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Systematic exploration of enzyme substrate preferences
The growing realization that lysine methylation plays a critical role in the development of many human diseases is perhaps not a surprising one. Dysfunction in the dynamic lysine methylation network (currently consisting of >5000 different lysine methylation modifications) has been identified as a prominent contributor to the development of many different types of cancer. For example, one pivotal study unveiled that the methyltransferase SMYD3 enhances the progression of Ras-driven leukemia through the methylation of the MAP3K2 protein at lysine 260. Given the involvement of lysine methylation in a growing number of different biological processes, it is now critical that we understand how these methyltransferase function and ID the proteins that they methylate.
We use synthesize peptide arrays to ID the sequence of amino acids that are necessary for an enzyme to recognize and methylate its substrate. With this information, we can work to identify in vivo enzyme substrates to build the enzyme-substrate network and help to establish the cellular roles of methyltransferase enzymes.
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