Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
UDP + fragment(1-24) of human basic fibroblast growth factor
UDP + ?
-
-
-
-
?
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-alpha-D-xylose + [protein]-L-serine
UDP + [protein]-3-O-(beta-D-xylosyl)-L-serine
UDP-D-xylose + aggrecan
UDP + ?
-
-
-
-
?
UDP-D-xylose + bamcan
UDP + ?
-
-
-
-
?
UDP-D-xylose + betaglycan-1
UDP + ?
-
-
-
-
?
UDP-D-xylose + bFGF-peptide
UDP + ?
-
-
-
-
?
UDP-D-xylose + biglycan
UDP + D-xylosyl-biglycan
UDP-D-xylose + biglycan
UDP + xylosyl-biglycan
-
-
-
?
UDP-D-xylose + bikunin
UDP + ?
UDP-D-xylose + bikunin
UDP + D-xylosyl-bikunin
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 + CD44
UDP + ?
-
-
-
-
?
UDP-D-xylose + collagen alpha2(IX)
UDP + ?
-
-
-
-
?
UDP-D-xylose + DDDSIEGSGGR
UDP + DDDSIEG(D-xylosyl)SGGR
UDP-D-xylose + DDDSIEGSGSGGR
UDP + DDD-(D-xylosyl)SIEGSGSGGR
-
-
-
?
UDP-D-xylose + DSISGDDLGSGDLGSGDFQR
?
UDP-D-xylose + DSISGDDLGSGDLGSGDFQR
UDP + ?
-
-
-
?
UDP-D-xylose + fibroblast growth factor 2
?
-
-
-
?
UDP-D-xylose + fibroblast growth factor 2 fragment 1-24
?
-
-
-
?
UDP-D-xylose + fibroblast growth factor 2 peptide
?
-
-
-
?
UDP-D-xylose + glypican-1
UDP + ?
-
-
-
-
?
UDP-D-xylose + GVEGSADFLK
UDP + GVEGS(-D-xylose)ADFLK
-
derived from collagen X
-
?
UDP-D-xylose + KKDSGPY
UDP + KKDS(-D-xylose)GPY
-
-
-
?
UDP-D-xylose + KTKGSGFFVF
UDP + KTKGS(-D-xylose)GFFVF
-
-
-
?
UDP-D-xylose + L-APLP2
UDP + ?
-
-
-
-
?
UDP-D-xylose + L-APP
UDP + ?
-
-
-
-
?
UDP-D-xylose + neuroglycan C
UDP + ?
-
-
-
-
?
UDP-D-xylose + NFDEIDRSGFGFN
UDP + NFDEIDRS(-D-xylose)GFGFN
-
-
-
?
UDP-D-xylose + perlecan-1
UDP + ?
-
-
-
-
?
UDP-D-xylose + perlecan-2
UDP + ?
-
-
-
-
?
UDP-D-xylose + perlecan-3
UDP + ?
-
-
-
-
?
UDP-D-xylose + phosphacan
UDP + ?
-
-
-
-
?
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 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-D-xylose + QEEEGSGGGGQR
UDP + QEEEG(D-xylosyl)SGGGGQR
-
-
-
?
UDP-D-xylose + QEEEGSGGGGQR
UDP + QEEEG-(D-xylosyl)-S-GGGGQR
-
-
-
?
UDP-D-xylose + QEEEGSGGGOK
UDP + QEEEGS(-D-xylose)GGGOK
UDP-D-xylose + QEEEGSGGGQK
UDP + ?
-
-
-
-
?
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 + SENEGSGMAQQK
UDP + ?
-
-
-
-
?
UDP-D-xylose + serglycin
UDP + ?
-
-
-
-
?
UDP-D-xylose + SIEGSGGR
UDP + D-xylosyl-SIEGSGGR
-
-
-
?
UDP-D-xylose + silk fibroin
?
-
-
-
?
UDP-D-xylose + silk fibroin
UDP + silk fibroin with xylosylserine
UDP-D-xylose + syndecan
UDP + ?
-
-
-
-
?
