Information on EC 3.2.1.184 - UDP-N,N'-diacetylbacillosamine 2-epimerase (hydrolysing)

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The expected taxonomic range for this enzyme is: Proteobacteria

EC NUMBER
COMMENTARY
3.2.1.184
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RECOMMENDED NAME
GeneOntology No.
UDP-N,N'-diacetylbacillosamine 2-epimerase (hydrolysing)
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
UDP-N,N'-diacetylbacillosamine + H2O = UDP + 2,4-diacetamido-2,4,6-trideoxy-D-mannopyranose
show the reaction diagram
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UDP-N,N'-diacetylbacillosamine + H2O = UDP + 2,4-diacetamido-2,4,6-trideoxy-D-mannopyranose
show the reaction diagram
the reaction proceeds with an inversion of stereochemistry at C-2 and retention of stereochemistry at C-1. Evidence of the cleavage of the C-1-O bond and the C-2-H bond supports an elimination/hydration mechanism similar to that of NeuC in sialic acid bisoynthesis
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UDP-N,N'-diacetylbacillosamine + H2O = UDP + 2,4-diacetamido-2,4,6-trideoxy-D-mannopyranose
show the reaction diagram
the reaction proceeds with an inversion of stereochemistry at C-2 and retention of stereochemistry at C-1. Evidence of the cleavage of the C-1-O bond and the C-2-H bond supports an elimination/hydration mechanism similar to that of NeuC in sialic acid bisoynthesis
Legionella pneumophila ATCC 33152D, Legionella pneumophila ATCC33152D
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PATHWAY
KEGG Link
MetaCyc Link
CMP-legionaminate biosynthesis II
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SYSTEMATIC NAME
IUBMB Comments
UDP-N,N'-diacetylbacillosamine hydrolase (2-epimerising)
Requires Mg2+. Involved in biosynthesis of legionaminic acid, a nonulosonate derivative that is incorporated by some bacteria into assorted virulence-associated cell surface glycoconjugates. The initial product formed by the enzyme from Legionella pneumophila, which incorporates legionaminic acid into the O-antigen moiety of its lipopolysaccharide, is 2,4-diacetamido-2,4,6-trideoxy-alpha-D-mannopyranose, which rapidly mutarotates to a mixture of anomers [1]. The enzyme from Campylobacter jejuni, which incorporates legionaminic acid into flagellin, prefers GDP-N,N'-diacetylbacillosamine [2].
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Cj1328
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gene name
neuC
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neuC
Campylobacter jejuni 11168
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neuC
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gene name
UDP-Bac2Ac4Ac 2-epimerase
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UDP-N-acetylglucosamine 2-epimerase
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UDP-N-acetylglucosamine 2-epimerase
Campylobacter jejuni 11168
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UDP-N-acetylglucosamine 2-epimerase
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ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
UDP-N,N'-diacetylbacillosamine + H2O
2,4-diacetamido-2,4,6-trideoxymannose + UDP
show the reaction diagram
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?
GDP-2,4-diacetamido-2,4,6-trideoxy-alpha-D-glucose + H2O
?
show the reaction diagram
Campylobacter jejuni, Campylobacter jejuni 11168
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enzyme performs C2-epimerization resulting in NDP removal. Enzyme does not react with UDP-2,4-diacetamido-2,4,6-trideoxy-alpha-D-glucose, but when the quantity of LegG is 10fold increased within this reaction, UDP removal is observed
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?
additional information
?
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when UDP-GlcNAc is incubated with the enzyme, no product formation is observed
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KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.0365
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UDP-N,N'-diacetylbacillosamine
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pH 7.5, 37°C
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
59.1
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UDP-N,N'-diacetylbacillosamine
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pH 7.5, 37°C
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
7.5
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assay at
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
37
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assay at
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
using Ni-NTA chromatography
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using Ni-NTA chromatography
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Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
expressed as a His-tagged fusion protein
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overexpressed in Escherichia coli as a His-tagged fusion protein
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