Glycyl radical activating enzymes: structure, mechanism, and substrate interactions.
The glycyl radical enzyme activating enzymes (GRE-AEs) are a group of enzymes that belong to the radical S-adenosylmethionine (SAM) superfamily and utilize a [4Fe-4S] cluster and SAM to catalyze H-atom abstraction from their substrate proteins. GRE-AEs activate homodimeric proteins known as glycyl radical enzymes (GREs) through the production of a glycyl radical. After activation, these GREs catalyze diverse reactions through the production of their own substrate radicals. The GRE-AE pyruvate formate lyase activating enzyme (PFL-AE) is extensively characterized and has provided insights into the active site structure of radical SAM enzymes including GRE-AEs, illustrating the nature of the interactions with their corresponding substrate GREs and external electron donors. This review will highlight research on PFL-AE and will also discuss a few GREs and their respective activating enzymes.
Department of Chemistry & Biochemistry and the Astrobiology Biogeocatalysis Research Center, Montana State University, Bozeman, MT 59717, United States.
Krista A
KA
Shisler
Department of Chemistry & Biochemistry and the Astrobiology Biogeocatalysis Research Center, Montana State University, Bozeman, MT 59717, United States. Electronic address: jbroderick@chemistry.montana.edu.
Joan B
JB
Broderick
D000123:Acetyltransferases; D004798:Enzymes / Q000737:chemistry* / Q000378:metabolism*; D011485:Protein Binding
D004798:Enzymes; D000123:Acetyltransferases; C040285:pyruvate formate-lyase activating enzyme
Glycyl radical enzyme (GRE); Glycyl radical enzyme activating enzyme (GRE–AE); Pyruvate formate lyase activating enzyme (PFL-AE); Radical S-adenosylmethionine (SAM) enzyme