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Molecular cloning and characterization of β1,4‐ N ‐acetylgalactosaminyltransferases IV synthesizing N , N ′‐diacetyllactosediamine 1
Author(s) -
Gotoh Masanori,
Sato Takashi,
Kiyohara Katsue,
Kameyama Akihiko,
Kikuchi Norihiro,
Kwon Yeon-Dae,
Ishizuka Yasuko,
Iwai Toshie,
Nakanishi Hiroshi,
Narimatsu Hisashi
Publication year - 2004
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(04)00219-4
Subject(s) - complementary dna , genbank , open reading frame , cloning (programming) , accession number (library science) , microbiology and biotechnology , recombinant dna , molecular cloning , enzyme , peptide sequence , amino acid , sequence (biology) , gene , molecular mass , biology , biochemistry , chemistry , computer science , programming language
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.