Date of Award
2009
Document Type
Thesis
Publication Status
Version of Record
Submission Date
October 2026
Abstract
Carbohydrate Active Enzyme family 6 (CA6) glycosyltransferases (GTs) are type II transmembrane proteins localized in the Golgi apparatus. CA6 GTs have a GT-A fold, a type of structure that resembles the Rossman fold and catalyze the transfer either galactose (Gal) or N-acetylgalactosamine (GalNAc) from the UDP nucleotide sugar to an non-reducing terminal Gal or GalNAc on an acceptor via an a-1,3 linkage. In this reaction, the anomeric configuration of the sugar moiety of the donor is retained in the product. CA6 GTs includes the histo-blood group A and B GTs, a-galactosyltransferase (a3GT), Forssman glycolipid synthase (FS), isogloboside 3 synthase (iGb3) in mammals. a3GT and its products (a-Gal epitode) are present in most mammals but are absent in humans and old world primates because of inactivating mutations. The absence of a3GT and its products results in the production of anti-a-Gal epitope natural antibodies in these species.
Extent
xvii, 150 p. : ill. (some col.).
Recommended Citation
Tumbale, Percy., "Structure-function relationships in eukaryotic and prokaryotic family 6 glycosyltransferases" (2009). Electronic Theses and Dissertations 2000 - 2009. 1786.
https://digitalcommons.fau.edu/etd_general_5/1786
Identifier
FADT186686
Comments
by Percy Tumbale.|Thesis (Ph.D.)--Florida Atlantic University, 2009.|Includes bibliography.|Electronic reproduction. Boca Raton, Fla., 2009. Mode of access: World Wide Web.|by Percy Tumbale.