A tandem enzymatic sp2-C-methylation process: coupling in situ S-adenosyl-L-methionine formation with methyl transfer

Joanna C Sadler, Luke D Humphreys, Glenn Burley, Radka Snajdrova

Research output: Contribution to journalArticle

6 Citations (Scopus)

Abstract

A one-pot, two-step biocatalytic platform for the regiospecfic C-methylation and C-ethylation of aromatic substrates is described. The tandem process utilizes SalL (Salinospora tropica) for in situ synthesis of S-adenosyl-L-methionine (SAM), followed by alkylation of aromatic substrates using the C-methyltransferase NovO (Streptomyces spheroides). Application of this methodology is demonstrated by the regiospecific labelling of aromatic substrates via the transfer of methyl, ethyl and isotopically-labelled 13CH3, 13CD3 and CD3 groups from their corresponding SAM analogues formed in situ.
LanguageEnglish
JournalChembiochem
Early online date31 Mar 2017
DOIs
Publication statusE-pub ahead of print - 31 Mar 2017

Fingerprint

S-Adenosylmethionine
Methylation
Methyltransferases
Alkylation
Streptomyces
Substrates
Labeling

Keywords

  • methyltransferase
  • alkylation
  • biocatalytic
  • S-adenosylmethionine
  • multi-enzyme reaction

Cite this

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abstract = "A one-pot, two-step biocatalytic platform for the regiospecfic C-methylation and C-ethylation of aromatic substrates is described. The tandem process utilizes SalL (Salinospora tropica) for in situ synthesis of S-adenosyl-L-methionine (SAM), followed by alkylation of aromatic substrates using the C-methyltransferase NovO (Streptomyces spheroides). Application of this methodology is demonstrated by the regiospecific labelling of aromatic substrates via the transfer of methyl, ethyl and isotopically-labelled 13CH3, 13CD3 and CD3 groups from their corresponding SAM analogues formed in situ.",
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A tandem enzymatic sp2-C-methylation process : coupling in situ S-adenosyl-L-methionine formation with methyl transfer. / Sadler, Joanna C; Humphreys, Luke D; Burley, Glenn; Snajdrova, Radka .

In: Chembiochem, 31.03.2017.

Research output: Contribution to journalArticle

TY - JOUR

T1 - A tandem enzymatic sp2-C-methylation process

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AU - Sadler, Joanna C

AU - Humphreys, Luke D

AU - Burley, Glenn

AU - Snajdrova, Radka

N1 - This is the peer reviewed version of the following article: Sadler, J. C., Humphreys, L. D., Burley, G., & Snajdrova, R. (2017). A tandem enzymatic sp2-C-methylation process: coupling in situ S-adenosyl-L-methionine formation with methyl transfer. Chembiochem, which has been published in final form at https://doi.org/10.1002/cbic.201700115. This article may be used for non-commercial purposes in accordance with Wiley Terms and Conditions for Self-Archiving.

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N2 - A one-pot, two-step biocatalytic platform for the regiospecfic C-methylation and C-ethylation of aromatic substrates is described. The tandem process utilizes SalL (Salinospora tropica) for in situ synthesis of S-adenosyl-L-methionine (SAM), followed by alkylation of aromatic substrates using the C-methyltransferase NovO (Streptomyces spheroides). Application of this methodology is demonstrated by the regiospecific labelling of aromatic substrates via the transfer of methyl, ethyl and isotopically-labelled 13CH3, 13CD3 and CD3 groups from their corresponding SAM analogues formed in situ.

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KW - alkylation

KW - biocatalytic

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KW - multi-enzyme reaction

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