Michael K. F. Mohr

This study investigates the ability of SAM-dependent enzymes to accept D-SAM instead of L-SAM, finding that several enzymes can utilize D-SAM and highlighting implications for enzyme engineering.

This study identifies SAM hydrolases in thermophilic archaea that counteract sulfonium epimerisation, maintaining metabolic stability by degrading inactive (RS,SC)-SAM.

This paper demonstrates the efficient conversion of formate into methyl groups in engineered Escherichia coli using SAM-dependent methyltransferases, achieving over 70% formate-derived methyl groups.