ArticleGlycoconjugate journal1999
UDP-N-Acetyl-alpha-D-glucosamine as acceptor substrate of beta-1,4-galactosyltransferase. Enzymatic synthesis of UDP-N-acetyllactosamine.
Article in Glycoconjugate journal, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 32 citations in OpenAlex.
- An untargeted metabolomics analysis in feces and brain of Orthoflaviviruses-infected mice.BMC microbiology · 2025Article
- Detection and Analysis of Proteins Modified by O-Linked N-Acetylglucosamine.Current protocols · 2021Article
- Structural reevaluation of Streptococcus pneumoniae Lipoteichoic acid and new insights into its immunostimulatory potency.The Journal of biological chemistry · 2013Article
- Detection and analysis of proteins modified by O-linked N-acetylglucosamine.Current protocols in protein science · 2011Article
- Detection and analysis of proteins modified by O-linked N-acetylglucosamine.Current protocols in molecular biology · 2011Article
- Highly efficient chemoenzymatic synthesis of beta1-4-linked galactosides with promiscuous bacterial beta1-4-galactosyltransferases.Chemical communications (Cambridge, England) · 2010Article
- UDP-Gal: GlcNAc-R beta1,4-galactosyltransferase--a target enzyme for drug design. Acceptor specificity and inhibition of the enzyme.Glycoconjugate journal · 2006Article
- A chemical synthesis of UDP-LacNAc and its regioisomer for finding 'oligosaccharide transferases'.Glycoconjugate journal · 2006Article
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Authors and funding
8 authors at 3 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The capacity of UDP-N-acetyl-alpha-D-glucosamine (UDP-GlcNAc) as an in vitro acceptor substrate for beta-1,4-galactosyltransferase (beta4GalT1, EC 2.4.1.38) from human and bovine milk and for recombinant human beta4GalT1, expressed in Saccharomyces cerevisiae, was evaluated. It turned out that each of the enzymes is capable to transfer Gal from UDP-alpha-D-galactose (UDP-Gal) to UDP-GlcNAc, affording Gal(beta1-4)GlcNAc(alpha1-UDP (UDP-LacNAc). Using beta4GalT1 from human milk, a preparative enzymatic synthesis of UDP-LacNAc was carried out, and the product was characterized by fast-atom bombardment mass spectrometry and 1H and 13C NMR spectroscopy. Studies with all three beta4GalTs in the presence of alpha-lactalbumin showed that the UDP-LacNAc synthesis is inhibited and that UDP-alpha-D-glucose is not an acceptor substrate. This is the first reported synthesis of a nucleotide-activated disaccharide, employing a Leloir glycosyltransferase with a nucleotide-activated monosaccharide as acceptor substrate. Interestingly, in these studies beta4GalT1 accepts an alpha-glycosidated GlcNAc derivative. The results imply that beta4GalT1 may be responsible for the biosynthesis of UDP-LacNAc, previously isolated from human milk.
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