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• W2948377810 abstract "Tubulin tyrosine ligase (TTL) catalyzes the addition of tyrosine derivatives to the C-terminal carboxylic acid of proteins. The enzyme binds to a 14-amino acid recognition sequence, termed Tub-tag, and allows for the introduction of tyrosine derivatives that carry a unique chemical handle. These handles enable subsequent bioorthogonal reactions with a great variety of probes or effector molecules. Clearly, this two-step chemoenzymatic approach, facilitates the site-specific functionalization of proteins. Furthermore, due to its broad substrate tolerance, tubulin tyrosine ligase also enables an enzymatic one-step modification. For example, a coumarin amino acid was utilized to generate fluorescently labeled proteins for advanced applications in imaging and diagnostics. Here we describe the modification of proteins using TTL in detail via a one-step as well as two-step procedure and highlight its practicability for applications in imaging, diagnostics, and cell biology." @default.
• W2948377810 created "2019-06-14" @default.
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• W2948377810 date "2019-01-01" @default.
• W2948377810 modified "2023-10-14" @default.
• W2948377810 title "Tubulin Tyrosine Ligase-Mediated Modification of Proteins" @default.
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• W2948377810 doi "https://doi.org/10.1007/978-1-4939-9546-2_17" @default.
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