Commentary on Copyright Act 1814

Legislation replacing the Statute of Anne 1710 (uk_1710) and providing that copyright in a literary work would last for twenty-eight years from the time of publication, but that ‘if the author shall be living' at the end of that period then the work was to be protected ‘for the residue of his natural life'.
The commentary explores the background to the legislation, and in particular the controversy over the library deposit provision in the wake of the decision in Beckford v. Hood (1798) (uk_1798a). The commentary suggests that the introduction of the reversionary lifetime copyright term had more to do with the opportunistic and timely intervention of one Member of Parliament (Samuel Egerton Brydges) than with any principled or considered position adopted on the part of the legislature.

Insight into the mechanism of galactokinase: role of a critical glutamate residue and helix/coil transitions

Galactokinase, the enzyme which catalyses the first committed step in the Leloir pathway, has attracted interest due to its potential as a biocatalyst and as a possible drug target in the treatment of type I galactosemia. The mechanism of the enzyme is not fully elucidated. Molecular dynamics (MD) simulations of galactokinase with the active site residues Arg-37 and Asp-186 altered predicted that two regions (residues 174-179 and 231-240) had different dynamics as a consequence. Interestingly, the same two regions were also affected by alterations in Arg-105, Glu-174 and Arg- 228. These three residues were identified as important in catalysis in previous computational studies on human galactokinase. Alteration of Arg-105 to methionine resulted in a modest reduction in activity with little change in stability. When Arg-228 was changed to methionine, the enzyme’s interaction with both ATP and galactose was affected. This variant was significantly less stable than the wild-type protein. Changing Glu-174 to glutamine (but not to aspartate) resulted in no detectable activity and a less stable enzyme. Overall, these combined in silico and in vitro studies demonstrate the importance of a negative charge at position 174 and highlight the critical role of the dynamics in to key regions of the protein. We postulate that these regions may be critical for mediating the enzyme’s structure and function.