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 hide
2.4.2.26
-
RECOMMENDED NAME
GeneOntology No.
protein xylosyltransferase
REACTION
REACTION DIAGRAM
COMMENTARY hide
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
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
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).
CAS REGISTRY NUMBER
COMMENTARY hide
55576-38-0
-
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
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
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 + acceptor protein substrate proteoglycan core protein
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 xylosylserine
show the reaction diagram
-
initiates the biosynthesis of the glycosaminoglycan linkage region
-
-
?
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 + xylosyl-biglycan
show the reaction diagram
-
-
-
?
UDP-D-xylose + bikunin
?
show the reaction diagram
-
-
-
-
?
UDP-D-xylose + bikunin
UDP + ?
show the reaction diagram
UDP-D-xylose + bikunin
UDP + D-xylosyl-bikunin
show the reaction diagram
UDP-D-xylose + bikunin
UDP + 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-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-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-NHQEEEGSGGGQKK(5-fluorescein)-CONH2
UDP + biotin-NHQEEEG-(D-xylosyl)SGGGQKK(5-fluorescein)-CONH2
show the reaction diagram
UDP-D-xylose + cartilage chondroitin sulfate proteoglycan
UDP + cartilage chondroitin sulfate proteoglycan with xylosylserine
show the reaction diagram
UDP-D-xylose + cartilage proteoglycan
UDP + cartilage proteoglycan with xylosylserine
show the reaction diagram
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
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
-
-
-
-
?
UDP-D-xylose + decorin (PG40) peptide
UDP + ?
show the reaction diagram
-
-
-
-
?
UDP-D-xylose + DSISGDDLGSGDLGSGDFQR
?
show the reaction diagram
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
-
-
-
?
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 + 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
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
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
-
-
-
?
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
UDP-D-xylose + QEEEGSGGGQGG
UDP + ?
show the reaction diagram
-
bikunin-type peptide
-
-
?
UDP-D-xylose + QEEEGSGGGQGG
UDP + QEEEGS(-D-xylose)GGGQGG
show the reaction diagram
-
peptide derived from bikunin
-
?
UDP-D-xylose + QEEEGSGGGQK
UDP + ?
show the reaction diagram
-
-
-
-
?
UDP-D-xylose + QEEEGSGGGQKK
UDP + QEEEG-(D-xylosyl)SGGGQKK
show the reaction diagram
UDP-D-xylose + QEEEGSGGGQKK
UDP + QEEEGS(-D-xylose)GGGQKK
show the reaction diagram
-
peptide derived from bikunin
-
?
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 + ?
show the reaction diagram
-
-
-
-
?
UDP-D-xylose + SDDYSGSGSG
UDP + SDDYS(-D-xylose)GSGSG
show the reaction diagram
-
synthetic peptide
-
-
?
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
-
-
-
?
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
?
show the reaction diagram
-
-
-
-
?
UDP-D-xylose + silk fibroin
UDP + ?
show the reaction diagram
-
-
-
-
?
UDP-D-xylose + silk fibroin
UDP + silk fibroin with xylosylserine
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 + ?
show the reaction diagram
-
-
-
-
?
