xylose + SIEGSGGR
UDP + D-xylosyl-SIEGSGGR
show the reaction diagram
-
-
-
-
?
UDP-D-xylose + SIEGSGGR
UDP + SIEG(D-xylosyl)SGGR
show the reaction diagram
-
-
-
-
?
UDP-D-xylose + silk fibroin
UDP + silk fibroin with xylosylserine
show the reaction diagram
-
-
-
?
UDP-D-xylose + silk fibroin
UDP + silk fibroin with xylosylserine
show the reaction diagram
-
-
-
-
?
UDP-D-xylose + silk fibroin
UDP + silk fibroin with xylosylserine
show the reaction diagram
-
-
-
?
UDP-D-xylose + silk fibroin
UDP + silk fibroin with xylosylserine
show the reaction diagram
Q9H1B5
-
-
-
?
UDP-D-xylose + silk fibroin
UDP + silk fibroin with xylosylserine
show the reaction diagram
-
-
-
-
?
UDP-D-xylose + silk fibroin
UDP + silk fibroin with xylosylserine
show the reaction diagram
-
acceptor substrate from Bombyx mori consists in large part of the repeating hexapeptide: Ser-Gly-Ala-Gly-Ala-Gly
-
-
?
UDP-D-xylose + silk fibroin
UDP + silk fibroin with xylosylserine
show the reaction diagram
-
acceptor substrate contains repetitive sequence Gly-Ser-Gly-Ala-Gly-Ala
-
-
?
UDP-D-xylose + silk fibroin
UDP + silk fibroin with xylosylserine
show the reaction diagram
-
silk fibroin is a low affinity acceptor for XT-II
-
-
?
UDP-D-xylose + silk fibroin
UDP + ?
show the reaction diagram
-
-
-
-
?
UDP-D-xylose + silk fibroin
?
show the reaction diagram
-
-
-
-
?
UDP-D-xylose + Smith-degraded chondroitin sulfate proteoglycan
UDP + ?
show the reaction diagram
-
-
-
-
?
UDP-D-xylose + Smith-degraded chondroitin sulfate proteoglycan
UDP + ?
show the reaction diagram
-
-
-
-
?
UDP-D-xylose + syndecan
UDP + ?
show the reaction diagram
-
-
-
-
?
UDP-D-xylose + syndecan-1
UDP + ?
show the reaction diagram
-
-
-
-
?
UDP-D-xylose + syndecan-4
UDP + ?
show the reaction diagram
-
-
-
-
?
UDP-D-xylose + TENEGSGLTNIK
UDP + TENEGS(-D-xylose)GLTNIK
show the reaction diagram
-
synthetic leukocyte-derived beta-A4-amyloid protein precursor homologous peptide
-
?
UDP-D-xylose + TENEGSGLTNIK
UDP + ?
show the reaction diagram
-
-
-
-
?
UDP-D-xylose + TENEGSGLTNIK
UDP + TENEG-(D-xylosyl)SGLTNIK
show the reaction diagram
-
QEEEGSGGGQKK is a better acceptor substrate than TENEGSGLTNIK
-
-
?
UDP-D-xylose + TENEGSGLTNIK
UDP + TENEG-(D-xylosyl)SGLTNIK
show the reaction diagram
-
the 3-A4-amyloid protein precursor protein peptide TENEGSGLTNIK is an acceptor substrate for XylT1
-
-
?
UDP-D-xylose + testican-2
UDP + ?
show the reaction diagram
-
-
-
-
?
UDP-D-xylose + thrombomodulin
UDP + ?
show the reaction diagram
-
-
-
-
?
UDP-D-xylose + VCRSGSGLVGK
UDP + VCRSGSGLVGK
show the reaction diagram
-
derived from apolipoprotein J
D-xylose bound to a serine residue
?
UDP-D-xylose + versican-beta
UDP + ?
show the reaction diagram
-
-
-
-
?
UDP-D-xylose + WAGGDASGE
UDP + WAGGDAS(-D-xylose)GE
show the reaction diagram
-
-
-
?
UDP-D-xylose + [Val36,Val38]delta1[Gly92,Ile94]delta2bikunin
UDP + ?
show the reaction diagram
-
-
-
-
?
additional information
?
-
-
-
-
-
-
additional information
?
-
-
substrate specificity
-
-
-
additional information
?
-
-
substrate preparation and specificity
-
-
-
additional information
?
-
-
tripeptide SGG is a poor substrate
-
-
-
additional information
?
-
-
very low activity with tripeptide SGG and peptide LNFSTGW
-
-
-
additional information
?
-
-
involved in the biosynthesis of the linkage region of proteochondroitin sulfate
-
-
-
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
?
-
-
synthesis of chondrioitin and heparan sulphates is initiated by UDP-alpha-D-xylose:proteoglycan core protein beta-D-xylosyltransferase
-
-
-
additional information
?
-
Q965Q8
synthesis of chondrioitin and heparan sulphates is initiated by UDP-alpha-D-xylose:proteoglycan core protein beta-D-xylosyltransferase
-
-
-
additional information
?
