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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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The acceptor substrate specificity of human beta4-galactosyltransferase V indicates its potential function in O-glycosylation.

In order to assess the function of the different human UDP-Gal:GlcNAc beta4-galactosyltransferases, the cDNAs of two of them, beta4-GalT I and beta4-GalT V, were expressed in the baculovirus/insect cell expression system. The soluble recombinant enzymes produced were purified from the medium and used to determine their in vitro substrate specificities. The specific activity of the recombinant beta4-GalT V was more than 15 times lower than that of beta4-GalT I, using GlcNAc beta-S-pNP as an acceptor. Whereas beta4-GalT I efficiently acts on all substrates having a terminal beta-linked GlcNAc, beta4-GalT V appeared to be far more restricted in acceptor usage. Beta4-GalT V acts with high preference on acceptors that contain the GlcNAc beta1-->6GalNAc structural element, as found in O-linked core 2-, 4- and 6-based glycans, but not on substrates related to V-linked or blood group I-active oligosaccharides. These results suggest that beta4-GalT V may function in the synthesis of lacNAc units on O-linked chains, particularly in tissues which do not express beta4-GalT I, such as brain.[1]

References

  1. The acceptor substrate specificity of human beta4-galactosyltransferase V indicates its potential function in O-glycosylation. van Die, I., van Tetering, A., Schiphorst, W.E., Sato, T., Furukawa, K., van den Eijnden, D.H. FEBS Lett. (1999) [Pubmed]
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