UDP-D-xylose + TENEGSGLTNIK
UDP + TENEG-(D-xylosyl)SGLTNIK
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 + 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
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
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 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
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
active in the absence of any added cation; active in the absence of any added cation
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
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
dithiothreitol
-
XT-II activity is completely abolished at a concentration of 1 mM dithiothreitol
Glycosaminoglycans
-
associate with the enzyme
-
heparin
N-Phenylmaleimide
-
treatment shows no effect on wild-type XT-I but strongly inactivaets the cysteine mutants C461A and C574A
protamine
-
adding protamine to a final concentration of 10 mg/ml decreases XT-II activity 4fold
UMP
-
25% residual activity at 10 mg/ml
UTP
-
4% residual activity at 10 mg/ml
additional information
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
EDTA
-
84% activation at 25 mM
histone protein
-
activity gains 1.5fold when histone protein is added at a concentration of 0.1 mg/ml
-
protamine
-
adding protamine to a final concentration of 0.1 mg/ml stimulates XT-II activity at least 2fold
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
-
additional information
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0188
Aggrecan
-
isoenzyme XT-I
-
0.0179 - 0.0222
bamcan
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
0.11 - 0.19
cartilage chondroitin sulfate proteoglycan
0.0146
CD44
-
isoenzyme XT-I
-
0.062
CDEASGIGPDDRD
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 - 0.0223
fragment(1-24) of human basic fibroblast growth factor
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 - 0.0171
glypican-1
2.67
GVEGSADFLK
-
-
-
0.00011 - 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 - 0.0134
L-APLP2
0.0131
L-APP
-
XT-I
-
0.0032 - 0.0236
neuroglycan C
0.13
NFDEIDRSGFGFN
-
-
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
-
0.39
PLVSSGEDEPK
-
-
0.022
QEEEGSGGGOK
-
-
-
0.008
QEEEGSGGGQGG
-
-
-
0.022
QEEEGSGGGQK
-
-
0.01172 - 0.093
QEEEGSGGGQKK
0.82
QEEEGTGGGQGG
-
-
-
8.6
QGGGGSGGGQGG
-
-
-
0.26
rat L2 chondroitin sulfate
-
-
-
1.39
SAAYSGSGSG
-
-
0.79
SDDYSGSGSG
-
-
-
0.019
SENEGSGMAEQK
20 - 55
Ser-Gly-Gly
0.0023 - 0.0111
serglycin
0.545 - 0.677
silk fibroin
0.064 - 0.18
Smith-degraded chondroitin sulfate proteoglycan
0.155
Smith-degraded chondroitin sulphate proteoglycan
-
-
-
0.0122 - 0.0178
syndecan
0.0074 - 0.0198
syndecan-1
0.0035 - 0.0141
syndecan-4
0.02 - 0.3905
TENEGSGLTNIK
0.0082 - 0.0103
testican-2
0.0029 - 0.0182
Thrombomodulin
0.0065 - 0.25
UDP-D-xylose
0.94
VCRSGSGLVGK
-
-
-
0.0127 - 0.0146
versican-beta
0.42
WAGGDASGE
-
-
-
0.0008
[Val36,Val38]delta1[Gly92,Ile94]delta2bikunin
-
-
additional information
additional information
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0363
biotin-NH-QEEEGSGGGQKK(5-fluorescein)-CONH2
Homo sapiens
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XylT-I or XylT-II
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
5.95 - 14.52
biotin-NH-QEEEGSGGGQKK(5-fluorescein)-CONH2
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00007 - 0.00015
heparin
0.0019 - 0.0246
UDP
additional information
additional information
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competitive inhibition of the acceptor substrates
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.0000003
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XylT-II, concentrated culture supernatant
0.002333
-
7087fold purified XylT-II
0.0285
-
purified enzyme
0.419
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purified enzyme
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5 - 7
-
-
7.5 - 8
-
;
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.7 - 7.5
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half-maximal activity at pH 5.7 and pH 7.5
6.5 - 8.5
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pH 6.5: about 70% of maximal activity, pH 8.5: about 60% of maximal activity
6.5 - 9
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pH 6.5: about 60% of maximal activity, pH 9.0: about 60% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
34
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assay at
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4 - 45
-
-
15 - 37
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15C: about 40% of maximal activity, 37C: maximal activity
16 - 37
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;
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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XT-I mRNA is not expressed but XT-II mRNA
Manually annotated by BRENDA team
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XT-II mRNA expression is higher than for XT-I. Very low XT-I mRNA expression
Manually annotated by BRENDA team
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unactivated platelets harbor significant XylT activity that is released upon activation with thrombin
Manually annotated by BRENDA team
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XT-I mRNA is not expressed but XT-II mRNA
Manually annotated by BRENDA team
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highest XT-II expression levels, low XT-I mRNA expression
Manually annotated by BRENDA team
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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
-
XT-II mRNA expression is higher than for XT-I. Very low XT-I mRNA expression
Manually annotated by BRENDA team
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XT-II mRNA expression is higher than for XT-I. Very low XT-I mRNA expression
Manually annotated by BRENDA team
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XT-II mRNA expression is higher than for XT-I. Very low XT-I mRNA expression
Manually annotated by BRENDA team
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cardiac fibroblast; cardiac fibroblast
Manually annotated by BRENDA team
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cell culture
Manually annotated by BRENDA team
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fibroblast; fibroblast
Manually annotated by BRENDA team
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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
-
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
Manually annotated by BRENDA team
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mesenchymal stem cell. Xylosyltransferase 1 is the predominant xylosyltransferase in the early phase of chondrogenic stem cell differentiation and xylosyltransferase 2 is upregulated 7 days after induction; mesenchymal stem cell. Xylosyltransferase 1 is the predominant xylosyltransferase in the early phase of chondrogenic stem cell differentiation and xylosyltransferase 2 is upregulated 7 days after induction
Manually annotated by BRENDA team
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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
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follicular fluid; mainly produced by granulosa-lutein cells
Manually annotated by BRENDA team
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isoforms XT-I and XT-II
Manually annotated by BRENDA team
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isoform XT-I and XT-II
Manually annotated by BRENDA team
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XT-II mRNA expression is higher than for XT-I. Very low XT-I mRNA expression
