Information on EC 2.4.1.B7 - ursodeoxycholate N-acetylglucosaminyltransferase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
2.4.1.B7
preliminary BRENDA-supplied EC number
RECOMMENDED NAME
GeneOntology No.
ursodeoxycholate N-acetylglucosaminyltransferase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
UDP-N-acetyl-D-glucosamine + ursodeoxycholate = UDP + 7beta-(N-acetyl-D-glucosaminyl)-ursodeoxycholate
show the reaction diagram
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SYSTEMATIC NAME
IUBMB Comments
UDP-N-acetyl-D-glucosamine:ursodeoxycholate 7beta-N-acetylglucosaminyltransferase
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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-D-glucose + ursodeoxycholate
UDP + 7beta-D-glucosyl-ursodeoxycholate
show the reaction diagram
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?
UDP-N-acetyl-D-glucosamine + ursodeoxycholate
UDP + 7beta-(N-acetyl-D-glucosaminyl)-ursodeoxycholate
show the reaction diagram
additional information
?
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also transfers N-acetyl-D-glucosamine to 17alpha-estradiol, 17beta-estradiol, 4-nitrophenol and 1-naphthol
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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-N-acetyl-D-glucosamine + ursodeoxycholate
UDP + 7beta-(N-acetyl-D-glucosaminyl)-ursodeoxycholate
show the reaction diagram
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i.e. 3',7'-dihydroxy-5'-cholanoic acid. Important role in the metabolism and elimination of ursodeoxycholic acid
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?
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00175 - 0.015
UDP-D-glucose
0.065
UDP-N-acetyl-D-glucosamine
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wild-type, pH 7.5, 37°C
0.049
ursodeoxycholate
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pH 7.5, 37°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5
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assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
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assay at
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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poor activity
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
53000
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x * 53000, SDS-PAGE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
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x * 53000, SDS-PAGE
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
analysis of homology models docked with UDP-sugar donors indicates that residue N391 in UGT3A1 is able to accommodate the N-acetyl group on C2 of UDP-GlcNAc so that the anomeric carbon atom C1 is optimally situated for catalysis involving residue His35. Replacement of Asn with Phe at position 391 disrupts this catalytically productive orientation of UDP-GlcNAc but allows a more optimal alignment of UDP-Glc for sugar donation
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in HEK293T cells
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C121G
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a polymorphic UGT3A1 variant containing a C121G substitution is catalytically inactive
N391F
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residue N391 is necessary for utilization of UDP-GlcNAc as substrate. Mutation N391F in UGT3A1 enhances its ability to utilize UDP-Glc and completely inhibits its ability to use UDP-GlcNAc. An analysis of homology models docked with UDP-sugar donors indicates that N391 in UGT3A1 is able to accommodate the N-acetyl group on C2 of UDP-GlcNAc so that the anomeric carbon atom C1 is optimally situated for catalysis involving residue His35. Replacement of Asn with Phe at position 391 disrupts this catalytically productive orientation of UDP-GlcNAc but allows a more optimal alignment of UDP-Glc for sugar donation
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
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important role in therapies for ameliorating the symptoms of cholestasis or for dissolving gallstones