B3GAT3 explained
Galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase 3 is an enzyme that in humans is encoded by the B3GAT3 gene.[1]
The protein encoded by this gene is a member of the glucuronyltransferase gene family, enzymes that exhibit strict acceptor specificity, recognizing nonreducing terminal sugars and their anomeric linkages. This gene product catalyzes the formation of the glycosaminoglycan-protein linkage by way of a glucuronyl transfer reaction in the final step of the biosynthesis of the linkage region of proteoglycans.[2]
Further reading
- Rual JF, Venkatesan K, Hao T . Towards a proteome-scale map of the human protein-protein interaction network. . Nature . 437 . 7062 . 1173–8 . 2005 . 16189514 . 10.1038/nature04209 . 2005Natur.437.1173R . 4427026 . etal.
- Venkatesan N, Barré L, Benani A . Stimulation of proteoglycan synthesis by glucuronosyltransferase-I gene delivery: A strategy to promote cartilage repair . Proc. Natl. Acad. Sci. U.S.A. . 101 . 52 . 18087–92 . 2005 . 15601778 . 10.1073/pnas.0404504102 . 535800 . etal. free .
- Gulberti S, Lattard V, Fondeur M . Phosphorylation and sulfation of oligosaccharide substrates critically influence the activity of human beta1,4-galactosyltransferase 7 (GalT-I) and beta1,3-glucuronosyltransferase I (GlcAT-I) involved in the biosynthesis of the glycosaminoglycan-protein linkage region of proteoglycans . J. Biol. Chem. . 280 . 2 . 1417–25 . 2005 . 15522873 . 10.1074/jbc.M411552200 . etal. free .
- Gerhard DS, Wagner L, Feingold EA . The Status, Quality, and Expansion of the NIH Full-Length cDNA Project: The Mammalian Gene Collection (MGC) . Genome Res. . 14 . 10B . 2121–7 . 2004 . 15489334 . 10.1101/gr.2596504 . 528928 . etal.
- Gulberti S, Fournel-Gigleux S, Mulliert G . The functional glycosyltransferase signature sequence of the human beta 1,3-glucuronosyltransferase is a XDD motif . J. Biol. Chem. . 278 . 34 . 32219–26 . 2003 . 12794088 . 10.1074/jbc.M207899200 . etal. free .
- Strausberg RL, Feingold EA, Grouse LH . Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences . Proc. Natl. Acad. Sci. U.S.A. . 99 . 26 . 16899–903 . 2003 . 12477932 . 10.1073/pnas.242603899 . 139241 . 2002PNAS...9916899M . etal. free .
- Kitagawa H, Taoka M, Tone Y, Sugahara K . Human glycosaminoglycan glucuronyltransferase I gene and a related processed pseudogene: genomic structure, chromosomal mapping and characterization . Biochem. J. . 358 . Pt 3 . 539–46 . 2001 . 11535117 . 10.1042/0264-6021:3580539 . 1222090 .
- Pedersen LC, Tsuchida K, Kitagawa H . Heparan/chondroitin sulfate biosynthesis. Structure and mechanism of human glucuronyltransferase I . J. Biol. Chem. . 275 . 44 . 34580–5 . 2000 . 10946001 . 10.1074/jbc.M007399200 . etal. free .
- Ouzzine M, Gulberti S, Netter P . Structure/function of the human Ga1beta1,3-glucuronosyltransferase. Dimerization and functional activity are mediated by two crucial cysteine residues . J. Biol. Chem. . 275 . 36 . 28254–60 . 2000 . 10842173 . 10.1074/jbc.M002182200 . etal. free .
- Tone Y, Kitagawa H, Imiya K . Characterization of recombinant human glucuronyltransferase I involved in the biosynthesis of the glycosaminoglycan-protein linkage region of proteoglycans . FEBS Lett. . 459 . 3 . 415–20 . 1999 . 10526176 . 10.1016/S0014-5793(99)01287-9 . 7878952 . etal. free . 1999FEBSL.459..415T .
- Herman T, Horvitz HR . Three proteins involved in Caenorhabditis elegans vulval invagination are similar to components of a glycosylation pathway . Proc. Natl. Acad. Sci. U.S.A. . 96 . 3 . 974–9 . 1999 . 9927678 . 10.1073/pnas.96.3.974 . 15335 . 1999PNAS...96..974H . free .
Notes and References
- Kitagawa H, Tone Y, Tamura J, Neumann KW, Ogawa T, Oka S, Kawasaki T, Sugahara K . Molecular cloning and expression of glucuronyltransferase I involved in the biosynthesis of the glycosaminoglycan-protein linkage region of proteoglycans . J Biol Chem . 273 . 12 . 6615–8 . Apr 1998 . 9506957 . 10.1074/jbc.273.12.6615 . free .
- Web site: Entrez Gene: B3GAT3 beta-1,3-glucuronyltransferase 3 (glucuronosyltransferase I).