Expressed Protein Ligation at Methionine: N‐Terminal Attachment of Homocysteine, Ligation, and Masking | Zendy

Tanaka Tomohiro | Zendy; Wagner Anne M. | Zendy; Warner John B. | Zendy; Wang Yanxin J. | Zendy; Petersson E. James | Zendy

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Expressed Protein Ligation at Methionine: N‐Terminal Attachment of Homocysteine, Ligation, and Masking

Author(s) -

Tanaka Tomohiro,

Wagner Anne M.,

Warner John B.,

Wang Yanxin J.,

Petersson E. James

Publication year - 2013

Publication title -

angewandte chemie international edition

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 5.831

H-Index - 550

eISSN - 1521-3773

pISSN - 1433-7851

DOI - 10.1002/anie.201302065

Subject(s) - ligation , homocysteine , chemical ligation , methionine , chemistry , biochemistry , microbiology and biotechnology , biology , amino acid

A useful handle : One major limitation of protein semi‐synthesis is the need for Cys at the ligation site in native chemical ligation reactions. It is shown that a transferase enzyme can deliver homocysteine to the N‐terminus of an expressed protein (see scheme). Homocysteine can be used in a ligation reaction and then converted to Met. This allows one to use the MetArg or MetLys motif as a point of disconnection in semi‐synthesis.

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