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Enzyme Nomenclature
Information on EC 2.4.2.42 - UDP-D-xylose:beta-D-glucoside alpha-1,3-D-xylosyltransferase
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The enzyme appears in viruses and cellular organisms
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EC NUMBER 
COMMENTARY 
2.4.2.42
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RECOMMENDED NAME
GeneOntology No.
UDP-D-xylose:beta-D-glucoside alpha-1,3-D-xylosyltransferase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
UDP-alpha-D-xylose + Glcbeta-Ser53-EGF-like domain of bovine factor IX(45-87) = UDP + Xylalpha(1-3)Glcbeta-Ser53-EGF-like domain of bovine factor IX(45-87)
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SYSTEMATIC NAME
IUBMB Comments
UDP-D-xylose:beta-D-glucoside alpha-1,3-D-xylosyltransferase
The enzyme is involved in the biosynthesis of the Xylalpha(1-3)Xylalpha(1-3)Glcbeta-1-O-Ser on epidermal growth factor-like domains [1].
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
UDP-D-xylose + 2-(pyridin-2-ylamino)ethyl beta-D-glucopyranoside
UDP + 2-(pyridin-2-ylamino)ethyl 3-O-alpha-D-xylopyranosyl-beta-D-glucopyranoside
UDP-D-xylose + Glcbeta-Ser53-EGF-like domain of bovine factor IX(45-87)
UDP + Xylalpha(1-3)Glcbeta-Ser53-EGF-like domain of bovine factor IX(45-87)
UDP-D-xylose + 2-(pyridin-2-ylamino)ethyl beta-D-glucopyranoside
UDP + 2-(pyridin-2-ylamino)ethyl 3-O-alpha-D-xylopyranosyl-beta-D-glucopyranoside
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?
UDP-D-xylose + 2-(pyridin-2-ylamino)ethyl beta-D-glucopyranoside
UDP + 2-(pyridin-2-ylamino)ethyl 3-O-alpha-D-xylopyranosyl-beta-D-glucopyranoside
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?
UDP-D-xylose + Glcbeta-Ser53-EGF-like domain of bovine factor IX(45-87)
UDP + Xylalpha(1-3)Glcbeta-Ser53-EGF-like domain of bovine factor IX(45-87)
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the enzyme is involved in the biosynthesis of the Xylalpha(1-3)Xylalpha(1-3)Glcbeta-1-O-Ser on epidermal growth factor-like domains
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?
UDP-D-xylose + Glcbeta-Ser53-EGF-like domain of bovine factor IX(45-87)
UDP + Xylalpha(1-3)Glcbeta-Ser53-EGF-like domain of bovine factor IX(45-87)
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activity is 12fold lower with reduced and alkylated Glc-EGF. This enzyme recognizes not only the glucose portion but also the tertiary structure of the EGF-like domain even though it transfers xylose to a glucose residue and not to peptide
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?
additional information
?
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the enzyme is appears to be involved in the biosynthesis of the Xylalpha(1-3)Glcbeta-Ser structure of glycoproteins such as human blood coagulation factors VII and IX
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
UDP-D-xylose + Glcbeta-Ser53-EGF-like domain of bovine factor IX(45-87)
UDP + Xylalpha(1-3)Glcbeta-Ser53-EGF-like domain of bovine factor IX(45-87)
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the enzyme is involved in the biosynthesis of the Xylalpha(1-3)Xylalpha(1-3)Glcbeta-1-O-Ser on epidermal growth factor-like domains
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?
additional information
?
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the enzyme is appears to be involved in the biosynthesis of the Xylalpha(1-3)Glcbeta-Ser structure of glycoproteins such as human blood coagulation factors VII and IX
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6 - 8
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pH 6.0: about 30% of maximal activity, pH 8.0: about 70% of maximal activity
6.6 - 7.6
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pH 6.6: about 80% of maximal activity, pH 7.6: about 90% of maximal activity
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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LINKS TO OTHER DATABASES (specific for EC-Number 2.4.2.42)
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