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

Elnaz Jalali; Jon S. Thorson

doi:10.1016/j.copbio.2021.02.010

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

Elnaz Jalali, Jon S. Thorson

Research output: Contribution to journal › Review article › peer-review

12 Scopus citations

Abstract

Transferases have emerged as among the best catalysts for enzyme-mediated bioorthogonal functional group installation to advance innovative in vitro, cell-based and in vivo chemical biology applications. This review introduces the key considerations for selecting enzyme catalysts and chemoselective reactions most amenable to bioorthogonal platform development and highlights relevant key technology development and applications for one ubiquitous transferase subclass — methyltransferases (MTs). Within this context, recent advances in MT-enabled bioorthogonal labeling/conjugation relevant to DNA, RNA, protein, and natural products (i.e. complex small molecule metabolites) are highlighted.

Original language	English
Pages (from-to)	290-298
Number of pages	9
Journal	Current Opinion in Biotechnology
Volume	69
DOIs	https://doi.org/10.1016/j.copbio.2021.02.010
State	Published - Jun 2021

Bibliographical note

Publisher Copyright:
© 2021 Elsevier Ltd

Funding

We gratefully acknowledge the support of R37 AI52218, R01 GM115261, the Center of Biomedical Research Excellence (COBRE) in Pharmaceutical Research and Innovation (CPRI, N.I.H.P20 GM130456), the University of Kentucky College of Pharmacy and the National Center for Advancing Translational Sciences (UL1TR000117 and UL1TR001998). We gratefully acknowledge the support of R37 AI52218 , R01 GM115261 , the Center of Biomedical Research Excellence (COBRE) in Pharmaceutical Research and Innovation ( CPRI , N.I.H. P20 GM130456 ), the U niversity of Kentucky College of Pharmacy and the National Center for Advancing Translational Sciences ( UL1TR000117 and UL1TR001998 ).

Funders	Funder number
Center of Biomedical Research Excellence	N.I.H.P20 GM130456
N.I.H.	P20 GM130456
Center for Pharmaceutical Research and Innovation
University of Kentucky College of Pharmacy
National Center for Advancing Translational Sciences (NCATS)	UL1TR001998, UL1TR000117
Central Power Research Institute

ASJC Scopus subject areas

Biotechnology
Bioengineering
Biomedical Engineering

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10.1016/j.copbio.2021.02.010

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abstract = "Transferases have emerged as among the best catalysts for enzyme-mediated bioorthogonal functional group installation to advance innovative in vitro, cell-based and in vivo chemical biology applications. This review introduces the key considerations for selecting enzyme catalysts and chemoselective reactions most amenable to bioorthogonal platform development and highlights relevant key technology development and applications for one ubiquitous transferase subclass — methyltransferases (MTs). Within this context, recent advances in MT-enabled bioorthogonal labeling/conjugation relevant to DNA, RNA, protein, and natural products (i.e. complex small molecule metabolites) are highlighted.",

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year = "2021",

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AU - Thorson, Jon S.

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AB - Transferases have emerged as among the best catalysts for enzyme-mediated bioorthogonal functional group installation to advance innovative in vitro, cell-based and in vivo chemical biology applications. This review introduces the key considerations for selecting enzyme catalysts and chemoselective reactions most amenable to bioorthogonal platform development and highlights relevant key technology development and applications for one ubiquitous transferase subclass — methyltransferases (MTs). Within this context, recent advances in MT-enabled bioorthogonal labeling/conjugation relevant to DNA, RNA, protein, and natural products (i.e. complex small molecule metabolites) are highlighted.

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JO - Current Opinion in Biotechnology

JF - Current Opinion in Biotechnology

ER -

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

Abstract

Bibliographical note

Funding

ASJC Scopus subject areas

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