Open AccessJourney on the Radical SAM Road as an Accidental Pilgrim
Author(s) -
Vahe Bandarian
Publication year - 2022
Publication title -
acs bio and med chem au
Language(s) - English
Resource type - Journals
ISSN - 2694-2437
DOI - 10.1021/acsbiomedchemau.1c00059
Subject(s) - cleave , chemistry , catalytic cycle , pilgrim , substrate (aquarium) , catalysis , enzyme , stereochemistry , combinatorial chemistry , nanotechnology , biochemistry , biology , materials science , philosophy , ecology , theology
Radical S -adenosyl-l-methionine (SAM) enzymes catalyze a diverse group of complex transformations in all aspects of cellular physiology. These metalloenzymes bind SAM to a 4Fe-4S cluster and reductively cleave SAM to generate a 5'-deoxyadenosyl radical, which generally initiates the catalytic cycle by catalyzing a H atom to activate the substrate for subsequent chemistry. This perspective will focus on our discovery of several members of this superfamily of enzymes, with a particular emphasis on the current state of the field, challenges, and outlook.