Enzymatic characterization of CMP-NeuAc:Galβ1-4GlcNAc-R α(2-3)-sialyltransferase from human placenta

Nemansky, Martin; Dh, van den Eijnden

doi:10.1007/bf00731193

Cited by 35 publications

(15 citation statements)

References 48 publications

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“…Interestingly, it has been found previously that the Galfl(1M)GlcNAcfll-R ~(2-6)-sialyltransferase whether isolated from rat liver [10,21] or bovine colostrum [22] also can act on GalNAcfl(1-4)GlcNAcfll-R with high efficiency. In view of these results it will be of interest to investigate whether other Galfl(1M)GlcNAcfll-R specific glycosyltransferases such as a(2 3)-sialyltransferase [23], a3-galactosyltransferase [24] and fl3-N-acetylglucosaminyltransferase [25] are similarly capable of acting on GalNAcfl(1-4)GlcNAcfll-R.…”

Section: Discussionmentioning

confidence: 99%

Conversion of GalNAcβ(1–4)GlcNAcβ‐OMe into GalNAcβ(1–4)‐[Fucα(1–3)]GlcNAcβ‐OMe using human milk α3/4‐fucosyltransferase synthesis of a novel terminal element in glycoprotein glycans

et al. 1993

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Incubation of GalNAcβ(1–4)GlcNAcβ‐OMe with GDP‐Fuc in the presence of human milk α3/4‐fucosyltransferase resulted in the formation of GalNAcβ(1–4)[Fucα(1–3)]GlcNAcβ‐OMe. Under conditions that led to complete α3‐fucosylation of Galβ(1–4)GlcNAcβ‐OEt, GalNAcβ(1–4)GlcNAcβ‐OMe was fucosylated for more than 85%. For the identification of the isolated fucosylated products one‐ and two‐ dimensional 1H‐NMR spectroscopy was applied. In vacuo molecular dynamics simulations of Galβ(1–4)[Fucα(1–3)]GlcNAcβ‐OEt and GalNAcβ(1–4)[Fucα(1–3)]GlcNAcβ‐OMe using the CHARMm based force field CHEAT, demonstrated only small differences between the conformations of these compounds. This illustrates the minor conformational influence of the substituent at C‐2′, i.e. a hydroxyl function versus a N‐acetyl group.

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Section: Discussionmentioning

confidence: 99%

Conversion of GalNAcβ(1–4)GlcNAcβ‐OMe into GalNAcβ(1–4)‐[Fucα(1–3)]GlcNAcβ‐OMe using human milk α3/4‐fucosyltransferase synthesis of a novel terminal element in glycoprotein glycans

et al. 1993

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“…The structures of all acceptors with connective tissue or albumen gland p4GalNAc-T are summarized in Table 1. Compound 1 was prepared from human fibrinogen [24] and compound 2 from bovine fibrinogen [25]. Compound 3 was a gift of Dr G. Strecker (UniversitC des Sciences et Techniques de Lille Flandres-Artois, Laboratoire de Chimie Biologique, Villeneuve d'Ascq, France), compounds 4-7 were gifts of Dr J. Lonngren (Stockholm University, Stockholm, Sweden), and compound 13 was a gift of Dr J. G. M. van der Ven (Bijvoet Center, Department of Bio-Organic Chemistry).…”

Section: Methodsmentioning

confidence: 99%

Identification of a Novel UDP‐GalNAc:GlcNAcβ‐Rβ1–4 N‐Acetylgalactosaminyltransferase from the Albumen Gland and Connective Tissue of the Snail Lymnaea stagnalis

