Information on EC 2.5.1.101 - N,N'-diacetyllegionaminate synthase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
2.5.1.101
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RECOMMENDED NAME
GeneOntology No.
N,N'-diacetyllegionaminate synthase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
2,4-diacetamido-2,4,6-trideoxy-alpha-D-mannopyranose + phosphoenolpyruvate + H2O = N,N'-diacetyllegionaminate + phosphate
show the reaction diagram
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
CMP-legionaminate biosynthesis I
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CMP-legionaminate biosynthesis II
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Amino sugar and nucleotide sugar metabolism
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SYSTEMATIC NAME
IUBMB Comments
phosphoenolpyruvate:2,4-diacetamido-2,4,6-trideoxy-alpha-D-mannopyranose 1-(2-carboxy-2-oxoethyl)transferase
Requires a divalent metal such as Mn2+. Isolated from the bacteria Legionella pneumophila and Campylobacter jejuni, where it is involved in the biosynthesis of legionaminic acid, a virulence-associated, cell surface sialic acid-like derivative.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
gene legI or Cj1327
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Manually annotated by BRENDA team
gene legI or Cj1327
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Manually annotated by BRENDA team
subsp. pneumophila, gene lpg0752 or neuB homologue, clustered with the neuC and neuA homologues
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
metabolism
additional information
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NeuB can be substituted by NanA from Escherichia coli, a sialic acid aldolase that catalyzes the condensation of 2,4-diacetamido-2,4,6-trideoxy-alpha-D-mannopyranose with pyruvate resulting in N,N'-diacetyllegionaminate formation, ability of sialyltransferases to utilize the CMP-N,N'-diacetyllegionaminate donor, overview
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2,4-diacetamido-2,4,6-trideoxy-alpha-D-mannopyranose + phosphoenolpyruvate + H2O
N,N'-diacetyllegionaminate + phosphate
show the reaction diagram
additional information
?
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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
2,4-diacetamido-2,4,6-trideoxy-alpha-D-mannopyranose + phosphoenolpyruvate + H2O
N,N'-diacetyllegionaminate + phosphate
show the reaction diagram
additional information
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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the synthase activity is dependent on the presence of a divalent metal ion
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.3
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assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant C- and N-terminally and inactive His-tagged enzyme from Escherichia coli strain BL21(DE3) by metal chelating chromatography, recombinant active MalE-NeuB fusion protein by amylose affinity chromatography to high yields, the MalE protein is removed by thrombin treatment
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recombinant N-terminally His6-tagged enzyme by nickel affinity chromatography
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
gene legI or Cj1327, DNA and ammino acid sequence determination and analysis, expression as N-terminally His6-tagged enzyme
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gene lpg 0752, cloning and expression of NeuB results in insoluble protein which possesses very low levels of N,N'-diacetyllegionaminate synthase activity
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gene lpg0752 or neuB, DNA and amino acid sequence determination and analysis, overexpression of the inactive C- and N-terminally His-tagged enzyme in Escherichia coli strain BL21(DE3), functional expression as MalE-NeuB fusion protein
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