|Gene:||legF||Accession Number: G-12623 (MetaCyc)|
Synonyms: Cj1331, NeuA3, PtmB
The subunit structure of this enzyme has not been reported.
Recombinant, C-terminal His6-tagged polypeptide was purified and characterized [Schoenhofen09].
In the food-borne pathogen Campylobacter jejuni this enzyme participates in the biosynthesis of CMP-N,N'-diacetyllegionaminate (CMP-legionaminic acid), a virulence-associated, cell surface sialic acid-like derivative (see pathway CMP-legionaminate biosynthesis I). Leg F catalyzes the synthesis of CMP-N,N'-diacetyllegionaminate (CMP-activated legionaminic acid) and is a homolog of Escherichia coli NeuA (see cytidine 5'-monophosphate N-acetylneuraminate synthetase) [Schoenhofen09].
|Map Position: [1,258,212 -> 1,258,919]|
Molecular Weight of Polypeptide: 26.661 kD (from nucleotide sequence)
Enzymatic reaction of: CMP-legionaminate synthase (CMP-legionaminic acid synthase)
EC Number: 18.104.22.168
The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.
The reaction is favored in the direction shown.
In Pathways: CMP-legionaminate biosynthesis I
This enzyme could efficiently catalyze production of CMP-N,N'-diacetyllegionaminate (CMP-legionaminic acid). Metabolites were purified and identified by capillary electrophoresis/mass spectrometry analysis and NMR spectroscopy [Schoenhofen09].
Schoenhofen09: Schoenhofen IC, Vinogradov E, Whitfield DM, Brisson JR, Logan SM (2009). "The CMP-legionaminic acid pathway in Campylobacter: biosynthesis involving novel GDP-linked precursors." Glycobiology 19(7);715-25. PMID: 19282391
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