Issue 81, 2024

A closer look at molecular mechanisms underlying inhibition of S-adenosyl-l-homocysteine hydrolase by transition metal cations

Abstract

We report biochemical and structural studies on inhibiting bacterial S-adenosyl-L-homocysteine hydrolase by transition metal cations. Our results revealed diverse molecular mechanisms of enzyme inactivation. Depending on the cation, the mechanism is based on arresting the enzyme in its closed, inactive conformation, disulfide bond formation within the active site or oxidation of the intermediate form of a cofactor.

Graphical abstract: A closer look at molecular mechanisms underlying inhibition of S-adenosyl-l-homocysteine hydrolase by transition metal cations

Supplementary files

Article information

Article type
Communication
Submitted
28 Jan 2024
Accepted
14 Pha 2024
First published
16 Pha 2024

Chem. Commun., 2024,60, 11504-11507

A closer look at molecular mechanisms underlying inhibition of S-adenosyl-L-homocysteine hydrolase by transition metal cations

M. Gawel, P. H. Malecki, J. Sliwiak, M. Stepniewska, B. Imiolczyk, J. Czyrko-Horczak, D. Jakubczyk, Ł. Marczak, M. E. Plonska-Brzezinska and K. Brzezinski, Chem. Commun., 2024, 60, 11504 DOI: 10.1039/D4CC03143A

To request permission to reproduce material from this article, please go to the Copyright Clearance Center request page.

If you are an author contributing to an RSC publication, you do not need to request permission provided correct acknowledgement is given.

If you are the author of this article, you do not need to request permission to reproduce figures and diagrams provided correct acknowledgement is given. If you want to reproduce the whole article in a third-party publication (excluding your thesis/dissertation for which permission is not required) please go to the Copyright Clearance Center request page.

Read more about how to correctly acknowledge RSC content.

Social activity

Spotlight

Advertisements