2.4.1.133: xylosylprotein 4-beta-galactosyltransferase
This is an abbreviated version!
For detailed information about xylosylprotein 4-beta-galactosyltransferase, go to the full flat file.
Word Map on EC 2.4.1.133
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2.4.1.133
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proteoglycans
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glycosaminoglycans
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ehlers-danlos
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beta-1,4-galts
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progeroid
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xylosyltransferase
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larsen
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hypermobility
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b3galt6
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laxity
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hypermobl
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reunion
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linkeropathies
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spondylodysplastic
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hyperextensibility
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drug development
- 2.4.1.133
- proteoglycans
- glycosaminoglycans
- ehlers-danlos
- beta-1,4-galts
-
progeroid
-
xylosyltransferase
-
larsen
- hypermobility
- b3galt6
- laxity
-
hypermobl
-
reunion
-
linkeropathies
-
spondylodysplastic
-
hyperextensibility
- drug development
Reaction
Synonyms
B4GALT7, beta-1,4 galactosyltransferase I, beta-1,4 galactosyltransferase V, beta-1,4-galactosyltransferase, beta-1,4-galactosyltransferase 7, beta-1,4-galactosyltransferase I, beta-1,4-galactosyltransferase-I, beta-1,4-galactosyltransferase-T7, beta-1,4-GalT, beta-1,4-GalT 7, beta-1,4-GalT I, beta-1,4-GalT V, beta-1,4-GalT-I, beta1,4-galactosyltransferase 7, beta1,4-galactosyltransferase I, beta1,4-galactosyltransferase VII, beta1,4-galactosyltransferase-7, beta1,4-GalT, beta1,4-GalT-I, beta1,4-GalT7, beta4-galactosyltransferase 7, beta4Gal-T7, beta4galactosyltransferase I, beta4GalT-7, beta4GalT7, dbeta4GalTI, galactosyltransferase I, galactosyltransferase, uridine diphosphogalactose-xylose, GalT I, GalT-I, hbeta4GalT7, MgGalT7, pNP-xylose-beta-1,4-galactosyltransferase, proteoglycan UDP-galactose:beta-xylose beta 1,4-galactosyltransferase I, SQV-3, UDP-D-galactose:D-xylose galactosyltransferase, UDP-D-galactose:xylose galactosyltransferase, UDP-galactose:O-beta-D-xylosylprotein 4-beta-D-galactosyltransferase, UDPgalactose:O-beta-D-xylosylprotein 4-beta-D-galactosyltransferase, xylosylprotein 4-beta-galactosyltransferase, xylosylprotein beta1,4-galactosyltransferase
ECTree
2.4.1.133 xylosylprotein 4-beta-galactosyltransferaseAdvanced search results
results (
results (Engineering
Engineering on EC 2.4.1.133 - xylosylprotein 4-beta-galactosyltransferase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
D211N
A186D
D165E
the apparent Km values of the D165E mutant toward UDP-galactose and 4-methylumbelliferyl-O-beta-D-xylopyranoside are about 3.8 and 5.5fold, respectively, higher than the wild type enzyme
D211N
D228E
the mutant expressed in HeLa cells retains about 40% activity of the wild type enzyme
D230A
the mutant shows increased Km values towards UDP-galactose and 4-methylumbelliferyl-O-beta-D-xylopyranoside compared to the wild type enzyme
DELTA1-81
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deletion construct is enzymatically active with Km values similar to wild-type towards donor and acceptor substrate, kcat higher compared to full-length wild-type
DELTA1-81/A186D
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kcat values similar to wild-type DELTA1-81 construct, Km values towards donor and acceptor substrates increased compared to wild-type
DELTA1-81/L206P
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in contrast to full-length mutant L206P this deletion mutant is enzymatically active, kcat values similar to wild-type DELTA1-81 construct, Km values towards donor and acceptor substrates increased compared to wild-type
DELTA1-81/R270C
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kcat values similar to wild-type DELTA1-81 construct, Km values towards donor and acceptor substrates increased compared to wild-type
E227D
the mutant displays similar apparent Km values toward both donor and acceptor substrates compared with the wild type enzyme
F221A
the mutant shows increased Km values towards UDP-galactose and 4-methylumbelliferyl-O-beta-D-xylopyranoside compared to the wild type enzyme