-
-
xylosyltransferase II is involved in the biosynthesis of the uniform tetrasaccharide linkage region in chondroitin sulfate and heparan sulfate proteoglycans, 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
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
UDP-D-xylose + acceptor protein substrate
UDP + acceptor protein substrate with xyloserine
show the reaction diagram
-
-
-
-
-
UDP-D-xylose + acceptor protein substrate
UDP + acceptor protein substrate with xyloserine
show the reaction diagram
-
-
-
-
-
UDP-D-xylose + acceptor protein substrate
UDP + acceptor protein substrate with xyloserine
show the reaction diagram
-
-
-
-
-
UDP-D-xylose + acceptor protein substrate
UDP + acceptor protein substrate with xyloserine
show the reaction diagram
-
-
-
-
-
UDP-D-xylose + acceptor protein substrate
UDP + acceptor protein substrate with xyloserine
show the reaction diagram
-
initiation of chondroitin sulfate biosynthesis
-
-
-
UDP-D-xylose + acceptor protein substrate
UDP + acceptor protein substrate with xyloserine
show the reaction diagram
-
enzyme may play a role in maintaining the haemostatic potential of the follicular fluid, enzyme is associated with large chondroitin sulfate-containing proteoglycans
-
-
-
UDP-D-xylose + acceptor protein substrate
UDP + acceptor protein substrate with xyloserine
show the reaction diagram
-
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-D-xylose + acceptor protein substrate
UDP + acceptor protein substrate with xylosylserine
show the reaction diagram
-
initiates the biosynthesis of the glycosaminoglycan linkage region
-
-
?
UDP-D-xylose + proteoglycan core protein
UDP + proteoglycan core protein with xyloserine
show the reaction diagram
Q9H1B5
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
show the reaction diagram
Q9H1B5
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
-
-
?
additional information
?
-
-
involved in the biosynthesis of the linkage region of proteochondroitin sulfate
-
-
-
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
?
-
-
synthesis of chondrioitin and heparan sulphates is initiated by UDP-alpha-D-xylose:proteoglycan core protein beta-D-xylosyltransferase
-
-
-
additional information
?
-
Q965Q8
synthesis of chondrioitin and heparan sulphates is initiated by UDP-alpha-D-xylose:proteoglycan core protein beta-D-xylosyltransferase
-
-
-
additional information
?
-
-
xylosyltransferase II is involved in the biosynthesis of the uniform tetrasaccharide linkage region in chondroitin sulfate and heparan sulfate proteoglycans, XT-II initiates the biosynthesis of both heparan sulfate and chondroitin sulfate
-
-
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
-
essentially required, Mg2+ and Mn2+ are equally effective
Ca2+
-
activates
Mg2+
-
essentially required, Ca2+ and Mn2+ are equally effective
Mg2+
-
-
Mg2+
-
necessity for Mg2+ or Mn2+ ions for enzymatic activity
Mn2+
-
essentially required, Mg2+ and Ca2+ are equally effective
Mn2+
-
-
Mn2+
-
necessity for Mg2+ or Mn2+ ions for enzymatic activity
additional information
-
active in the absence of any added cation; active in the absence of any added cation
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
beta-mercaptoethanol
-
XT-II activity is completely abolished at a concentration 1% (v/v) beta-mercaptoethanol
CDP
-
23% residual activity at 10 mg/ml
CMP
-
45% residual activity at 10 mg/ml
Co2+
-
Co2+ reduces activity by more than 60% at 5 mM
CTP
-
8% residual activity at 10 mg/ml
Cu2+
-
enzyme activity is abolished by Cu2+
Cu2+
-
complete inhibition at 5 mM
dithiothreitol
-
XT-II activity is completely abolished at a concentration of 1 mM dithiothreitol
Glycosaminoglycans
-
associate with the enzyme
-
heparin
-
non-competitive inhibitor using fragment(1-24) of human basic fibroblast growth factor as xylose acceptor
N-Phenylmaleimide
-
treatment shows no effect on wild-type XT-I but strongly inactivaets the cysteine mutants C461A and C574A
Ni2+
