Streamlined recycling of S-adenosylmethionine

Jason Micklefield

doi:10.1038/s41929-019-0323-6

Streamlined recycling of S-adenosylmethionine

Jason Micklefield^*

^*Corresponding author for this work

Research output: Contribution to journal › Article › peer-review

Abstract

S-adenosylmethionine (SAM)-dependent methyltransferase enzymes have significant synthetic potential, but their utility as biocatalysts has been limited by the availability of SAM. An elegant and simple method addressing this long-standing problem has now been developed using a halide methyltransferase (HMT) enzyme for SAM regeneration in vitro.

Original language	English
Journal	Nature Catalysis
DOIs	https://doi.org/10.1038/s41929-019-0323-6
Publication status	Published - 8 Jul 2019

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title = "Streamlined recycling of S-adenosylmethionine",

abstract = "S-adenosylmethionine (SAM)-dependent methyltransferase enzymes have significant synthetic potential, but their utility as biocatalysts has been limited by the availability of SAM. An elegant and simple method addressing this long-standing problem has now been developed using a halide methyltransferase (HMT) enzyme for SAM regeneration in vitro.",

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SN - 2520-1158

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Streamlined recycling of S-adenosylmethionine

Abstract

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