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Enzymatic synthesis of blood group A and B trisaccharide analogues by Nina O.L Seto; Catherine A Compston; Adam Szpacenko; Monica M Palcic is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.

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Glycosyltransferases A and B utilize the donor substrates UDP-GalNAc and UDP-Gal, respectively, in the biosynthesis of the human blood group A and B trisaccharide antigens from the O(H)-acceptor substrates. These enzymes were cloned as synthetic genes and expressed in Escherichia coli, thereby generating large quantities of enzyme for donor specificity evaluations. The amino acid sequence of glycosyltransferase A only differs from glycosyltransferase B by four amino acids, and alteration of these four amino acid residues (Arg-176 Gly, Gly-235 Ser, Leu-266 Met and Gly-268Ala) can change the donor substrate specificity from UDP-GalNAc to UDP-Gal. Crossovers in donor substrate specificity have been observed, i.e., the A transferase can utilize UDP-Gal and B transferase can utilize UDP-GalNAc donor substrates. We now report a unique donor specificity for each enzyme type. Only A transferase can utilize UDP-GlcNAc donor substrates synthesizing the blood group A trisaccharide analog a-D-Glcp-NAc-(1 3)-[a-L-Fucp-(1 2)]-b-D-Galp-O-(CH 2 ) 7 CH 3 (4). Recombinant blood group B was shown to use UDP-Glc donor substrates synthesizing blood group B trisaccharide analog a-D-Glcp- In addition, a

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Author

Nina O.L Seto; Catherine A Compston; Adam Szpacenko; Monica M Palcic

Publisher

Elsevier Science; Elsevier ; Elsevier Ltd.; Elsevier BV (ISSN 0008-6215)

Published

2000

Language

EN

Field

Biochemistry, Genetics and Molecular Biology (Life Sciences)