Kinetic and catalytic features of N-myristoyltransferases

Frédéric Rivière; Paul Monassa; Carmela Giglione; Thierry Meinnel

doi:10.1016/bs.mie.2023.02.018

Kinetic and catalytic features of N-myristoyltransferases

Methods Enzymol. 2023:684:167-190. doi: 10.1016/bs.mie.2023.02.018. Epub 2023 Mar 21.

Authors

Frédéric Rivière¹, Paul Monassa¹, Carmela Giglione², Thierry Meinnel³

Affiliations

¹ Université Paris-Saclay, CEA, CNRS, Institute for Integrative Biology of the Cell (I2BC), Gif-sur-Yvette cedex, France.
² Université Paris-Saclay, CEA, CNRS, Institute for Integrative Biology of the Cell (I2BC), Gif-sur-Yvette cedex, France. Electronic address: carmela.giglione@i2bc.paris-saclay.fr.
³ Université Paris-Saclay, CEA, CNRS, Institute for Integrative Biology of the Cell (I2BC), Gif-sur-Yvette cedex, France. Electronic address: thierry.meinnel@i2bc.paris-saclay.fr.

PMID: 37230588
DOI: 10.1016/bs.mie.2023.02.018

Abstract

N-myristoyltransferases (NMTs) are members of the large family of GCN5-related N-acetyltransferases (GNATs). NMTs mainly catalyze eukaryotic protein myristoylation, an essential modification tagging protein N-termini and allowing successive subcellular membrane targeting. NMTs use myristoyl-CoA (C14:0) as major acyl donor. NMTs were recently found to react with unexpected substrates including lysine side-chains and acetyl-CoA. This chapter details the kinetic approaches that have allowed the characterization of the unique catalytic features of NMTs in vitro.

Keywords: Acetylation; Enzyme kinetics; Glycine; Lysine; Myristoylation; N-myristoyltransferase; N-terminus; Protein acylation.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Acyltransferases* / chemistry
Amino Acid Sequence

Substances

glycylpeptide N-tetradecanoyltransferase
Acyltransferases