UDP-D-xylose + syndecan-1
UDP + ?
-
-
-
-
?
UDP-D-xylose + syndecan-4
UDP + ?
-
-
-
-
?
UDP-D-xylose + TENEGSGLTNIK
UDP + ?
-
-
-
-
?
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 + testican-2
UDP + ?
-
-
-
-
?
UDP-D-xylose + thrombomodulin
UDP + ?
-
-
-
-
?
UDP-D-xylose + VCRSGSGLVGK
UDP + VCRSGSGLVGK
-
derived from apolipoprotein J
D-xylose bound to a serine residue
?
UDP-D-xylose + versican-beta
UDP + ?
-
-
-
-
?
UDP-D-xylose + WAGGDASGE
UDP + WAGGDAS(-D-xylose)GE
-
-
-
?
UDP-D-xylose + [Val36,Val38]delta1[Gly92,Ile94]delta2bikunin
UDP + ?
-
-
-
-
?
additional information
?
-
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 + biglycan
UDP + D-xylosyl-biglycan
-
-
-
-
?
UDP-D-xylose + biglycan
UDP + D-xylosyl-biglycan
-
-
-
?
UDP-D-xylose + bikunin
?
-
-
-
-
?
UDP-D-xylose + bikunin
?
-
-
-
?
UDP-D-xylose + bikunin
UDP + ?
-
-
-
-
?
UDP-D-xylose + bikunin
UDP + ?
-
-
-
?
UDP-D-xylose + bikunin
UDP + D-xylosyl-bikunin
-
-
-
-
?
UDP-D-xylose + bikunin
UDP + D-xylosyl-bikunin
-
-
-
?
UDP-D-xylose + bikunin
UDP + D-xylosyl-bikunin
-
-
-
?
UDP-D-xylose + bikunin
UDP + D-xylosyl-bikunin
-
-
-
?
UDP-D-xylose + bikunin
UDP + D-xylosyl-bikunin
-
-
-
?
UDP-D-xylose + bikunin
UDP + D-xylosyl-bikunin
-
-
-
?
UDP-D-xylose + bikunin
UDP + D-xylosyl-bikunin
-
-
-
?
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
-
-
-
?
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
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
-
-
-
?
UDP-D-xylose + DDDSIEGSGGR
UDP + DDDSIEG(D-xylosyl)SGGR
syndecan peptide substrate
-
-
?
UDP-D-xylose + DSISGDDLGSGDLGSGDFQR
?
-
-
-
?
UDP-D-xylose + DSISGDDLGSGDLGSGDFQR
?
the enzyme modifies the peptide with up to two xylose residues
-
-
?
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
-
-
-
?
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
?
-
-
tripeptide SGG is a poor substrate
-
-
?
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
?
-
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
?
-
-
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
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
UDP-alpha-D-xylose + [protein]-L-serine
UDP + [protein]-3-O-(beta-D-xylosyl)-L-serine
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
-
-
?
additional information
?
-
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
?
-
-
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
?
-
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
?
-
-
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
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Adenoma, Pleomorphic
The relationship between proteoglycan inhibition via xylosyltransferase II silencing and the implantation of salivary pleomorphic adenoma.
Astrocytoma
Circulating microRNAs as Biomarkers for Pediatric Astrocytomas.
Cardiomyopathy, Dilated
Transforming growth factor beta1-regulated xylosyltransferase I activity in human cardiac fibroblasts and its impact for myocardial remodeling.
Cataract
Abnormal Proteoglycan Synthesis Due to Gene Defects Causes Skeletal Diseases with Overlapping Phenotypes.
Cataract
Corneal clouding, cataract, and colobomas with a novel missense mutation in B4GALT7-a review of eye anomalies in the linkeropathy syndromes.
Cataract
Homozygosity for frameshift mutations in XYLT2 result in a spondylo-ocular syndrome with bone fragility, cataracts, and hearing defects.
Cataract
Spondyloocular Syndrome - Novel Mutations in XYLT2 Gene and Expansion of the Phenotypic Spectrum.
