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Literature summary for 2.5.1.101 extracted from

  • Glaze, P.A.; Watson, D.C.; Young, N.M.; Tanner, M.E.
    Biosynthesis of CMP-N,N-diacetyllegionaminic acid from UDP-N,N-diacetylbacillosamine in Legionella pneumophila (2008), Biochemistry, 47, 3272-3282.
    View publication on PubMed
Search for more literature for 2.5.1.101

Cloned(Commentary)

Cloned (Comment) Organism
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 Legionella pneumophila

Metals/Ions

Metals/Ions Comment Organism Structure
additional information the synthase activity is dependent on the presence of a divalent metal ion Legionella pneumophila

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2,4-diacetamido-2,4,6-trideoxy-alpha-D-mannopyranose + phosphoenolpyruvate + H2O Legionella pneumophila
-
 N,N'-diacetyllegionaminate + phosphate
-
 ?
2,4-diacetamido-2,4,6-trideoxy-alpha-D-mannopyranose + phosphoenolpyruvate + H2O Legionella pneumophila ATCC 33152D
-
 N,N'-diacetyllegionaminate + phosphate
-
 ?
additional information Legionella pneumophila the enzyme condenses 2,4-diacetamido-2,4,6-trideoxymannose with phosphoenolpyruvate, the reaction proceeded via a C-O bond cleavage process ?
-
 ?
additional information Legionella pneumophila ATCC 33152D the enzyme condenses 2,4-diacetamido-2,4,6-trideoxymannose with phosphoenolpyruvate, the reaction proceeded via a C-O bond cleavage process ?
-
 ?

Organism

Organism UniProt Comment Textmining
Legionella pneumophila
-
 subsp. pneumophila, gene lpg0752 or neuB homologue, clustered with the neuC and neuA homologues
-
Legionella pneumophila ATCC 33152D
-
 subsp. pneumophila, gene lpg0752 or neuB homologue, clustered with the neuC and neuA homologues
-

Purification (Commentary)

Purification (Comment) Organism
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 Legionella pneumophila

Reaction

Reaction Comment Organism Reaction ID
2,4-diacetamido-2,4,6-trideoxy-alpha-D-mannopyranose + phosphoenolpyruvate + H2O = N,N'-diacetyllegionaminate + phosphate C-O bond cleavage process reaction via a oxocarbenium ion intermediate generated by an initial attack of C-3 of phosphoenolpyruvate on the aldehyde of 2,4-diacetamido-2,4,6-trideoxymannose. This attack is facilitated by the divalent cation that serves as an electrophilic catalyst and polarizes the carbonyl of the aldehyde. Water then adds to the oxocarbenium ion intermediate to give a tetrahedral intermediate that subsequently collapses to generate phosphate and the product 2-oxo acid, overview Legionella pneumophila
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2,4-diacetamido-2,4,6-trideoxy-alpha-D-mannopyranose + phosphoenolpyruvate + H2O
-
 Legionella pneumophila N,N'-diacetyllegionaminate + phosphate
-
 ?
2,4-diacetamido-2,4,6-trideoxy-alpha-D-mannopyranose + phosphoenolpyruvate + H2O
-
 Legionella pneumophila N,N'-diacetyllegionaminate + phosphate NMR spectroscopic product identification ?
2,4-diacetamido-2,4,6-trideoxy-alpha-D-mannopyranose + phosphoenolpyruvate + H2O
-
 Legionella pneumophila ATCC 33152D N,N'-diacetyllegionaminate + phosphate
-
 ?
2,4-diacetamido-2,4,6-trideoxy-alpha-D-mannopyranose + phosphoenolpyruvate + H2O
-
 Legionella pneumophila ATCC 33152D N,N'-diacetyllegionaminate + phosphate NMR spectroscopic product identification ?
additional information the enzyme condenses 2,4-diacetamido-2,4,6-trideoxymannose with phosphoenolpyruvate, the reaction proceeded via a C-O bond cleavage process Legionella pneumophila ?
-
 ?
additional information the enzyme does not show measurable activity with ManNAc Legionella pneumophila ?
-
 ?
additional information the enzyme condenses 2,4-diacetamido-2,4,6-trideoxymannose with phosphoenolpyruvate, the reaction proceeded via a C-O bond cleavage process Legionella pneumophila ATCC 33152D ?
-
 ?
additional information the enzyme does not show measurable activity with ManNAc Legionella pneumophila ATCC 33152D ?
-
 ?

Synonyms

Synonyms Comment Organism
N,N'-diacetyllegionaminic acid synthase
-
 Legionella pneumophila
NeuB
-
 Legionella pneumophila
NeuB homologue
-
 Legionella pneumophila

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
 assay at Legionella pneumophila

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.4
-
 assay at Legionella pneumophila

General Information

General Information Comment Organism
evolution the gene encoding the enzyme shows homology to known sialic acid biosynthetic gene neuB Legionella pneumophila
metabolism the three enzymes, UDP-N,N'-diacetylbacillosamine 2-epimerase, N,N'-diacetyllegionaminic acid synthase, and CMP-N,N'-diacetyllegionaminic acid synthetase, constitute a pathway that converts a UDP-linked bacillosamine derivative into a CMP-linked legionaminic acid derivative, the activated form of legionaminic acid used in lipopolysaccharide biosynthesis, overview Legionella pneumophila