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Alpha1--&gt;3/4fucosyltransferases (FucTs) from several species contain a highly conserved His-His motif adjacent to an enzyme region correlating with the ability to catalyze fucose transfer to type 1 chain acceptors. Site-directed mutagenesis has been employed to analyze structure-function relationships of this His-His motif in human FucT-IV. The results indicate that most changes of His(113) and His(114) and nearby residues of FucT-IV reduced the specific activity of the enzymes. Analysis of acceptor properties demonstrated close similarity of most mutants with wild-type FucT-IV, whereas an apparent preference for the H-type II acceptor was observed for the His(114) mutants. Kinetic studies demonstrated that mutants of His(114) had a substantially increased K(m) for acceptor compared to other enzymes tested. The dramatic increase in acceptor K(m) for the His(114) mutants, particularly for the nonfucosylated acceptor, suggests that this His-His motif is involved in acceptor binding and perhaps interacts with GlcNAc residues of type 2 acceptors. The presence of fucose in acceptor substrates may promote more efficient substrate binding and presumably partially overcomes the weaker interaction with GlcNAc caused by the mutation.

A highly conserved His-His motif present in 1->3/4fucosyltransferases is required for optimal activity and functions in acceptor binding