Cysts
Polycystic disease caused by deficiency in xylosyltransferase 2, an initiating enzyme of glycosaminoglycan biosynthesis.
Diabetes Complications
Identification of a xylosyltransferase II gene haplotype marker for diabetic nephropathy in type 1 diabetes.
Diabetes Mellitus, Type 1
Identification of a xylosyltransferase II gene haplotype marker for diabetic nephropathy in type 1 diabetes.
Diabetes Mellitus, Type 1
Impact of polymorphisms in the genes encoding xylosyltransferase I and a homologue in type 1 diabetic patients with and without nephropathy.
Diabetes Mellitus, Type 1
Novel sequence variants in the human xylosyltransferase I gene and their role in diabetic nephropathy.
Diabetic Nephropathies
Human xylosyltransferases in health and disease.
Diabetic Nephropathies
Identification of a xylosyltransferase II gene haplotype marker for diabetic nephropathy in type 1 diabetes.
Diabetic Nephropathies
The Xylosyltransferase I Gene Polymorphism c.343G>T (p.A125S) Is a Risk Factor for Diabetic Nephropathy in Type 1 Diabetes.
Essential Hypertension
Xylosyltransferase gene variants and their role in essential hypertension.
Glaucoma
Corneal clouding, cataract, and colobomas with a novel missense mutation in B4GALT7-a review of eye anomalies in the linkeropathy syndromes.
Hearing Loss
Abnormal Proteoglycan Synthesis Due to Gene Defects Causes Skeletal Diseases with Overlapping Phenotypes.
Hearing Loss
Spondyloocular Syndrome - Novel Mutations in XYLT2 Gene and Expansion of the Phenotypic Spectrum.
Hearing Loss, Sensorineural
Homozygosity for frameshift mutations in XYLT2 result in a spondylo-ocular syndrome with bone fragility, cataracts, and hearing defects.
Infections
Hepatitis C virus infection propagates through interactions between Syndecan-1 and CD81 and impacts the hepatocyte glycocalyx.
Infections
Sulfonated azo dyes enhance the genome release of enterovirus A71 VP1-98K variants by preventing the virions from being trapped by sulfated glycosaminoglycans at acidic pH.
Joint Diseases
UDP-D-xylose: proteoglycan core protein beta-D-xylosyltransferase: a new marker of cartilage destruction in chronic joint diseases.
Kidney Diseases
Polycystic disease caused by deficiency in xylosyltransferase 2, an initiating enzyme of glycosaminoglycan biosynthesis.
Lipodystrophy
Adipose tissue loss and lipodystrophy in xylosyltransferase II deficient mice.
Mastocytoma
Glycosylation of serine residues by a uridine diphosphate-xylose: protein xylosyltransferase from mouse mastocytoma.
Mucopolysaccharidosis III
Impairment of glycosaminoglycan synthesis in mucopolysaccharidosis type IIIA cells by using siRNA: a potential therapeutic approach for Sanfilippo disease.
Neoplasms
The relationship between proteoglycan inhibition via xylosyltransferase II silencing and the implantation of salivary pleomorphic adenoma.
Neoplasms
Xylosyltransferase II is a significant contributor of circulating xylosyltransferase levels and platelets constitute an important source of xylosyltransferase in serum.
Osteoarthritis
Human xylosyltransferases in health and disease.
Osteoarthritis
Serum xylosyltransferase 1 level increases during early posttraumatic osteoarthritis in mice with high bone forming potential.
Osteoporosis
Abnormal Proteoglycan Synthesis Due to Gene Defects Causes Skeletal Diseases with Overlapping Phenotypes.
Osteoporosis
Recent Discoveries in Monogenic Disorders of Childhood Bone Fragility.
Osteoporosis
Spondyloocular Syndrome - Novel Mutations in XYLT2 Gene and Expansion of the Phenotypic Spectrum.
protein xylosyltransferase deficiency
Homozygosity for frameshift mutations in XYLT2 result in a spondylo-ocular syndrome with bone fragility, cataracts, and hearing defects.
protein xylosyltransferase deficiency
Xylosyltransferase 2 deficiency and organ homeostasis.
