Abstract
The enzyme β4-galactosyltransferase-I (β4GalT-I; UDP-Gal:GlcNAc β4-galactosyltransferase; EC 2.4.1.38) is a constitutively expressed, trans-Golgi resident, type II membrane-bound glycoprotein that is widely distributed in vertebrates. The protein domain structure established for β4GalT-I consists of: (1) a short NH2-terminal cytoplasmic domain of 11 or 24 amino acids depending on the protein isoform (Shaper et al. 1988; Russo et al. 1990); (2) a large COOH-terminal luminal domain containing the catalytic center (~270 amino acids) linked to a single transmembrane domain (19 amino acids) through a glycosylated peptide segment (~86 amino acids) termed the stem region. In essentially all vertebrate tissues, the primary function of β4GalT-I is to catalyze the transfer of Gal from UDP-Gal to GlcNAcβ-R, forming the N-acetyllactosamine (Galβ1-4GlcNAcβ1-R) or poly-N-acetyllactosamine structures assembled on glycoconjugates.
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References
Asano M, Furukawa K, Kido M, Matsumoto S, Umesaki Y (1997) Growth retardation and early death of β1,4-galactosyltransferase knockout mice with augmented proliferation and abnormal differentiation of epithelial cells. EMBO J 16:1850–1855
Andrews P (1970) Purification of lactose synthetase A protein from human milk and demonstration of its interaction with α-lactalbumin. FEBS Lett 9:297–300
Barker R, Olsen KW, Shaper JH, Hill RL (1972) Agarose derivatives of uridine diphosphate and N-acetylglucosamine for the purification of a galactosyltransferase. J Biol Chem 247:7135–7147
Bendiak B, Ward LD, Simpson RJ (1993) Proteins of the Golgi apparatus: purification to homogeneity, N-terminal sequence, and unusually large Stokes radius of the membrane-bound form of UDP-galactose:N-acetylglucosamine β1-4galactosyltrans-ferase from rat liver. Eur J Biochem 216:405–417
Brew K, Vanaman TC, Hill RL (1968) The role of α-lactalbumin and the A protein in lactose synthetase: a unique mechanism for the control of a biological reaction. Proc Natl Acad Sci USA 59:491–497
Brodbeck U, Ebner KE (1966) Resolution of a soluble lactose synthetase into two protein components and solubilization of microsomal lactose synthetase. J Biol Chem 241:1391–1397
Charron M, Shaper JH, Shaper NL (1998) The increased level of β1,4-galactosyltransferase required for lactose biosynthesis is achieved in part by translational control. Proc Natl Acad Sci USA 95:14805–14810
Charron M, Shaper NL, Rajput B, Shaper JH (1999) A novel 14-base-pair regulatory element is essential for in vivo expression of murine β4-galactosyltransferase-l in late pachytene spermatocytes and round spermatids. Mol Cell Biol 19:5823–5832
Chung SJ, Takayama S, Wong C-H (1998) Acceptor substrate-based selective inhibition of galactosyltransferases. Bioorg Med Chem Lett 8:3359–3364
Ebner KE, Mawal R, Fitzgerald DK, Colvin B (1972) Lactose synthetase (UDP-D-galactose:acceptor β-4-galactosyltransferase) from bovine milk. Methods Enzymol 28:500–510
Fleischer B, Mclntyre JO, Kempner ES (1993) Target sizes of galactosyltransferase, sialyltransferase, and uridine diphosphatase in Golgi apparatus of rat liver. Biochemistry 32:2076–2081
Gastinel LN, Cambillau C, Bourne Y (1999) Crystal structures of the bovine β4-galactosyltransferase catalytic domain and its complex with uridine diphosphogalactose. EMBO J 18:3546–3557
Grobler JA, Rao KR, Pervaiz S, Brew K (1994) Protein sequences of two highly divergent canine type c lysozymes: implications for the evolutionary origins of the lysozyme α-lactalbumin superfamily. Arch Biochem Biophys 313:360–366
Harduin-Lepers A, Shaper NL, Mahoney JA, Shaper JH (1992) Murine β1,4 galactosyltransferase: round spermatid transcripts are characterized by an extended 5′-untranslated region. Glycobiology 2:361–368
