Abstract：
:Galactokinase catalyses the ATP-dependent phosphorylation of galactose. A galactokinase-like sequence was identified in a Fasciola hepatica EST library. Recombinant expression of the corresponding protein in Escherichia coli resulted in a protein of approximately 50 kDa. The protein is monomeric, like galactokinases from higher animals, yeasts and some bacteria. The protein has no detectable enzymatic activity with galactose or N-acetylgalactosamine as a substrate. However, it does bind to ATP. Molecular modelling predicted that the protein adopts a similar fold to galactokinase and other GHMP kinases. However, a key loop in the active site was identified which may influence the lack of activity. Sequence analysis strongly suggested that this protein (and other proteins annotated as "galactokinase" in the trematodes Schistosoma mansoni and Clonorchis sinensis) are closer to N-acetylgalactosamine kinases. No other galactokinase-like sequences appear to be present in the genomes of these three species. This raises the intriguing possibility that these (and possibly other) trematodes are unable to catabolise galactose through the Leloir pathway due to the lack of a functional galactokinase.
journal_name
Exp Parasitoljournal_title
Experimental parasitologyauthors
Zinsser VL,Cox C,McAuley M,Hoey EM,Trudgett A,Timson DJdoi
10.1016/j.exppara.2018.07.013subject
Has Abstractpub_date
2018-09-01 00:00:00pages
65-72eissn
0014-4894issn
1090-2449pii
S0014-4894(18)30054-7journal_volume
192pub_type
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