Pseudoxanthoma Elasticum
Human xylosyltransferases in health and disease.
Refractive Errors
Corneal clouding, cataract, and colobomas with a novel missense mutation in B4GALT7-a review of eye anomalies in the linkeropathy syndromes.
Retinal Detachment
Corneal clouding, cataract, and colobomas with a novel missense mutation in B4GALT7-a review of eye anomalies in the linkeropathy syndromes.
Stomach Neoplasms
Glucoside xylosyltransferase 2 as a diagnostic and prognostic marker in gastric cancer via comprehensive analysis.
Strabismus
Corneal clouding, cataract, and colobomas with a novel missense mutation in B4GALT7-a review of eye anomalies in the linkeropathy syndromes.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.0188
Aggrecan
-
isoenzyme XT-I
-
0.0208
betaglycan-1
-
isoenzyme XT-I
-
0.0093 - 0.0137
bFGF-peptide
-
0.0097
biglycan
-
isoenzyme XT-I
-
0.0006 - 0.0656
bikunin
-
0.022
bikunin-derived aminoterminus homologous peptide
-
-
-
0.0019
Bio-QEEEGSGGGQKK-F
-
0.0025 - 0.0061
biotin-NH-QEEEGSGGGQKK(5-fluorescein)-CONH2
0.0052
biotin-NHQEEEGSGGGQKK(5-fluorescein)-CONH2
recombinant enzyme
0.155 - 0.19
cartilage chondroitin sulfate proteoglycan
-
0.0146
CD44
-
isoenzyme XT-I
-
0.0034
collagen alpha2(IX)
-
isoenzyme XT-I
-
0.062
fibroblast growth factor 2
recombinant enzyme
-
0.0191
fibroblast growth factor 2 fragment 1-24
-
-
0.0208 - 0.0223
fragment(1-24) of human basic fibroblast growth factor
-
0.0109 - 0.0171
glypican-1
-
0.0572
human basic fibroblast growth factor
-
native XT-I
-
0.0032 - 0.0236
neuroglycan C
-
0.0133
perlecan-1
-
isoenzyme XT-I
-
0.0102 - 0.0145
perlecan-2
-
0.0094 - 0.0187
perlecan-3
-
0.0166
phosphacan
-
isoenzyme XT-I
-
0.0023 - 0.0111
serglycin
-
0.545 - 0.677
silk fibroin
-
0.0122 - 0.0178
syndecan
-
0.0074 - 0.0198
syndecan-1
-
0.0035 - 0.0141
syndecan-4
-
0.0082 - 0.0103
testican-2
-
0.0029 - 0.0182
Thrombomodulin
-
0.0127 - 0.0146
versican-beta
-
0.0008
[Val36,Val38]delta1[Gly92,Ile94]delta2bikunin
-
-
0.0179
bamcan
-
isoenzyme XT-II
-
0.0222
bamcan
-
isoenzyme XT-I
-
0.0093
bFGF-peptide
-
isoenzyme XT-II
-
0.0137
bFGF-peptide
-
isoenzyme XT-I
-
0.0006
bikunin
-
recombinant mutant bikunin
-
0.0009
bikunin
-
recombinant wild-type bikunin
-
0.0009
bikunin
-
37Ā°C, pH 6.5
-
0.0009
bikunin
pH 6.5, 37Ā°C, wild-type enzyme
-
0.0009
bikunin
pH 6.5, 37Ā°C, mutant enzyme D316G
-
0.0009
bikunin
-
37Ā°C, pH 6.5, mutant enzyme DELTA1-184
-
0.001
bikunin
pH 6.5, 37Ā°C, wild-type enzyme
-
0.001
bikunin
pH 6.5, 37Ā°C, mutant enzyme C933A
-
0.0011
bikunin
pH 6.5, 37Ā°C, mutant enzyme D314G
-
0.0011
bikunin
pH 6.5, 37Ā°C, mutant enzyme D745E
-
0.0011
bikunin
-
37Ā°C, pH 6.5, mutant enzyme K262A
-
0.0011
bikunin
-
37Ā°C, pH 6.5, mutant enzyme R270A
-
0.0012
bikunin
pH 6.5, 37Ā°C, mutant enzyme C920A
-
0.0012
bikunin
pH 6.5, 37Ā°C, mutant enzyme W746D
-
0.0012
bikunin
pH 6.5, 37Ā°C, mutant enzyme W746G
-
0.0012
bikunin
-
37Ā°C, pH 6.5, mutant enzyme S269A
-
0.0013
bikunin
pH 6.5, 37Ā°C, mutant enzyme W746N
-
0.0013
bikunin
-
37Ā°C, pH 6.5, mutant enzyme E263A
-
0.0013
bikunin
-
37Ā°C, pH 6.5, mutant enzyme K272A
-
0.0013
bikunin
-
37Ā°C, pH 6.5, mutant enzyme S266A
-
0.0014
bikunin
pH 6.5, 37Ā°C, mutant enzyme C301A
-
0.0014
bikunin
pH 6.5, 37Ā°C, mutant enzyme C675A
-
0.0014
bikunin
-
37Ā°C, pH 6.5, mutant enzyme DELTA1-213
-
0.0014
bikunin
-
37Ā°C, pH 6.5, mutant enzyme DELTA1-260
-
0.0016
bikunin
pH 6.5, 37Ā°C, mutant enzyme C542A
-
0.002
bikunin
pH 6.5, 37Ā°C, mutant enzyme C927A
-
0.0028
bikunin
pH 6.5, 37Ā°C, mutant enzyme C285A
-