Hashimoto H, Endo T, Kajihara Y (1997) Synthesis of the first tricomponent bisubstrate analog that exhibits potent inhibition against GlcNAc: β-1,4-galactosyltransferase. J Org Chem 62:1914–1915
Lo N-W, Shaper JH, Pevsner J, Shaper NL (1998) The expanding β4-galactosyltransferase gene family: messages from the databanks. Glycobiology 8:517–526
Lu Q-X, Hasty P, Shur BD (1997) Targeted mutation in β1,4-galactosyltransferase leads to pituitary insufficiency and neonatal lethality. Dev Biol 181:257–267
McGuire EJ, Jourdian GW, Carlson DM, Roseman S (1965) Incorporation of D-galactose into glycoproteins. J Biol Chem 240:PC4112–4115
Nixon B, Lu Q, Wassler MJ, Foote CI, Ensslin MA, Shur BD (2001) Galactosyltransferase function during mammalian fertilization. Cells Tissues Organs 168:46–57
Rajput B, Shaper NL, Shaper JH (1996) Transcriptional regulation of murine β1,4 galactosyltransferase in somatic cells: analysis of a gene that serves both a housekeeping and a mammary gland-specific function. J Biol Chem 271:5131–5142
Russo RN, Shaper NL, Shaper JH (1990) Bovine β1,4-galactosyltransferase: two sets of mRNA transcripts encode two forms of the protein with different amino-terminal domains. J Biol Chem 265:3324–3331
Shaper NL, Hollis GF, Douglas JG, Kirsch IR, Shaper JH (1988) Characterization of the full length cDNA for murine β-1,4-galactosyltransferase: novel features at the 5′-end predict two translational start sites at two in-frame AUG’s. J Biol Chem 263:10420–10428
Shaper NL, Meurer JA, Joziasse DH, Chou TD, Smith EJ, Schnaar RL, Shaper JH (1997) The chicken genome contains two functional nonallelic β1,4-galactosyltransferase genes: chromosomal assignment to syntenic regions tracks fate of the two gene lineages in the human genome. J Biol Chem 272:31389–31399
Smith CA, Brew K (1977) Isolation and characteristics of galactosyltransferase from Golgi membranes of lactating sheep mammary glands. J Biol Chem 252:7294–7299
Snow DM, Shaper JH, Shaper NL, Hart GW (1999) Determination of β1,4-galactosyltransferase enzymatic activity by capillary electrophoresis and laserinduced fluorescence detection. Anal Biochem 271:36–42
Spiro RG (1962) Studies on the monosaccharide sequence of the serum glycoprotein fetuin. J Biol Chem 237:646–652
Strous GJ, van Kerkhof P, Fallon RJ, Schwartz AL (1987) Golgi galactosyltransferase contains serine-linked phosphate. Eur J Biochem 169:307–311
Takayama S, Chung SJ, Igarashi Y, Ichikawa Y, Sepp A, Lechler RI, Wu J, Hayashi T, Siuzdak G, Wong C-H (1999) Selective inhibition of β-1,4-and α-1,3-galactosyltransferases: donor sugar-nucleotide based approach. Bioorg Med Chem 7:401–409
Trayer IP, Hill RL (1971) The purification and properties of the A protein of lactose synthetase. J Biol Chem 246:6666–6675
Watkins W, Hassid WZ (1962) The synthesis of lactose by particulate enzyme preparations from guinea pig and bovine mammary glands. J Biol Chem 237:1432–1440
Zhou D, Malissard M, Berger EG, Hennet T (2000) Secretion and purification of recombinant galactosyltransferase from insect cells using pFmel-protA, a novel transponsition-based baculovirus transfer vector. Arch Biochem Biophys 373:3–7
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© 2002 Springer Japan
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Shaper, N.L., Shaper, J.H. (2002). β4-Galactosyltransferase-I. In: Taniguchi, N., et al. Handbook of Glycosyltransferases and Related Genes. Springer, Tokyo. https://doi.org/10.1007/978-4-431-67877-9_2
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DOI: https://doi.org/10.1007/978-4-431-67877-9_2
Publisher Name: Springer, Tokyo
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