|Gene:||glmU||Accession Number: G-12615 (MetaCyc)|
The subunit structure of this enzyme has not been reported.
In the food-borne pathogen Campylobacter jejuni this enzyme was proposed to participate 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). Although GlmU was proposed to catalyze the acetylation of GDP-D-glucosamine, the reaction did not go to completion as compared with its known substrate D-glucosamine 1-phosphate, using capillary electrophoresis/mass spectrometry based assays. Other putative N-acetyltransferases from the Campylobacter jejuni jejuni NCTC 11168 = ATCC 700819 flagellar glycosylation locus that can efficiently catalyze this reaction are also being screened. In Escherichia coli GlmU is a bifunctional enzyme responsible for both the acetylation of D-glucosamine 1-phosphate and uridylation of N-acetyl-α-D-glucosamine 1-phosphate (see fused N-acetylglucosamine-1-phosphate uridyltransferase and glucosamine-1-phosphate acetyltransferase) [Schoenhofen09].
Recombinant, N-terminal His6-tagged polypeptide was purified and characterized [Schoenhofen09].
|Map Position: [768,906 -> 770,195]|
Molecular Weight of Polypeptide: 47.906 kD (from nucleotide sequence)
Relationship Links: InterPro:IN-FAMILY:IPR001451 , InterPro:IN-FAMILY:IPR005882 , InterPro:IN-FAMILY:IPR011004 , InterPro:IN-FAMILY:IPR025877 , Panther:IN-FAMILY:PTHR22572:SF17 , Pfam:IN-FAMILY:PF00132 , Pfam:IN-FAMILY:PF12804 , Prosite:IN-FAMILY:PS00101
Enzymatic reaction of: GDP-glucosamine N-acetyltransferase
EC Number: 2.3.1.-
The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the direction in which it was curated.
The reaction is favored in the direction shown.
In Pathways: CMP-legionaminate biosynthesis I
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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