FEBS Letters | |
Molecular cloning and characterization of β1,4‐N‐acetylgalactosaminyltransferases IV synthesizing N,N′‐diacetyllactosediamine1 | |
Kameyama, Akihiko2  Kwon, Yeon-Dae2  Narimatsu, Hisashi2  Iwai, Toshie2  Ishizuka, Yasuko2  Nakanishi, Hiroshi1  Kikuchi, Norihiro2  Sato, Takashi2  Gotoh, Masanori2  Kiyohara, Katsue2  | |
[1]Biological Information Research Center, AIST, Central-6, 1-1 Higashi, Tsukuba, Ibaraki 305-8568, Japan | |
[2]Glycogene Function Team, Research Center for Glycoscience, National Institute of Advanced Industrial Science and Technology (AIST), Open Space Laboratory Central-2, 1-1-1 Umezono, Tsukuba, Ibaraki 305-8568, Japan | |
关键词: Glycosyltransferase; N-Acetylgalactosaminyltransferase; N-Glycan; N; N′-Diacetyllactosediamine; Glycodelin; Lutropin; LacdiNAc; N; N′-diacetyllactosediamine (GalNAcβ1-4GlcNAc); GalNAc; N-acetylgalactosamine; GlcNAc; N-acetylglucosamine; LH; lutropin; Man; mannose; Gd; glycodelin; NeuAc; N-acetylneuraminic acid; Gal; galactose; Le; Lewis; Lex; Galβ1-4(Fucα1-3)GlcNAc; Fuc; fucose; Ley; Fucα1-2Galβ1-4(Fucα1-3)GlcNAc; β4GalNAc-T; β1; 4-N-acetylgalactosaminyltransferase; β4GT; β1; 4-glycosyltransferase; EST; expressed sequence tag; ORF; open reading frame; RACE; rapid amplification of cDNA ends; HEK; human embryonic kidney; GlcA; glucuronic acid; pNp; para-nitrophenyl; Bz; benzyl; Glc; glucose; Xyl; xylose; MS; mass spectrometry; MALDI-TOF; matrix-assisted laser desorption/ionization-time of flight; GAPDH; glyceraldehyde-3-phosphate dehydrogenase; HPLC; high performance liquid chromatography; | |
DOI : 10.1016/S0014-5793(04)00219-4 | |
学科分类:生物化学/生物物理 | |
来源: John Wiley & Sons Ltd. | |
【 摘 要 】
A sequence highly homologous to β1,4-N-acetylgalactosaminyltransferase III (β4GalNAc-T3) was found in a database of human expressed sequence tags. The full-length open reading frame of the gene, β4GalNAc-T4 (GenBank accession number AB089939), was cloned using the 5′ rapid amplification of cDNA ends method. It encodes a typical type II transmembrane protein of 1039 amino acids having 42.6% identity with β4GalNAc-T3. The recombinant enzyme transferred N-acetylgalactosamine to N-acetylglucosamine-β-benzyl with a β1,4-linkage to form N,N′-diacetyllactosediamine as did β4GalNAc-T3. In specificity toward oligosaccharide acceptor substrates, it was quite similar to β4GalNAc-T3 in vitro, however, the tissue distributions of the two enzymes were quite different. These results indicated that the two enzymes have similar roles in different tissues.
【 授权许可】
Unknown
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