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Structure-based evolutionary relationship of glycosyltransferases: a case study of vertebrate beta 1,4-galactosyltransferase, invertebrate beta 1,4-N-acetylgalactosaminyltransferase and alpha-polypeptidyl-N-acetylgalactosaminyltransferase

  1. Author:
    Ramakrishnan, B.
    Qasba, P. K.

  2. Author Address

    [Ramakrishnan, Boopathy; Qasba, Pradman K.] NCI, Struct Glycobiol Sect, Ctr Canc Res, Nanobiol Program, Frederick, MD 21702 USA. [Ramakrishnan, Boopathy] NCI, Basic Res Program, SAIC Frederick Inc, Ctr Canc Res,Nanobiol Program, Frederick, MD 21702 USA.;Qasba, PK, NCI, Struct Glycobiol Sect, Ctr Canc Res, Nanobiol Program, Frederick, MD 21702 USA.
    1. Year: 2010
    2. Date: Oct
  2. Journal: Current Opinion in Structural Biology
    1. 20
    2. 5
    3. Pages: 536-542
  4. Type of Article: Review
  5. ISSN: 0959-440X
  1. 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 beta 1,4-N-acetyl-glactosaminyltransferase (beta 4GaINAc-T) and the vertebrate beta 1 4-galactosyltransferase I (beta 4Gal-T1) are related by a single amino acid residue change Comparison of the catalytic domain crystal structures of the beta 4Gal-T1 and the alpha-polypeptidyl-GaINAc-T (alpha ppGaINAc-T) shows that their protein structure and sequences are similar Therefore, it seems that the invertebrate beta 4GaINAc-T and the catalytic domain of alpha ppGaINAc-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 beta 4GaINAc-T might have mutated thus converting the enzyme to a beta 4Gal-T1 in vertebrates

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External Sources

  1. View Full Text
  2. DOI: 10.1016/j.sbi.2010.07.004
  3. View record in Web of Science®
  4. WOS: 000284676900002

Library Notes

  1. Fiscal Year: FY2010-2011
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