0.0044
bikunin
pH 6.5, 37Ā°C, mutant enzyme D747E
-
0.005
bikunin
-
37Ā°C, pH 6.5, mutant enzyme DELTA1-266
-
0.0053
bikunin
pH 6.5, 37Ā°C, mutant enzyme C257A
-
0.0054
bikunin
-
37Ā°C, 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, 37Ā°C, 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)
-
0.0119
bikunin
pH 6.5, 37Ā°C, 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)
-
0.0025
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
0.155
cartilage chondroitin sulfate proteoglycan
-
trifluoromethanesulfonic acid-degraded substrate
-
0.19
cartilage chondroitin sulfate proteoglycan
-
hydrogen fluoride-degraded substrate
-
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
-
0.0109
glypican-1
-
isoenzyme XT-II
-
0.0171
glypican-1
-
isoenzyme XT-I
-
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
-
0.0102
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
-
0.0023
serglycin
-
isoenzyme XT-II
-
0.0111
serglycin
-
isoenzyme XT-I
-
0.545
silk fibroin
-
-
-
0.677
silk fibroin
recombinant enzyme
-
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
-
0.0082
testican-2
-
isoenzyme XT-II
-
0.0103
testican-2
-
isoenzyme XT-I
-
0.0029
Thrombomodulin
-
isoenzyme XT-II
-
0.0182
Thrombomodulin
-
isoenzyme XT-I
-
0.0127
versican-beta
-
isoenzyme XT-II
-
0.0146
versican-beta
-
isoenzyme XT-I
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
-
XT-I mRNA is not expressed but XT-II mRNA
brenda
-
XT-II mRNA expression is higher than for XT-I. Very low XT-I mRNA expression
brenda
-
-
brenda
-
-
brenda
-
unactivated platelets harbor significant XylT activity that is released upon activation with thrombin
brenda
-
XT-I mRNA is not expressed but XT-II mRNA
brenda
-
highest XT-II expression levels, low XT-I mRNA expression
brenda
-
XT-II mRNA expression is higher than for XT-I
brenda
-
XT-I mRNA is not expressed but XT-II mRNA
brenda
-
-
brenda
-
XT-II mRNA expression is higher than for XT-I. Very low XT-I mRNA expression
brenda
-
-
brenda
-
XT-II mRNA expression is higher than for XT-I. Very low XT-I mRNA expression
brenda
-
XT-II mRNA expression is higher than for XT-I. Very low XT-I mRNA expression
brenda
cardiac fibroblast
brenda
-
cell culture
brenda
fibroblast
brenda
-
XT-II mRNA expression is higher than for XT-I. Very low XT-I mRNA expression
brenda
-
-
brenda
-
XT-I mRNA is not expressed but XT-II mRNA
brenda
-
XT-I mRNA is not expressed but XT-II mRNA
brenda
-
XT-II mRNA expression is higher than for XT-I
brenda
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
brenda
-
isoforms XT-I and XT-II
brenda
-
isoform XT-I and XT-II
brenda
-
XT-II mRNA expression is higher than for XT-I. Very low XT-I mRNA expression
brenda
-
equal expression levels of XT-I and XT-II
brenda
-
of healthy and infertile men with oligo-, astheno- or teratozoospermia, and of men after vasectomy
brenda
-
highest activity
brenda
-
isoform XT-II, low content
brenda
-
equal expression levels of XT-I and XT-II
brenda
XT-I is highly expressed in testes
brenda
-
XT-I mRNA expression is higher than for XT-II
brenda
-
equal expression levels of XT-I and XT-II
brenda
-
patients with osteoarthritis
brenda
elevated xylosyltransferase I activities in Pseudoxanthoma elasticum patients
brenda
increased activity of xylosyltransferase I in the blood serum of patients with connective tissue diseases
brenda
-
XylT2 is predominant
brenda
-
-
brenda
-
low content of isoform XT-II, and very low content of isoform XT-I
brenda
-
-
brenda
-
brenda
-
sternal, from heart
brenda
-
-
brenda
-
