Chris expanded our transaminase toolbox by cloning a new (R) selective enzyme which has the advantage of expressing in very high quantities and it’s very stable. Together with out collaborator Louise Gourlay in Milan, we have also successfully crystallised the structure and provided very useful insight into the quaternary structure of such enzyme. The tetrameter could be further stabilised by introducing strategic cysteine residues to enable the formation of intra-subunit disulfur bridges.

This work was carried out in collaboration with Johnson Matthey who provided great support throughout the project.

The paper can be found here







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