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Project 1 Jun.-Prof. Jennifer Andexer

SAM–dependent methyltransferases in chemical synthesis

Biocatalytic methylation is an interesting option for technical applications, as methyl transferases catalyse the methylation of a wide range of compounds in a region- and stereospecific manner. There are, however, two major drawbacks: the instability and high price of the cofactor S-adenosylmethionine (SAM) and the fact that most methyl transferases suffer from product inhibition by the SAM-derived by-product S-adenosylhomocysteine (SAH). The project described aims at integrating the methyltransferase in an enzyme cascade where SAM is supplied and SAH removed in situ. In the next step, this cascade will be adapted to the use of SAM-derivatives such as the corresponding ethyl or allyl compounds to extend the applicability of the system for further alkylations.


Figure 1: Overview of the enzyme cascade. I. MAT, II. MT, III. SAH–degrading enzyme.



Jun.-Prof. Dr. Jennifer Andexer

Institute of Pharmaceutical Sciences

Pharmaceutical and Medicinal Chemistry

Albertstr. 25

79104 Freiburg

Phone: +49 (0) 761 203-67398

Fax: +49 (0) 761 203-6351

email: jennifer.andexer@pharmazie.uni-freiburg.de

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