F221Y
the mutant shows increased Km values towards UDP-galactose and 4-methylumbelliferyl-O-beta-D-xylopyranoside compared to the wild type enzyme
H195A
H195Q
H195R
L206A
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mutant shows similar enzymatic activity compared to wild-type, Km towards donor substrate similar to wild-type, increased towards acceptor substrate
L206P
R226A
R226K
R270A
R270C
R270K
V164A
the mutant shows increased Km values towards UDP-galactose and 4-methylumbelliferyl-O-beta-D-xylopyranoside compared to the wild type enzyme
W222A
the mutant shows decreased Km value towards UDP-galactose compared to the wild type enzyme
W222F
the mutation has no significant effect on the Km value toward donor or acceptor substrate
W224H
the mutant is able to sustain decorin glycosaminoglycan chain substitution but not glycosaminoglycan synthesis from exogenously added xyloside
Y194A
Y194F
Y196A
Y196F
Y199A
Y199F
Y306G/W307G
double-mutant deprives the galactosyltransferase activity of GalT I, the point mutation abolishes the ability of GalT I to promote cell cycle progression of hepatoma cells
additional information
D211N
site-directed mutagenesis, the catalytic base Asp211 is mutated to Asn residue, inactive mutant, substrate-bound crystal structure analysis
A186D
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mutant shows decreased enzymatic activity compared to wild-type, Km towards donor and acceptor substrate increased compared to wild-type
A186D
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the mutant exhibits 9times reduced activity compared to the wild type enzyme
A186D
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the mutation is associated with the progeroid form of the Ehlers-Danlos syndrome and with the reduction of enzyme activity. The mutation weakly impairs the binding of the donor substrate. Glycosaminoglycan biosynthesis is slightly affected by the mutation
H195A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
H195Q
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
H195R
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
L206P
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loss of activity upon L206P substitution due to altered protein folding is the primary cause for the glycosaminoglycan synthesis defect in patients with the progeroid form of Ehlers-Danlos syndrome carrying the compound
L206P
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the mutation is associated with the progeroid form of the Ehlers-Danlos syndrome and with the reduction of enzyme activity. Glycosaminoglycan biosynthesis is fully inhibited by the mutation
R226A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
R226K
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
R270A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
R270C
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compared to control fibroblasts, galactosyltransferase activity in beta4GalT-7Arg270Cys cells is approximately three times reduced over a temperature range of 25-41°C. The reduced beta4GalT-7 activity results in abnormal extracellular matrix structure due to altered decorin and biglycan glycosylation and defective collagen
R270C
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mutant shows similar enzymatic activity compared to wild-type, Km towards donor substrate weakly increased compared to wild-type and strongly increased towards acceptor substrate
R270C
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the mutation is associated with the progeroid form of the Ehlers-Danlos syndrome and with the reduction of enzyme activity. The mutation strongly impairs the binding of the acceptor substrate. Glycosaminoglycan biosynthesis is decreased by the mutation
R270C
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the substitution strongly reduces enzyme affinity towards xyloside acceptor to about 60% compared to the wild type enzyme, thus affecting glycosaminoglycan chains formation
R270K
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
Y196F
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
Y199F
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
additional information
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decorin is less efficiently substituted with glycosaminoglycan chains upon expression of beta4GalT-7(186D) compared to beta4GalT-7-expressing cells. Cells expressing beta4GalT-7206P do not synthesize the proteoglycan form of decorin
additional information
construction of a soluble enzyme mutant by truncation of the first 60 N-terminal amino acids
additional information
construction of truncated mutant beta4GalT7DELTA81
