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Molecular cloning and expression of mouse ceramide glucosyltransferase
Author(s) -
Ichikawa Shinichi,
Ozawa Katsuya,
Hirabayashi Yoshio
Publication year - 1998
Publication title -
iubmb life
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.132
H-Index - 113
eISSN - 1521-6551
pISSN - 1521-6543
DOI - 10.1080/15216549800202282
Subject(s) - glucosyltransferase , complementary dna , biology , ceramide , biochemistry , glucosyltransferases , peptide sequence , glycosylation , cloning (programming) , homology (biology) , microbiology and biotechnology , amino acid , gene , apoptosis , computer science , programming language
Ceramide glucosyltransferase (EC 2.4.1.80) catalyzcs the first glycosylation step of glycosphingolipid (GSL) synthesis, the transfer of glucose from UDP‐Glucose to hydrophobic ceramide and generate gtucosylceramide (GlcCer). We have chined mouse ceramide glucosyltransferase cDNA from a brain cDNA library by PCR based homology cloning. The nucleotide sequence determination revealed that mouse ceramidc glucosyltransferase cDNA encodes 394 amino acids with a calculated molecular mass of 45 kDa. The amino acid sequence of mouse ceramide glucosyltransferase showed 98% identity with the human sequence. Homology searches against currently available databases identified three homologous proteins in Caenorhabditis elegans and one homologous protein in Cyanobacteria. Highly conserved sequences of ceramide glucosyltransferases and the homologs among a wide variety of organisms suggest biological significance of the lipid glucosylation system.