Enzyme-mediated bioorthogonal technologies: catalysts, chemoselective reactions and recent methyltransferase applications

Jalali, Elnaz; Thorson, Jon S.

doi:10.1016/j.copbio.2021.02.010

Cited by 13 publications

(14 citation statements)

References 66 publications

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“…However, bioorthogonal units with stimuli-responsiveness are rare, because they are not easily biochemically masked. Although some enzymes or light-modulated bioorthogonal reactions [128][129][130] have been realized in vitro, their in vivo applications are rarely reported. Rao et al used a reductase-responsive cyanobenzothiazole (CBT)-cysteine condensation to in situ synthesize polymers in vivo (Fig.…”

Section: Intracellular Bioorthogonal Polymerizationmentioning

confidence: 99%

Polymerization in living organisms

Lei

Zhang

et al. 2023

Chem. Soc. Rev.

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Section: Intracellular Bioorthogonal Polymerizationmentioning

confidence: 99%

Polymerization in living organisms

Lei

Zhang

et al. 2023

Chem. Soc. Rev.

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“…[2] Regioand stereoselective transfer of the methyl group onto biomolecules and small molecule substrates is catalysed by methyltransferases (MTs). [3][4][5] Due to their versatile substrate range, MTs are desired tools for biotechnology. [3,6] SAM analogues with modifications at the alkyl substituent of the sulfonium further diversify possible products that can be synthesised using wildtype MTs.…”

Section: S-adenosyl-l-methionine (Sammentioning

confidence: 99%

Enzymatic Synthesis of L-Methionine Analogues and Application in a Methyltransferase Catalysed Alkylation Cascade

Mohr

Saleem-Batcha

Cornelissen

et al. 2023

Preprint

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Chemical modification of small molecules is a key step for the development of pharmaceuticals. S-adenosyl-L-methionine (SAM) analogues are used by methyltransferases (MTs) to transfer alkyl, allyl and benzyl moieties chemo-, stereo- and regioselectively onto substrates, enabling an enzymatic way for specific derivatization of a wide range of molecules. L-Methionine analogues are required for the synthesis of SAM analogues. Most of these are not commercially available. In nature, O-acetyl-L-homoserine sulfhydrolases (OAHS) catalyse the synthesis of L methionine from O-acetyl-L-homoserine or L homocysteine, and methyl mercaptan. Here, we investigated the substrate scope of ScOAHS from Saccharomyces cerevisiae for the production of L methionine analogues from L homocysteine and organic thiols. The promiscuous enzyme was used to synthesise nine different L methionine analogues with modifications on the thioether residue up to a conversion of 75%. ScOAHS was combined with an established MT dependent three-enzyme alkylation cascade, allowing transfer of in total seven moieties onto two MT substrates. Ethylation was nearly doubled with the new four-enzyme cascade, indicating a beneficial effect of the in situ production of L methionine analogues with ScOAHS.

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“…This issue will not be discussed in depth because there is already a review on MT-mediated bio-orthogonal reactions. 83 …”

Section: Labeling Nucleic Acid Modifications With the Functional Groupmentioning

confidence: 99%

“…AdoMet analogs transferred functional groups (methyl groups or groups including vinyl, alkynyl, or azide groups) into target macromolecular substrates catalysed by methyltransferases (MTs). [83][84][85][86][87] The transferred functional groups on DNA or RNA serve as a substrate for subsequent bio-orthogonal procedures that modify fluorescent groups or other functional groups. This issue will not be discussed in depth because there is already a review on MT-mediated bio-orthogonal reactions.…”

Section: Rsc Chemical Biology Reviewmentioning

confidence: 99%