from heart sternal cartilage
brenda
-
cell culture supernatant
brenda
-
brenda
-
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
brenda
-
low activity
brenda
-
XT-II mRNA expression is higher than for XT-I. Low XT-I mRNA expression
brenda
-
isoform XT-II, low content
brenda
-
sternal cartilage
brenda
-
low activity
brenda
expresson of xylosyltransferase 2, no expression of xylosyltransferase 1
brenda
XT-II is exclusively expressed in liver tissues, in the HeLa cervical carcinoma cell line, and in K-562 erythroleukemia cells
brenda
-
XT-I mRNA is not expressed but XT-II mRNA
brenda
-
-
brenda
-
XT-II mRNA expression is higher than for XT-I. Very low XT-I mRNA expression
brenda
-
-
brenda
-
brenda
-
choriocarcinoma cell line
brenda
-
XT-I mRNA expression is higher than for XT-II
brenda
expresson of xylosyltransferase 2, no expression of xylosyltransferase 1
brenda
-
XT-I mRNA is not expressed but XT-II mRNA
brenda
-
-
brenda
-
isoforms XT-I and XT-II
brenda
XT-I and XT-II are highly expressed in kidney
brenda
-
-
brenda
-
isoform XT-II
brenda
expresson of xylosyltransferase 2, no expression of xylosyltransferase 1
brenda
XT-II is exclusively expressed in liver tissues, in the HeLa cervical carcinoma cell line, and in K-562 erythroleukemia cells
brenda
XT-II is highly expressed in liver, no XT-I mRNA is detectable in liver
brenda
-
-
brenda
-
isoform XT-II, and low content of isoform XT-I
brenda
XT-II is highly expressed in lung
brenda
mesenchymal stem cell
brenda
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
brenda
-
mainly produced by granulosa-lutein cells
brenda
-
follicular fluid
brenda
-
-
brenda
-
brenda
-
of healthy and infertile men with oligo-, astheno- or teratozoospermia, and of men after vasectomy
brenda
additional information
-
no activity in EFO-21 cells
brenda
additional information
-
activity in several human cell lines, culture supernatant, overview
brenda
additional information
-
enzyme activity in seminal plasma of infertile men is significantly reduced
brenda
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
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
C257A
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
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
C561A
UDP inhibition is significantly reduced
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
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
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
-
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
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
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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
-
brenda
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
brenda
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
brenda
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)
brenda
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)
brenda
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
brenda
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
brenda
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)
brenda
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
brenda
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
brenda
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)
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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)
brenda
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
brenda
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
brenda