Manually annotated by BRENDA team
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equal expression levels of XT-I and XT-II
Manually annotated by BRENDA team
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of healthy and infertile men with oligo-, astheno- or teratozoospermia, and of men after vasectomy
Manually annotated by BRENDA team
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highest activity
Manually annotated by BRENDA team
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isoform XT-II, low content
Manually annotated by BRENDA team
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equal expression levels of XT-I and XT-II
Manually annotated by BRENDA team
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XT-I mRNA expression is higher than for XT-II
Manually annotated by BRENDA team
-
equal expression levels of XT-I and XT-II
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
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isoform XT-II, type II transmembrane protein
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
71000
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gel filtration
95000 - 100000
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gel filtration
95800
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XylT-II, gel filtration
110000 - 120000
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gel filtration
110000
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gel filtration
120000
additional information
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enzyme activity is also detected in a peak of MW 500000
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
tetramer
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2 * 23000 + 2 * 27000, 2 pairs of dissimilar subunits, SDS-PAGE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
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reaching a temperature of 37C, XT-II has 66% of the activity compared with 30C
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C or -80C, Tris-HCl 50 mM, pH 7.0, NaCl 50 mM, stable for at least 15 weeks
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-80C, -20C or 4C, 3-4 weeks, no loss of activity
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25C, 2 weeks, no loss of activity
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storage at 4C, 25C or 37C lead to rapid loss of activity
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
affinity chromatography on QEEEGSGGGQGG-resin
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by affinity chromatography
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from cell culture supernatant
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from cell culture supernatant; partial
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full-length XylT-II purified to homogeneity as inclusion bodies, by maltose binding protein affinity chromatography and heparin affinity chromatography
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partial
recombinant enzyme expressed in High Five insect cells
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wild-type, and recombinant from CHO-K1 cells
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XylT-II purified by fractionated ammonium sulfate precipitation, heparin affinity and ion exchange chromatography, 7087fold with a final yield of 2.6%
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
5' and 3' deletion constructs expressed in SW1353 cells
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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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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
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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
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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
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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inducible expression in Pichia pastoris
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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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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
members of the activator protein 1 and specificity protein 1 family of transcription factors are necessary for the transcriptional regulation of the XYLT1 gene. Transcription factors of the specificity protein 1 family, especially specificity protein 3, are very likely involved in the regulation of the XT-I mRNA expression. A 531-bp core promoter element is able to drive the transcription on a basal level. A binding site for transcription factors of the activator protein 1 family, which is essential for full promoter activity is located 730 bp 5' of the translation initiation site. A promoter element containing this binding site is able to drive the transcription to about 79fold above control in SW1353 chondrosarcoma cells
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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
XT-I gene expression is up-regulated by TGF-beta1
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C257A
-
2.3fold decrease in the ratio of Vmax to KM-value as compared to wild-type enzyme
C276A
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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
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2.9fold decrease in the ratio of Vmax to KM-value as compared to wild-type enzyme
C561A
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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
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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
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
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80% of the activity of wild-type enzyme,Km-value for bikunin is 1.2fold higher than wild-type value
D316G
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as active as wild-type enzyme, Km-value for bikunin is identical to wild-type value
D745E
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mutant retains full activity, Km-value for bikunin is 1.2fold higher than wild-type value
D745G
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loss of activity
D747E
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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
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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
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KM-value for bikunin is 6fold higher than wild-type value, Vmax is 1.3fold lower than wild-type value
DELTA1-273
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more than 98% of activity
DELTA261-272
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inactive mutant enzyme
DELTA721-726
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inactive mutant enzyme
E263A
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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
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
R270A
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KM-value for bikunin is 1.2fold higher than wild-type value, Vmax is 1.4fold higher than wild-type value
S266A
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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
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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
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 hide
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