-
enzyme activity is abolished by Ni2+
Ni2+
-
complete inhibition at 5 mM
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
UDP
-
5% residual activity at 10 mg/ml
UMP
-
25% residual activity at 10 mg/ml
UTP
-
4% residual activity at 10 mg/ml
Zn2+
-
strong
Zn2+
-
enzyme activity is abolished by Zn2+
Zn2+
-
complete inhibition at 5 mM
additional information
-
competitive inhibition of the acceptor substrates
-
additional information
-
no inhibition by CDP
-
additional information
-
-
-
additional information
-
lysozyme does not change the activity of XT-II at any concentration
-
additional information
-
reduced total XylT activity in sera from mice possessing visible tumors as compared to controls
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
EDTA
-
84% activation at 25 mM
protamine
-
adding protamine to a final concentration of 0.1 mg/ml stimulates XT-II activity at least 2fold
Sodium citrate
-
72% activation at 25 mM
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
-
additional information
-
0.5-10 ng/ml transforming growth factor beta1 does not induce expression of isozyme XT-II
-
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
-
additional information
-
the c-Jun/activator protein-1 transcription factor is essential for full XYLT1 promoter activity in SW1353 cells
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0188
Aggrecan
-
isoenzyme XT-I
-
0.0179
bamcan
-
isoenzyme XT-II
-
0.0222
bamcan
-
isoenzyme XT-I
-
0.0208
betaglycan-1
-
isoenzyme XT-I
-
0.0093
bFGF-peptide
-
isoenzyme XT-II
-
0.0137
bFGF-peptide
-
isoenzyme XT-I
-
0.0097
biglycan
-
isoenzyme XT-I
-
0.0006
bikunin
-
recombinant mutant bikunin
-
0.0009
bikunin
-
recombinant wild-type bikunin
-
0.0009
bikunin
-
-
-
0.0009
bikunin
-
pH 6.5, 37C, mutant enzyme D316G; pH 6.5, 37C, wild-type enzyme
-
0.0009
bikunin
-
37C, pH 6.5; 37C, pH 6.5, mutant enzyme DELTA1-184
-
0.001
bikunin
-
pH 6.5, 37C, mutant enzyme C933A; pH 6.5, 37C, wild-type enzyme
-
0.0011
bikunin
-
pH 6.5, 37C, mutant enzyme D314G; pH 6.5, 37C, mutant enzyme D745E
-
0.0011
bikunin
-
37C, pH 6.5, mutant enzyme K262A; 37C, pH 6.5, mutant enzyme R270A
-
0.0012
bikunin
-
pH 6.5, 37C, mutant enzyme C920A
-
0.0012
bikunin
-
pH 6.5, 37C, mutant enzyme W746D; pH 6.5, 37C, mutant enzyme W746G
-
0.0012
bikunin
-
37C, pH 6.5, mutant enzyme S269A
-
0.0013
bikunin
-
pH 6.5, 37C, mutant enzyme W746N
-
0.0013
bikunin
-
37C, pH 6.5, mutant enzyme E263A; 37C, pH 6.5, mutant enzyme K272A; 37C, pH 6.5, mutant enzyme S266A
-
0.0014
bikunin
-
pH 6.5, 37C, mutant enzyme C301A; pH 6.5, 37C, mutant enzyme C675A
-
0.0014
bikunin
-
37C, pH 6.5, mutant enzyme DELTA1-213; 37C, pH 6.5, mutant enzyme DELTA1-260
-
0.0016
bikunin
-
pH 6.5, 37C, mutant enzyme C542A
-
0.002
bikunin
-
pH 6.5, 37C, mutant enzyme C927A
-
0.0028
bikunin
-
pH 6.5, 37C, mutant enzyme C285A
-
0.0044
bikunin
-
pH 6.5, 37C, mutant enzyme D747E
-
0.005
bikunin
-
37C, pH 6.5, mutant enzyme DELTA1-266
-
0.0053
bikunin
-
pH 6.5, 37C, mutant enzyme C257A
-
0.0054
bikunin
-
37C, pH 6.5, mutant enzyme DELTA1-272
-
0.0064
bikunin
-
isoenzyme XT-II with mutant bikunin (sequence QEE-GSGRGQLV)
-
0.0069
bikunin
-
pH 6.5, 37C, mutant enzyme D747G
-
0.0077
bikunin
-
isoenzyme XT-II with mutant bikunin (sequence QEEEGSGHNMLV)
-
0.0085
bikunin
-
isoenzyme XT-II with mutant bikunin (sequence QEEESSGGGQLV)
-
0.0093
bikunin
-
isoenzyme XT-II with mutant bikunin (sequence QEEEGSGSLALV)
-
0.0099
bikunin
-
isoenzyme XT-I with mutant bikunin (sequence QEEERSGGGQLV)
-
0.0103
bikunin
-
isoenzyme XT-I with mutant bikunin (sequence QEEESSGGGQLV)
-
0.0108
bikunin
-
-
-
0.0119
bikunin
-
pH 6.5, 37C, mutant enzyme C563A
-
0.0123
bikunin
-
isoenzyme XT-I with mutant bikunin (sequence QEE-GSGGGQLV)
-
0.0125
bikunin
-
isoenzyme XT-I with mutant bikunin (sequence QEEEGSGHNMLV)
-
0.0133
bikunin
-
isoenzyme XT-I with mutant bikunin (sequence QEEEGSSCGQLV)
-
0.0137
bikunin
-
isoenzyme XT-II with mutant bikunin (sequence QEEEGSGRRALV)
