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 Jun 2024
Accepted
14 Aug 2024
First published
16 Aug 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

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