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Recent advances in radical SAM enzymology: new structures and mechanisms.
Wang, Jiarui; Woldring, Rory P; Román-Meléndez, Gabriel D; McClain, Alan M; Alzua, Brian R; Marsh, E Neil G.
Afiliação
  • Wang J; Department of Chemistry, University of Michigan , Ann Arbor, Michigan 48109, United States.
ACS Chem Biol ; 9(9): 1929-38, 2014 Sep 19.
Article em En | MEDLINE | ID: mdl-25009947
The radical S-adenosylmethionine (SAM) superfamily of enzymes catalyzes an amazingly diverse variety of reactions ranging from simple hydrogen abstraction to complicated multistep rearrangements and insertions. The reactions they catalyze are important for a broad range of biological functions, including cofactor and natural product biosynthesis, DNA repair, and tRNA modification. Generally conserved features of the radical SAM superfamily include a CX3CX2C motif that binds an [Fe4S4] cluster essential for the reductive cleavage of SAM. Here, we review recent advances in our understanding of the structure and mechanisms of these enzymes that, in some cases, have overturned widely accepted mechanisms.
Assuntos

Texto completo: 1 Base de dados: MEDLINE Assunto principal: S-Adenosilmetionina / Enzimas Idioma: En Ano de publicação: 2014 Tipo de documento: Article

Texto completo: 1 Base de dados: MEDLINE Assunto principal: S-Adenosilmetionina / Enzimas Idioma: En Ano de publicação: 2014 Tipo de documento: Article