AI Article Synopsis
- The article discusses the less-explored area of phosphoramidation, which modifies nitrogen in amino acids like His, Lys, and Arg, compared to the more common protein phosphorylation.
- Research on the enzymes responsible for creating and breaking down these phosphoramidates has been ongoing since the 1950s, but only recently have key enzymes been identified and studied effectively.
- The review focuses on summarizing what is currently known about these enzymes, including their structure, functions, and the new chemical tools developed for studying them.
Article Abstract
In contrast to well-recognized protein phosphorylation on the side-chain oxygen of Ser, Thr, or Tyr residues, analogous phosphoramidation of the nitrogen of His, Lys, and Arg side chains remains much less investigated, mainly due to the instability of post-translational modifications and technical difficulties involved in their analysis. For example, reports on the enzyme activities responsible for the formation and hydrolysis of these phosphoramidates date back to as early as the 1950s, but some of these enzymes have only recently been identified and functionally characterized; this has been aided by the development of novel research tools. In this review, we summarize current knowledge of the enzymes that hydrolyze protein N-phosphoramidates, in terms of their structure, activities, and biological functions, as well as the chemical tools used to investigate them.
Download full-text PDF |
Source |
|---|---|
| http://dx.doi.org/10.1002/cbic.201800566 | DOI Listing |
Publication Analysis
Top Keywords
Similar Publications
Want AI Summaries of new PubMed Abstracts delivered to your In-box?
Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!