At the confluence of ribosomally synthesized peptide modification and radical S-adenosylmethionine (SAM) enzymology.
J Biol Chem
; 292(40): 16397-16405, 2017 10 06.
Article
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| MEDLINE
| ID: mdl-28830931
ABSTRACT
Radical S-adenosylmethionine (RS) enzymology has emerged as a major biochemical strategy for the homolytic cleavage of unactivated C-H bonds. At the same time, the post-translational modification of ribosomally synthesized peptides is a rapidly expanding area of investigation. We discuss the functional cross-section of these two disciplines, highlighting the recently uncovered importance of protein-protein interactions, especially between the peptide substrate and its chaperone, which functions either as a stand-alone protein or as an N-terminal fusion to the respective RS enzyme. The need for further work on this class of enzymes is emphasized, given the poorly understood roles performed by multiple, auxiliary iron-sulfur clusters and the paucity of protein X-ray structural data.
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1
Banco de datos:
MEDLINE
Asunto principal:
S-Adenosilmetionina
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Procesamiento Proteico-Postraduccional
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Chaperonas Moleculares
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Proteínas Hierro-Azufre
Idioma:
En
Año:
2017
Tipo del documento:
Article