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Information on EC 3.2.1.183 - UDP-N-acetylglucosamine 2-epimerase (hydrolysing) and Organism(s) Escherichia coli and UniProt Accession P27828

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IUBMB Comments
The enzyme is found in mammalian liver, as well as in some pathogenic bacteria including Neisseria meningitidis and Staphylococcus aureus. It catalyses the first step of sialic acid (N-acetylneuraminic acid) biosynthesis. The initial product formed is the alpha anomer, which rapidly mutarotates to a mixture of anomers . The mammalian enzyme is bifunctional and also catalyses EC 2.7.1.60, N-acetylmannosamine kinase. cf. EC 5.1.3.14, UDP-N-acetylglucosamine 2-epimerase (non-hydrolysing).
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Escherichia coli
UNIPROT: P27828
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Word Map
The taxonomic range for the selected organisms is: Escherichia coli
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Synonyms
bifunctional udp-n-acetylglucosamine 2-epimerase/n-acetylmannosamine kinase, bifunctional udp-glcnac 2-epimerase/mannac kinase, uridine diphosphate-n-acetylglucosamine-2-epimerase, uridine diphosphate-n-acetylglucosamine 2-epimerase/n-acetylmannosamine kinase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
GNE
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siaA
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UDP-N-acetylglucosamine 2-epimerase
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SYSTEMATIC NAME
IUBMB Comments
UDP-N-acetyl-alpha-D-glucosamine hydrolase (2-epimerising)
The enzyme is found in mammalian liver, as well as in some pathogenic bacteria including Neisseria meningitidis and Staphylococcus aureus. It catalyses the first step of sialic acid (N-acetylneuraminic acid) biosynthesis. The initial product formed is the alpha anomer, which rapidly mutarotates to a mixture of anomers [2]. The mammalian enzyme is bifunctional and also catalyses EC 2.7.1.60, N-acetylmannosamine kinase. cf. EC 5.1.3.14, UDP-N-acetylglucosamine 2-epimerase (non-hydrolysing).
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
UDP-N-acetyl-alpha-D-glucosamine + H2O
N-acetyl-alpha-D-mannosamine + UDP
show the reaction diagram
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-
?
UDP-N-alpha-D-acetylglucosamine + H2O
N-acetyl-alpha-D-mannosamine + UDP
show the reaction diagram
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enzyme catalyzes the formation of ManNAc from UDP-GlcNAc via a 2-acetamidoglucal intermediate
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?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5
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assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
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neuC is deleted from the chromosome of EV36, a K-12-K1 hybrid, by allelic exchange. Exogenously added sialic acid restores capsule expression to the deletion strain, confirming that NeuC is necessary for sialic acid synthesis. The NeuC homologue from serotype III Streptococcus agalactiae complements deletion mutant
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
45000
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SDS-PAGE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
neuC gene is cloned into an intein expression vector
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed as a His-tagged fusion protein
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Vann, W.F.; Daines, D.A.; Murkin, A.S.; Tanner, M.E.; Chaffin, D.O.; Rubens, C.E.; Vionnet, J.; Silver, R.P.
The NeuC protein of Escherichia coli K1 is a UDP N-acetylglucosamine 2-epimerase
J. Bacteriol.
186
706-712
2004
Escherichia coli
Manually annotated by BRENDA team
Ringenberg, M.A.; Steenbergen, S.M.; Vimr, E.R.
The first committed step in the biosynthesis of sialic acid by Escherichia coli K1 does not involve a phosphorylated N-acetylmannosamine intermediate
Mol. Microbiol.
50
961-975
2003
Escherichia coli
Manually annotated by BRENDA team