-
0.015
bikunin
-
isoenzyme XT-II with mutant bikunin (sequence QEEEGSGGRSVLV)
-
0.0151
bikunin
-
isoenzyme XT-I with mutant bikunin (sequence QEEEGSGCGQLV)
-
0.0153
bikunin
-
isoenzyme XT-I with mutant bikunin (sequence QEEEGSSGGQLV)
-
0.0199
bikunin
-
isoenzyme XT-I with mutant bikunin (sequence QEEEGSGSLALV)
-
0.02
bikunin
-
isoenzyme XT-I with mutant bikunin (sequence QKEEGSGGGQLV)
-
0.0205
bikunin
-
isoenzyme XT-I with mutant bikunin (sequence QEE-GSGRGQLV)
-
0.0215
bikunin
-
isoenzyme XT-II with mutant bikunin (sequence QEEEGSGCYKLV)
-
0.022
bikunin
-
; recombinant enzyme
-
0.0227
bikunin
-
isoenzyme XT-II with mutant bikunin (sequence QEEEGSGCGQLV)
-
0.0242
bikunin
-
isoenzyme XT-II with mutant bikunin (sequence QEEEGSGRHLLV)
-
0.0243
bikunin
-
isoenzyme XT-I with mutant bikunin (sequence QEEESSGRGQLV)
-
0.0251
bikunin
-
isoenzyme XT-I with mutant bikunin (sequence QEEEGSGGRSVLV)
-
0.0274
bikunin
-
isoenzyme XT-I with wild-type bikunin (sequence QEEEGSGGGQLV)
-
0.0288
bikunin
-
isoenzyme XT-I with mutant bikunin (sequence QEEEGSTSLV)
-
0.0301
bikunin
-
isoenzyme XT-I with mutant bikunin (sequence QEEEGSGCYKLV)
-
0.0318
bikunin
-
isoenzyme XT-I with mutant bikunin (sequence QLTTGSGGGQLV)
-
0.0356
bikunin
-
isoenzyme XT-II with mutant bikunin (sequence QKEEGSGGGQLV)
-
0.0462
bikunin
-
isoenzyme XT-II with wild-type bikunin (sequence QEEEGSGGGQLV)
-
0.0463
bikunin
-
isoenzyme XT-II
-
0.0508
bikunin
-
isoenzyme XT-II with mutant bikunin (sequence QEEEGSGCRVLV)
-
0.0543
bikunin
-
isoenzyme XT-I with mutant bikunin (sequence QEEEGSGCRVLV)
-
0.0572
bikunin
-
isoenzyme XT-I with mutant bikunin (sequence QEEEGSGRHLLV)
-
0.0586
bikunin
-
isoenzyme XT-I with mutant bikunin (sequence QEEEGSGRRALV)
-
0.0656
bikunin
-
isoenzyme XT-I with mutant bikunin (sequence QPQIGSGGGQLV)
-
0.022
bikunin-derived aminoterminus homologous peptide
-
-
-
0.0019
Bio-QEEEGSGGGQKK-F
-
-
0.0025
biotin-NH-QEEEGSGGGQKK(5-fluorescein)-CONH2
-
XylT-I
0.0052
biotin-NH-QEEEGSGGGQKK(5-fluorescein)-CONH2
-
-
0.0061
biotin-NH-QEEEGSGGGQKK(5-fluorescein)-CONH2
-
XylT-II
0.0052
biotin-NHQEEEGSGGGQKK(5-fluorescein)-CONH2
-
recombinant enzyme
0.11
cartilage chondroitin sulfate proteoglycan
-
-
-
0.155
cartilage chondroitin sulfate proteoglycan
-
trifluoromethanesulfonic acid-degraded substrate
-
0.19
cartilage chondroitin sulfate proteoglycan
-
hydrogen fluoride-degraded substrate
-
0.0146
CD44
-
isoenzyme XT-I
-
0.062
CDEASGIGPDDRD
-
-
0.062
CDEASGIGPEVPDDRD
-
-
0.0034
collagen alpha2(IX)
-
isoenzyme XT-I
-
0.5
DDDSIEGSGGR
-
-
0.037
decorin (PG40) peptide
-
-
-
0.062
fibroblast growth factor 2
-
recombinant enzyme
-
0.0191
fibroblast growth factor 2 fragment 1-24
-
-
-
0.12
FMLEDEASGIGP
-
-
-
0.0208
fragment(1-24) of human basic fibroblast growth factor
-
native XT-I
-
0.0223
fragment(1-24) of human basic fibroblast growth factor
-
recombinant XT-I
-
8.5
Gln-Ser-Gly
-
-
28
Gly-Ser-Gly
-
-
0.04
Gly-Ser-Gly-Ser-Gly-Ser-Gly-Ser-Gly-Ser
-
0.2 mM in terms of Ser
87
Gly-Thr-Gly
-
-
0.0109
glypican-1
-
isoenzyme XT-II
-
0.0171
glypican-1
-
isoenzyme XT-I
-
2.67
GVEGSADFLK
-
-
-
0.00011
HF-degraded chondroitin sulfate proteoglycan
-
-
-
0.0029
HF-degraded chondroitin sulfate proteoglycan
-
-
-
1.02
HF-degraded chondroitin sulfate proteoglycan
-
-
-
0.0572
human basic fibroblast growth factor
-
native XT-I
-
8.27
KKDSGPY
-
-
3.625
KTKGSGFFVF
-
-
0.0104
L-APLP2
-
isoenzyme XT-II
-
0.0134
L-APLP2
-
isoenzyme XT-I
-
0.0032
neuroglycan C
-
isoenzyme XT-II
-
0.0236
neuroglycan C
-
isoenzyme XT-I
-
0.13
NFDEIDRSGFGFN
-
-
0.0133
perlecan-1
-
isoenzyme XT-I
-
0.0102
perlecan-2
-
isoenzyme XT-II
-
0.0145
perlecan-2
-
isoenzyme XT-I
-
0.0094
perlecan-3
-
isoenzyme XT-II
-
0.0187
perlecan-3
-
isoenzyme XT-I
-
0.0166
phosphacan
-
isoenzyme XT-I
-
0.39
PLVSSGEDEPK
-
-
0.022
QEEEGSGGGOK
-
-
-
0.008
QEEEGSGGGQGG
-
-
-
0.022
QEEEGSGGGQK
-
-
0.01172
QEEEGSGGGQKK
-
in Xylt2
-
0.02048
QEEEGSGGGQKK
-
in Xylt1
-
0.093
QEEEGSGGGQKK
-
-
-
0.82
QEEEGTGGGQGG
