Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
1979255 | Current Opinion in Structural Biology | 2010 | 7 Pages |
Abstract
Cell surface glycans play important cellular functions and are synthesized by glycosyltransferases. Structure and function studies show that the donor sugar specificity of the invertebrate β1,4-N-acetyl-glactosaminyltransferase (β4GalNAc-T) and the vertebrate β1,4-galactosyltransferase I (β4Gal-T1) are related by a single amino acid residue change. Comparison of the catalytic domain crystal structures of the β4Gal-T1 and the α-polypeptidyl-GalNAc-T (αppGalNAc-T) shows that their protein structure and sequences are similar. Therefore, it seems that the invertebrate β4GalNAc-T and the catalytic domain of αppGalNAc-T might have emerged from a common primordial gene. When vertebrates emerged from invertebrates, the amino acid that determines the donor sugar specificity of the invertebrate β4GalNAc-T might have mutated, thus converting the enzyme to a β4Gal-T1 in vertebrates.
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Authors
Boopathy Ramakrishnan, Pradman K Qasba,