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  • Title: Key involvement of all three GlcNAc hydroxyl groups in the recognition of beta-D-GlcpNAc-(1-->2)-alpha-D-Manp-(1-->6)-beta-D-Glcp-OR by N-acetylglucosaminyltransferase-V.
    Author: Kanie O, Crawley SC, Palcic MM, Hindsgaul O.
    Journal: Bioorg Med Chem; 1994 Nov; 2(11):1231-41. PubMed ID: 7757419.
    Abstract:
    N-Acetylglucosaminyltransferase-V (GlcNAc T-V) transfers a beta-linked GlcNAc residue from UDP-GlcNAc to OH-6' (of the alpha Man residue) in oligosaccharides terminating in the sequence beta-D-GlcpNAc-(1-->2)-alpha-D-Manp-(1-->6)-beta-D-Glcp(or Manp)-OR (3, R = (CH2)7CH3). It was previously found that OH-4" (of the GlcNAc residue) in 3 was a critical element for substrate recognition by this enzyme. We show here that OH-3" and OH-6" are also key recognition elements. Four analogs of trisaccharide 3 where OH-3" and OH-6" were replaced, independently, by NH2 and NHAc groups, were prepared by multi-step chemical synthesis and kinetically evaluated as substrates for GlcNAc T-V from hamster kidney. These substitutions were selected since they replaced the OH groups with groups probing both hydrogen bonding and steric bulk. The 3"-modified compounds were found to be very poor substrates with Km values more than 50-fold elevated over that for 3 (26 microM) while the 6"-modified compounds were completely inactive. An intact 3,4,6 triol system in the terminal GlcNAc residue therefore appears to be the key polar group system that is recognized by this enzyme.
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