-
-
-
8.6
QGGGGSGGGQGG
-
-
-
0.26
rat L2 chondroitin sulfate
-
-
-
1.39
SAAYSGSGSG
-
-
0.79
SDDYSGSGSG
-
-
-
0.019
SENEGSGMAEQK
-
-
0.019
SENEGSGMAQQK
-
-
20
Ser-Gly-Gly
-
-
-
55
Ser-Gly-Gly
-
-
-
0.0023
serglycin
-
isoenzyme XT-II
-
0.0111
serglycin
-
isoenzyme XT-I
-
0.545
silk fibroin
-
-
-
0.545
silk fibroin
-
-
-
0.677
silk fibroin
-
; recombinant enzyme
-
0.064
Smith-degraded chondroitin sulfate proteoglycan
-
-
-
0.18
Smith-degraded chondroitin sulfate proteoglycan
-
-
-
0.155
Smith-degraded chondroitin sulphate proteoglycan
-
-
-
0.0122
syndecan
-
isoenzyme XT-II
-
0.0178
syndecan
-
isoenzyme XT-I
-
0.0074
syndecan-1
-
isoenzyme XT-II
-
0.0198
syndecan-1
-
isoenzyme XT-I
-
0.0035
syndecan-4
-
isoenzyme XT-I
-
0.0141
syndecan-4
-
isoenzyme XT-II
-
0.02
TENEGSGLTNIK
-
-
0.2132
TENEGSGLTNIK
-
in Xylt1
0.3905
TENEGSGLTNIK
-
in Xylt2
0.0082
testican-2
-
isoenzyme XT-II
-
0.0103
testican-2
-
isoenzyme XT-I
-
0.0029
Thrombomodulin
-
isoenzyme XT-II
-
0.0182
Thrombomodulin
-
isoenzyme XT-I
-
0.0065
UDP-D-xylose
-
-
0.01
UDP-D-xylose
-
cosubstrate: Smith-degraded chondroitin sulfate
0.019
UDP-D-xylose
-
Smith-degraded proteoglycan, value on serine basis
0.025
UDP-D-xylose
-
-
0.1
UDP-D-xylose
-
cosubstrate: DDDSIEGSGGR
0.18
UDP-D-xylose
-
; cosubstrate: CDEASGIGPDDRD
0.25
UDP-D-xylose
-
about
0.0065
UDP-xylose
-
cosubstrate: QEEEGSGGGQGG
0.94
VCRSGSGLVGK
-
-
-
0.0127
versican-beta
-
isoenzyme XT-II
-
0.0146
versican-beta
-
isoenzyme XT-I
-
0.42
WAGGDASGE
-
-
-
0.0008
[Val36,Val38]delta1[Gly92,Ile94]delta2bikunin
-
-
0.0131
L-APP
-
XT-I
-
additional information
additional information
-
-
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0363
biotin-NH-QEEEGSGGGQKK(5-fluorescein)-CONH2
-
XylT-I or XylT-II
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
5.95
biotin-NH-QEEEGSGGGQKK(5-fluorescein)-CONH2
-
XylT-II
14214
14.52
biotin-NH-QEEEGSGGGQKK(5-fluorescein)-CONH2
-
XylT-II
14214
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00007
heparin
-
pH 6.5, 37C, mutant enzyme D745E
0.00011
heparin
-
pH 6.5, 37C, mutant enzyme D747E; pH 6.5, 37C, mutant enzyme W746N
0.00012
heparin
-
pH 6.5, 37C, mutant enzyme W746G; pH 6.5, 37C, wild-type enzyme
0.00013
heparin
-
pH 6.5, 37C, mutant enzyme W746D
0.00014
heparin
-
pH 6.5, 37C, mutant enzyme D316G
0.0019
UDP
-
pH 6.5, 37C, mutant enzyme D745E
0.0072
UDP
-
pH 6.5, 37C, mutant enzyme D314G
0.0108
UDP
-
pH 6.5, 37C, wild-type enzyme
0.0113
UDP
-
pH 6.5, 37C, mutant enzyme D316G
0.0147
UDP
-
pH 6.5, 37C, mutant enzyme D747E
0.0172
UDP
-
pH 6.5, 37C, mutant enzyme D747G
0.0179
UDP
-
pH 6.5, 37C, mutant enzyme W746N
0.0196
UDP
-
pH 6.5, 37C, mutant enzyme W746D
0.0246
UDP
-
pH 6.5, 37C, mutant enzyme W746G
0.00015
heparin
-
pH 6.5, 37C, mutant enzyme D314G; pH 6.5, 37C, mutant enzyme D747G
additional information
additional information
-
competitive inhibition of the acceptor substrates
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.0000003
-
XylT-II, concentrated culture supernatant
0.002333
-
7087fold purified XylT-II
0.0285
-
purified enzyme
0.419
-
purified enzyme
additional information
-
-
additional information
-
enzyme assay
additional information
-
activity in several human cell lines, overview
additional information
-
activity in several tissues, overview
additional information
-
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.5 - 7
-
-
6.5
-
assay at
7
-
depends on buffer system
7.5 - 8
-
;
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.7 - 7.5
-
half-maximal activity at pH 5.7 and pH 7.5
6.5 - 8.5
-
pH 6.5: about 70% of maximal activity, pH 8.5: about 60% of maximal activity
6.5 - 9
-
pH 6.5: about 60% of maximal activity, pH 9.0: about 60% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
34
-
assay at
37
-
assay at
37
-
assay at
37
-
assay at
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4 - 45
-
-
15 - 37
-
15C: about 40% of maximal activity, 37C: maximal activity
16 - 37
-
;
