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Helena Kristiansson and Dr. David J. Timson Increased Promiscuity of Human Galactokinase Following Alteration of a Single Amino Acid Residue Distant from the Active Site ChemBioChem 12

Version of Record online: 11 JUL 2011 | DOI: 10.1002/cbic.201100308

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Making moves: The specificity of human galactokinase has been expanded by alteration of a tyrosine residue such that the enzyme is able to catalyse phosphorylation of D-mannose and D-fructose. This residue most likely controls the enzyme's specificity by modulating the flexibility of residues in the active site.

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