Mulder¹,

Spronk²,

Schachter³

et al. 1995

European Journal of Biochemistry

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Both the albumen gland, one of the female accessory sex glands, and connective tissue of the freshwater snail Lymnaea stagnalis contain N-acetylgalactosaminyltransferase activity, capable of transferring GalNAc from UDP-GalNAc in Pl -4 linkage to the terminal GlcNAc residue of GlcNAcP-R. The albumin gland enzyme was partially purified by affinity chromatography on UDP-hexanolamine-Sepharose 4B. Using GlcNAcPl -2Manal-6(GlcNAcP1-2Manal-3)Man~l-4GlcNAcP1-4GlcNAc or GlcNAcPlOMe as substrates, the enzyme showed an absolute requirement for MnZ+ with an optimum concentration of 12.5-50 mM. The optimal pH was approximately pH 7.0. The enzyme activity was independent of the Triton X-100 concentration in the range 0.25-2.5%, and no activation effect was found. The more labile connective tissue microsomal enzyme, subjected to the same optimization procedure, gave comparable results. Both enzyme activities have similar substrate specificities towards GlcNAc or GlcNAcPlOMe, and towards oligosaccharides or glycopeptides with a non-reducing terminal P-GlcNAc unit, but cannot act on GlcNAcal-OMe. Saccharides with non-reducing terminal Gal or GalNAc residues, and free GalNAc, Gal or Glc residues are not acceptors. Product analysis was carried out for albumen gland N-acetylgalactosaminyltransferase and four acceptors having GlcNAcPl -R as the terminal non-reducing unit, and for connective tissue N-acetylgalactosaminyltransferase with GlcNAcPl-OMe as acceptor. In all instances, products with GalNAc PI -4-linked to GlcNAc were obtained, showing that the connective tissue and the albumen gland activities are probably from one enzyme. This enzyme activity can be identified as UDP-GalNAc :GlcNAcP-R Pl -4 N-acetylgalactosaminyltransferase, and is probably involved in the biosynthesis of N,N'-diacetyllactosediamine-containing glycoproteins, like hemocyanin, in the snail L. stugnalis.

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Section: Enzymes and Activity Assaysmentioning

confidence: 99%

“…On the other hand two ~3-NeuAcTs have been described that are capable to catalize the synthesis of a NeuAc~2---> 3Galfll ~ 4GIcNAc sequence. In human placenta a ~3-NeuAcT was identified [12] that was later shown to have a high preference for Galfll-~4GlcNAc [13]. Recently a sialyltransferase has been cloned that probably corresponds to this placenta enzyme [14,15].…”

Section: Introductionmentioning

confidence: 99%

“…The results obtained in these studies, therefore, did not provide an explanation for the specific ~2--* 3/ct2--~ 6-sialylation patterns occurring on N-linked oligosaccharide chains. We have recently determined the acceptor specificity of the c~3-NeuAcT from placenta with di-, tri-and tetra-antennary glycan structures [13]. In this study these data are complemented with the acceptor properties of these branched substrates for the ~6-NeuAcT isolated from bovine colostrum.…”

Section: Introductionmentioning

confidence: 99%

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Branching and elongation with lactosaminoglycan chains of N‐linked oligosaccharides result in a shift toward termination with α2→3‐linked rather than with α2→6‐linked sialic acid residues

1995

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The activity of bovine colostrum CMP-NeuAc: Gal/31--~4GIcNAcl3-R c~2-->6-sialyltransferase (a6-NenAcT) toward oligosaccharides that form part of complex-type, Nlinked glycans appears significantly reduced when a bisecting GlcNAc residue or additional branches are present, or when core GIcNAc residues are absent. By contrast human placenta CMPNeuAc: Gall~l -->4GicNAc/]-R a2--> 3-sialyltransferase (a3-NeuAcT) is much less sensitive to structural variations in these acceptors. Furthermore the a3-NeuAcT shows a much higher activity than the c~6-NeuAcT with oligosaccharides that form part of linear and branched iactosaminoglycan extensions. These results indicate that, in tissues that express both enzymes, branching and lactosaminoglycan formation of N-linked glycans will cause a shift from termination with ~2-->6-1inked sialic acid to termination with a2-->3-1inked sialic acid residues. These findings provide an enzymatic basis for the sialic acid linkage-type patterns found on the oligosaccharide chains of N-glycoproteins.

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Enzymatic characterization of CMP-NeuAc:Galβ1-4GlcNAc-R α(2-3)-sialyltransferase from human placenta

Cited by 35 publications

References 48 publications

Conversion of GalNAcβ(1–4)GlcNAcβ‐OMe into GalNAcβ(1–4)‐[Fucα(1–3)]GlcNAcβ‐OMe using human milk α3/4‐fucosyltransferase synthesis of a novel terminal element in glycoprotein glycans

Conversion of GalNAcβ(1–4)GlcNAcβ‐OMe into GalNAcβ(1–4)‐[Fucα(1–3)]GlcNAcβ‐OMe using human milk α3/4‐fucosyltransferase synthesis of a novel terminal element in glycoprotein glycans

Identification of a Novel UDP‐GalNAc:GlcNAcβ‐Rβ1–4 N‐Acetylgalactosaminyltransferase from the Albumen Gland and Connective Tissue of the Snail Lymnaea stagnalis

Branching and elongation with lactosaminoglycan chains of N‐linked oligosaccharides result in a shift toward termination with α2→3‐linked rather than with α2→6‐linked sialic acid residues

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