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
XT-I mRNA is not expressed but XT-II mRNA
Manually annotated by BRENDA team
-
XT-II mRNA expression is higher than for XT-I. Very low XT-I mRNA expression
Manually annotated by BRENDA team
-
XylT levels in plasma are approximately 200% lower than those in serum due in part to XylT released by platelets during blood clotting in vitro. In Xylt2+/+ mice, total serum XylT activity is 42% higher than in plasma. In Xylt2-/- mice, no significant difference between serum and plasma total XylT activity
Manually annotated by BRENDA team
-
unactivated platelets harbor significant XylT activity that is released upon activation with thrombin
Manually annotated by BRENDA team
-
patients with osteoarthritis
Manually annotated by BRENDA team
-
elevated xylosyltransferase I activities in Pseudoxanthoma elasticum patients
Manually annotated by BRENDA team
-
increased activity of xylosyltransferase I in the blood serum of patients with connective tissue diseases
Manually annotated by BRENDA team
-
XylT2 is predominant
Manually annotated by BRENDA team
-
XylT2 is predominant. XylT levels in serum are approximately 200% higher than those in plasma due in part to XylT released by platelets during blood clotting in vitro. In Xylt2+/+ mice, total serum XylT activity is 42% higher than in plasma. In Xylt2-/- mice, no significant difference between serum and plasma total XylT activity
Manually annotated by BRENDA team
-
XT-I mRNA is not expressed but XT-II mRNA
Manually annotated by BRENDA team
-
low content of isoform XT-II, and very low content of isoform XT-I
Manually annotated by BRENDA team
-
8% activity compared to epiphyseal cartilage
Manually annotated by BRENDA team
-
highest XT-II expression levels, low XT-I mRNA expression
Manually annotated by BRENDA team
-
XT-II mRNA expression is higher than for XT-I
Manually annotated by BRENDA team
-
XT-I mRNA is not expressed but XT-II mRNA
Manually annotated by BRENDA team
-
sternal, from heart
Manually annotated by BRENDA team
-
XT-II mRNA expression is higher than for XT-I. Very low XT-I mRNA expression
Manually annotated by BRENDA team
-
from heart sternal cartilage, cell culture supernatant
Manually annotated by BRENDA team
-
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
Manually annotated by BRENDA team
-
XT-II mRNA expression is higher than for XT-I. Very low XT-I mRNA expression
Manually annotated by BRENDA team
-
XT-II mRNA expression is higher than for XT-I. Very low XT-I mRNA expression
Manually annotated by BRENDA team
-
XT-II mRNA expression is higher than for XT-I. Low XT-I mRNA expression
Manually annotated by BRENDA team
-
highest activity
Manually annotated by BRENDA team
-
cardiac fibroblast
Manually annotated by BRENDA team
-
isoform XT-II, low content
Manually annotated by BRENDA team
-
sternal cartilage
Manually annotated by BRENDA team
Rattus norvegicus Lewis1WR1
-
-
-
Manually annotated by BRENDA team
-
XT-II mRNA expression is higher than for XT-I. Very low XT-I mRNA expression
Manually annotated by BRENDA team
-
low activity
Manually annotated by BRENDA team
-
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
Manually annotated by BRENDA team
-
XT-I mRNA is not expressed but XT-II mRNA
Manually annotated by BRENDA team
-
XT-II mRNA expression is higher than for XT-I. Very low XT-I mRNA expression
Manually annotated by BRENDA team
-
XT-I mRNA is not expressed but XT-II mRNA
Manually annotated by BRENDA team
-
choriocarcinoma cell line
Manually annotated by BRENDA team
-
XT-I mRNA expression is higher than for XT-II
Manually annotated by BRENDA team
-
expresson of xylosyltransferase 2, no expression of xylosyltransferase 1
Manually annotated by BRENDA team
-
XT-I mRNA is not expressed but XT-II mRNA
Manually annotated by BRENDA team
-
XT-II is exclusively expressed in liver tissues, in the HeLa cervical carcinoma cell line, and in K-562 erythroleukemia cells
Manually annotated by BRENDA team
-
