Beta-1,4-galactosyltransferase 5 is an enzyme that in humans is encoded by the B4GALT5gene.[1][2][3]
This gene is one of seven beta-1,4-galactosyltransferase (beta4GalT) genes. They encode type II membrane-bound glycoproteins that appear to have exclusive specificity for the donor substrate UDP-galactose; all transfer galactose in a beta1,4 linkage to similar acceptor sugars: GlcNAc, Glc, and Xyl. Each beta4GalT has a distinct function in the biosynthesis of different glycoconjugates and saccharide structures. As type II membrane proteins, they have an N-terminal hydrophobic signal sequence that directs the protein to the Golgi apparatus and which then remains uncleaved to function as a transmembrane anchor. By sequence similarity, the beta4GalTs form four groups: beta4GalT1 and beta4GalT2, beta4GalT3 and beta4GalT4, beta4GalT5 and beta4GalT6, and beta4GalT7. The function of the enzyme encoded by this gene is not clear. This gene was previously designated as B4GALT4 but was renamed to B4GALT5. In the literature it is also referred to as beta4GalT2.[3]
References
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Xu S, Zhang S, Chen C, et al. (2003). "Over-expression of beta-1,4-galactosyltransferase V increases the growth of astrocytoma cell line". J. Exp. Clin. Cancer Res. 21 (3): 409–14. PMID12385586.
Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID14702039.
Sato T, Furukawa K (2004). "Transcriptional regulation of the human beta-1,4-galactosyltransferase V gene in cancer cells: essential role of transcription factor Sp1". J. Biol. Chem. 279 (38): 39574–83. doi:10.1074/jbc.M405805200. PMID15263012.
Jiang J, Chen X, Shen J, et al. (2006). "Beta1,4-galactosyltransferase V functions as a positive growth regulator in glioma". J. Biol. Chem. 281 (14): 9482–9. doi:10.1074/jbc.M504489200. PMID16461357.
Sato T, Furukawa K (2007). "Sequential action of Ets-1 and Sp1 in the activation of the human beta-1,4-galactosyltransferase V gene involved in abnormal glycosylation characteristic of cancer cells". J. Biol. Chem. 282 (38): 27702–12. doi:10.1074/jbc.M611862200. PMID17656364.
Kitayama K, Hayashida Y, Nishida K, Akama TO (2007). "Enzymes responsible for synthesis of corneal keratan sulfate glycosaminoglycans". J. Biol. Chem. 282 (41): 30085–96. doi:10.1074/jbc.M703695200. PMID17690104.