Information on EC 5.1.3.23 - UDP-2,3-diacetamido-2,3-dideoxyglucuronic acid 2-epimerase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
5.1.3.23
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RECOMMENDED NAME
GeneOntology No.
UDP-2,3-diacetamido-2,3-dideoxyglucuronic acid 2-epimerase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
UDP-2,3-diacetamido-2,3-dideoxy-alpha-D-glucuronate = UDP-2,3-diacetamido-2,3-dideoxy-alpha-D-mannuronate
show the reaction diagram
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Amino sugar and nucleotide sugar metabolism
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UDP-2,3-diacetamido-2,3-dideoxy-alpha-D-mannuronate biosynthesis
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SYSTEMATIC NAME
IUBMB Comments
2,3-diacetamido-2,3-dideoxy-alpha-D-glucuronate 2-epimerase
This enzyme participates in the biosynthetic pathway for UDP-alpha-D-ManNAc3NAcA (UDP-2,3-diacetamido-2,3-dideoxy-alpha-D-mannuronic acid), an important precursor of the B-band lipopolysaccharide of Pseudomonas aeroginosa serotype O5 and of the band-A trisaccharide of Bordetella pertussis, both important respiratory pathogens [1]. The enzyme is highly specific as UDP-alpha-D-GlcNAc, UDP-alpha-D-GlcNAcA (UDP-2-acetamido-2-deoxy-alpha-D-glucuronic acid) and UDP-alpha-D-GlcNAc3NAc (UDP-2,3-diacetamido-2,3-dideoxy-alpha-D-glucose) cannot act as substrates [1].
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
UDP-2,3-diacetamido-2,3-dideoxy-alpha-D-glucuronate
UDP-2,3-diacetamido-2,3-dideoxy-alpha-D-mannuronate
show the reaction diagram
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-2,3-diacetamido-2,3-dideoxy-alpha-D-glucuronate
UDP-2,3-diacetamido-2,3-dideoxy-alpha-D-mannuronate
show the reaction diagram
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30 - 37
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40300
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x * 40300, His6-WbpI, SDS-PAGE
42600
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x * 42600, His6–WlbD, SDS-PAGE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
crystals of the mutant Gln339Arg wlbD enzyme obtained by sitting-drop vapour diffusion, uncomplexed Gln339Arg and UDP-GlcNAc complex. Space group as P2(1)2(1)2(1), with unit-cell parameters a = 78, b = 91, c = 125 A, alpha = 78 A, b = 91 A, c = 90 A. The asymmetric unit contains two monomers and 53% solvent
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
His6-WbpI stored at -20°C in the presence of 25% glycerol retains activity for at least 4 weeks
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His6-WlbD stored at -20°C in the presence of 25% glycerol retains activity for at least 4 weeks
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
His6-WbpI is overexpressed in Escherichia coli RosettaTM cells
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His6–WlbD is overexpressed in Escherichia coli RosettaTM cells
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overexpression in Escherichia coli
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Show AA Sequence (120 entries)
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