Ferredoxins as interchangeable redox components in support of MiaB, a radical S‐adenosylmethionine methylthiotransferase
Sign Up to like & getrecommendations! Published in 2019 at "Protein Science"
DOI: 10.1002/pro.3548
Abstract: MiaB is a member of the methylthiotransferase subclass of the radical S‐adenosylmethionine (SAM) superfamily of enzymes, catalyzing the methylthiolation of C2 of adenosines bearing an N6‐isopentenyl (i6A) group found at position 37 in several tRNAs… read more here.
Keywords: ferredoxins interchangeable; radical adenosylmethionine; methylthiotransferase; interchangeable redox ... See more keywords
Paramagnetic 1H NMR Spectroscopy to Investigate the Catalytic Mechanism of Radical S-Adenosylmethionine Enzymes.
Sign Up to like & getrecommendations! Published in 2019 at "Journal of molecular biology"
DOI: 10.1016/j.jmb.2019.08.018
Abstract: Iron-sulfur clusters in radical S-adenosylmethionine (SAM) enzymes catalyze an astonishing array of complex and chemically challenging reactions across all domains of life. Here we showed that 1H NMR spectroscopy experiments tailored to reveal hyperfine-shifted signals… read more here.
Keywords: radical adenosylmethionine; nmr spectroscopy; sam; mechanism radical ... See more keywords
NosN, a Radical S-Adenosylmethionine Methylase, Catalyzes Both C1 Transfer and Formation of the Ester Linkage of the Side-Ring System during the Biosynthesis of Nosiheptide.
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DOI: 10.1021/jacs.7b08492
Abstract: Nosiheptide, a member of the e series of macrocyclic thiopeptide natural products, contains a side-ring system composed of a 3,4-dimethylindolic acid (DMIA) moiety connected to Glu6 and Cys8 of the thiopeptide backbone via ester and… read more here.
Keywords: radical adenosylmethionine; catalyzes transfer; ester; methylase catalyzes ... See more keywords