Structures of Human Ketohexokinase Isoforms
Author Information
Author(s): Trinh Chi H., Asipu Aruna, Bonthron David T., Phillips Simon E. V.
Primary Institution: University of Leeds
Hypothesis
The effect of the Ala43Thr mutation may confer a selective deficiency of KHK-C while preserving KHK-A activity.
Conclusion
The study reveals structural differences between the KHK-A and KHK-C isoforms that affect their stability and function.
Supporting Evidence
- The study solved the crystal structures of KHK-A and KHK-C, revealing differences in their active sites.
- KHK-A was found to be more thermostable than KHK-C.
- Mutations Gly40Arg and Ala43Thr were modeled in the context of the KHK structure.
Takeaway
Scientists studied two versions of a protein that helps break down sugar, finding that small changes in the protein can affect how well it works.
Methodology
The structures were determined using X-ray crystallography and molecular replacement techniques.
Limitations
The resolution of the KHK-C structure was lower than that of KHK-A, affecting the clarity of the active site.
Digital Object Identifier (DOI)
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