isoforms XT-I and XT-II
Manually annotated by BRENDA team
-
XT-I and XT-II are highly expressed in kidney
Manually annotated by BRENDA team
Rattus norvegicus Lewis1WR1
-
-
-
Manually annotated by BRENDA team
-
isoform XT-II
Manually annotated by BRENDA team
-
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
Manually annotated by BRENDA team
-
XT-II is highly expressed in liver, no XT-I mRNA is detectable in liver
Manually annotated by BRENDA team
-
liver is a significant source of circulating XylT2 activity
Manually annotated by BRENDA team
-
XT-I mRNA is not expressed but XT-II mRNA
Manually annotated by BRENDA team
-
isoform XT-II, and low content of isoform XT-I
Manually annotated by BRENDA team
-
XT-II is highly expressed in lung
Manually annotated by BRENDA team
-
XT-II mRNA expression is higher than for XT-I
Manually annotated by BRENDA team
-
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
Manually annotated by BRENDA team
-
mainly produced by granulosa-lutein cells, follicular fluid
Manually annotated by BRENDA team
-
low activity
Manually annotated by BRENDA team
Rattus norvegicus Lewis1WR1
-
low activity
-
Manually annotated by BRENDA team
-
isoforms XT-I and XT-II
Manually annotated by BRENDA team
-
isoform XT-I and XT-II
Manually annotated by BRENDA team
-
XT-II mRNA expression is higher than for XT-I. Very low XT-I mRNA expression
Manually annotated by BRENDA team
-
equal expression levels of XT-I and XT-II
Manually annotated by BRENDA team
-
of healthy and infertile men with oligo-, astheno- or teratozoospermia, and of men after vasectomy
Manually annotated by BRENDA team
-
highest activity
Manually annotated by BRENDA team
-
of healthy and infertile men with oligo-, astheno- or teratozoospermia, and of men after vasectomy
Manually annotated by BRENDA team
-
from heart blood
Manually annotated by BRENDA team
-
isoform XT-II, low content
Manually annotated by BRENDA team
Rattus norvegicus Lewis1WR1
-
-
-
Manually annotated by BRENDA team
-
equal expression levels of XT-I and XT-II
Manually annotated by BRENDA team
-
XT-I is highly expressed in testes
Manually annotated by BRENDA team
-
XT-I mRNA expression is higher than for XT-II
Manually annotated by BRENDA team
Rattus norvegicus Lewis1WR1
-
-
-
Manually annotated by BRENDA team
-
equal expression levels of XT-I and XT-II
Manually annotated by BRENDA team
-
mesenchymal stem cell, 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
Manually annotated by BRENDA team
additional information
-
no activity in EFO-21 cells
Manually annotated by BRENDA team
additional information
-
activity in several human cell lines, culture supernatant, overview
Manually annotated by BRENDA team
additional information
-
enzyme activity in seminal plasma of infertile men is significantly reduced
Manually annotated by BRENDA team
additional information
-
no activity in liver and intestine with an exogenous receptor
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
in cell culture supernatant
-
Manually annotated by BRENDA team
-
human cell cultures
-
Manually annotated by BRENDA team
-
isoform XT-I
-
Manually annotated by BRENDA team
-
secreted into the culture supernatant
-
Manually annotated by BRENDA team
-
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
Manually annotated by BRENDA team
-
isoform XT-II, type II transmembrane protein
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
71000
-
gel filtration
637617
95000 - 100000
-
gel filtration
637611
95800
-
XylT-II, gel filtration
702029
110000 - 120000
-
gel filtration
637610
110000
-
gel filtration
684886
120000
-
gel filtration, amino acid sequence determination
637618, 637619
120000
-
; SDS-PAGE
679132
additional information
-
enzyme activity is also detected in a peak of MW 500000
637618
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
-
x * 91000, isoform XT-I, amino acid sequence determination, x * 97000, isoform XT-II, amino acid sequence determination
?
