Biochemical genesis of enzymatic and non-enzymatic post-translational modifications

Erin Q Jennings; Kristofer S Fritz; James J Galligan

doi:10.1016/j.mam.2021.101053

Biochemical genesis of enzymatic and non-enzymatic post-translational modifications

Mol Aspects Med. 2022 Aug:86:101053. doi: 10.1016/j.mam.2021.101053. Epub 2021 Nov 24.

Authors

Erin Q Jennings¹, Kristofer S Fritz², James J Galligan³

Affiliations

¹ Department of Pharmacology and Toxicology, College of Pharmacy, University of Arizona, Tucson, AZ, 85721, USA.
² Skaggs School of Pharmacy and Pharmaceutical Sciences, University of Colorado Anschutz Medical Campus, Aurora, CO, USA.
³ Department of Pharmacology and Toxicology, College of Pharmacy, University of Arizona, Tucson, AZ, 85721, USA. Electronic address: jgalligan@pharmacy.arizona.edu.

Abstract

Post-translational modifications (PTMs) alter protein structure, function, and localization and play a pivotal role in physiological and pathophysiological conditions. Many PTMs arise from endogenous metabolic intermediates and serve as sensors for metabolic feedback to maintain cell growth and homeostasis. A key feature to PTMs is their biochemical genesis, which can result from either non-enzymatic adduction (nPTMs) or through enzyme-catalyzed reactions (ePTMs). The abundance and site-specificity of PTMs are determined by dedicated classes of enzymes that add (writers) or remove (erasers) the chemical addition. In this review we will highlight the biochemical genesis and regulation of a few of the 700+ PTMs that have been identified.

Keywords: Acylation; Glycation; Glycosylation; Glyoxalase; Metabolism; Sirtuin; Sulfenylation.

Publication types

Review
Research Support, N.I.H., Extramural
Research Support, Non-U.S. Gov't

MeSH terms

Humans
Protein Processing, Post-Translational*
Proteins*

Substances

Proteins

Abstract

Publication types

MeSH terms

Substances

Grants and funding