B4GALT5
B4GALT5 (beta-1,4-galactosyltransferase 5, also known as beta4GalT-V) is a Golgi-resident glycosyltransferase that transfers galactose from UDP-galactose to acceptor sugars. It synthesises lactosylceramide, the starting point for ganglioside biosynthesis. Browse Assay Genie's current range of B4GALT5 research reagents below, or read on for the biology behind the target.
B4GALT5 catalyses the synthesis of lactosylceramide (LacCer) by transferring galactose from UDP-galactose to glucosylceramide (GlcCer). LacCer is the starting point in the biosynthesis of all gangliosides, the membrane-bound glycosphingolipids that play pivotal roles in the central nervous system, including neuronal maturation and axonal and myelin formation. B4GALT5 has also been reported to play a role in the glycosylation of BMPR1A and in regulation of its protein stability, and it is essential for extraembryonic development during early embryogenesis.
The B4GALT5 gene is one of seven beta-1,4-galactosyltransferase (beta4GalT) genes. These encode type II membrane-bound glycoproteins with apparent 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. The protein belongs to the glycosyltransferase 7 family and sits within the HGNC gene group of beta 4-glycosyltransferases. Its N-terminal hydrophobic signal sequence directs it to the Golgi apparatus and remains uncleaved to act as a transmembrane anchor.
By sequence similarity the beta4GalTs form four groups: beta4GalT1 and beta4GalT2, beta4GalT3 and beta4GalT4, beta4GalT5 and beta4GalT6, and beta4GalT7. The gene was previously designated B4GALT4 before being renamed B4GALT5, and the literature also refers to it as beta4GalT2. Its earlier name was UDP-Gal:betaGlcNAc beta 1,4-galactosyltransferase, polypeptide 5. The mouse ortholog is B4galt5.
B4GALT5 makes lactosylceramide from glucosylceramide, the first step towards all gangliosides, so it is a focus for studying glycosphingolipid metabolism.
Gangliosides contribute to neuronal maturation and to axonal and myelin formation in the CNS, linking this enzyme to nervous system biology.
B4GALT5 is essential for extraembryonic development during early embryogenesis, making it relevant to studies of early mammalian development.
The enzyme influences glycosylation and protein stability of BMPR1A, and belongs to a beta4GalT family with differing substrate roles.
B4GALT5 transfers galactose from UDP-galactose to glucosylceramide to form lactosylceramide, the starting point for all gangliosides. It also contributes to glycosylation of BMPR1A and regulation of its protein stability, and is essential for extraembryonic development during early embryogenesis.
B4GALT5 is also called beta4GalT-V, and its earlier name was UDP-Gal:betaGlcNAc beta 1,4-galactosyltransferase, polypeptide 5. The gene was previously designated B4GALT4, and in the literature it is also referred to as beta4GalT2, so check which name a source uses.
B4GALT5 has a mouse ortholog, B4galt5, and belongs to the glycosyltransferase 7 family. As a type II membrane protein it localises to the Golgi apparatus, where its uncleaved N-terminal signal sequence acts as a transmembrane anchor. Check the datasheet of any product for its validated reactivity.
Other beta-1,4-galactosyltransferases and glycosylation-related targets, including the BMPR1A receptor.
Gene and protein annotations from HGNC, NCBI Gene and UniProt O43286; product specifications from Assay Genie datasheets.