-
x * 97000, calculated from sequence
monomer
-
1 * 78000, SDS-PAGE
monomer
-
1 * 120000, SDS-PAGE
monomer
-
1 * 90000, SDS-PAGE under reducing conditions
tetramer
-
2 * 23000 + 2 * 27000, 2 pairs of dissimilar subunits, SDS-PAGE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
-
N-glycosylated
glycoprotein
-
3 potential N-glycosylation sites, isoforms XT-I and XT-II
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
-
reaching a temperature of 37C, XT-II has 66% of the activity compared with 30C
684886
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-80C, -20C or 4C, 3-4 weeks, no loss of activity
-
25C, 2 weeks, no loss of activity
-
-20C or -80C, Tris-HCl 50 mM, pH 7.0, NaCl 50 mM, stable for at least 15 weeks
-
storage at 4C, 25C or 37C lead to rapid loss of activity
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
partial
-
by affinity chromatography
-
from cell culture supernatant
-
from cell culture supernatant; partial
-
full-length XylT-II purified to homogeneity as inclusion bodies, by maltose binding protein affinity chromatography and heparin affinity chromatography
-
recombinant enzyme expressed in High Five insect cells
-
wild-type, and recombinant from CHO-K1 cells
-
XylT-II purified by fractionated ammonium sulfate precipitation, heparin affinity and ion exchange chromatography, 7087fold with a final yield of 2.6%
-
affinity chromatography on QEEEGSGGGQGG-resin
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Pichia pastoris
Q965Q8
expression in Pichia pastoris
-
inducible expression in Pichia pastoris
-
5' and 3' deletion constructs expressed in SW1353 cells
-
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 CHO cells, high five insect cells, HEK293 cells, and SaOS-2 cells, and in Pichia pastoris
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expressed in Pichia pastoris strain X-33
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expressed in the xylosyltransferase-deficient pgsA-745 (S745) CHO cell line 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. Soluble form of human XT-II is expressed in the xylosyltransferase-deficient pgsA-745 (S745) Chinese hamster ovary cell line
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expressed in xylosyltransferase-deficient pgsA-745 CHO cells; expression in Pichia pastoris. Transfection of the xylosyltransferase-deficient Chinese hamster ovary mutant pgsA-745 with XT-II coding cDNA completely restores glycosaminoglycan biosynthesis
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expression in Pichia pastoris
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expression of various GFP-tagged XT-II mutants with C-terminal truncations and deletions in HEK-293 and SaOS-2 cells; 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
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high-level expression in High Five insect cells
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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)
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soluble active form of human XT-I is expressed in High Five insect cells, Trichoplusia ni
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soluble mutant enzymes of human XT-I with deletions at the N-terminal domain are expressed in insect cells
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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
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c-Myc/TGFalpha doubly transgenic mice. Modified minigene Xylt2 expression construct producing a protein lacking the 45 N-terminal amino acids including the transmembrane domains. The Xylt1 expression cassette producing a protein that lacks 94 N-terminal amino acids including the transmembrane domain which is predicted as for XylT2. Both Xylt1 and Xylt2 expression cassettes cloned into a modified pcDNA3.1 vector containing a transferrin signal peptide and an HPC4 epitope tag in frame on the N-terminus
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DNA sequence determination and analysis of isoforms XT-I and XT-II, chromosome mapping
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
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
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XT-I gene expression is down-regulated by IL-1beta
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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
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XT-I gene expression is up-regulated by TGF-beta1
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XT-I gene expression is down-regulated by IL-1beta
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XT-I gene expression is up-regulated by TGF-beta1
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C257A
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2.3fold decrease in the ratio of Vmax to KM-value as compared to wild-type enzyme
C276A
-
mutation results in a nearly inactive enzyme
C285A
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5.4fold decrease in the ratio of Vmax to KM-value as compared to wild-type enzyme
C301A
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2.3fold decrease in the ratio of Vmax to KM-value as compared to wild-type enzyme
C471A
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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
C561A
-
UDP inhibition is significantly reduced
C563A
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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
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1.5fold increase in the ratio of Vmax to KM-value as compared to wild-type enzyme
C902A
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1.5fold increase in the ratio of Vmax to KM-value as compared to wild-type enzyme
C927A
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1.4fold decrease in the ratio of Vmax to KM-value as compared to wild-type enzyme
C933A
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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
D745G
-
loss of activity
D747E
-
reduced substrate affinity, about 35% of the wild-type activity, Km-value for bikunin is 4.4fold higher than wild-type value
D747G
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reduced substrate affinity, about 35% of the wild-type activity, Km-value for bikunin is 7.7fold 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
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KM-value for bikunin is 1.6fold higher than wild-type value, Vmax is 1.1fold higher than wild-type value
DELTA1-260
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KM-value for bikunin is 1.6fold higher than wild-type value, Vmax is identical to wild-type value
DELTA1-266
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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
DELTA1-273
-
more than 98% of activity
DELTA261-272
-
inactive mutant enzyme
DELTA721-726
-
inactive mutant enzyme
E263A
-
KM-value for bikunin is 1.4fold higher than wild-type value, Vmax is 2fold higher than wild-type value
K262A
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KM-value for bikunin is 1.2fold 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
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KM-value for bikunin is 1.3fold higher than wild-type value, Vmax is 1.1fold higher than wild-type value
W746D
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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
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about 25% of wild-type activity, Km-value for bikunin is 1.4fold higher than wild-type value
K272A
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KM-value for bikunin is 1.4fold higher than wild-type value, Vmax is 1.7fold higher than wild-type value
additional information
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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
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
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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
diagnostics
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the enzyme is a diagnostic marker of an enhanced proteoglycan biosynthesis
medicine
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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
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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
-
xylosyltransferase I is a fibrosis marker
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, 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
-
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