The radical SAM enzyme AlbA catalyzes thioether bond formation in subtilosin A

2012 ◽  
Vol 8 (4) ◽  
pp. 350-357 ◽  
Author(s):  
Leif Flühe ◽  
Thomas A Knappe ◽  
Michael J Gattner ◽  
Antje Schäfer ◽  
Olaf Burghaus ◽  
...  
Keyword(s):  
Bond Formation ◽  
Radical Sam ◽  
Radical Sam Enzyme

scholarly journals Thioether bond formation by SPASM domain radical SAM enzymes: Cα H-atom abstraction in subtilosin A biosynthesis

2016 ◽  
Vol 52 (37) ◽  
pp. 6249-6252 ◽  
Author(s):  
Alhosna Benjdia ◽  
Alain Guillot ◽  
Benjamin Lefranc ◽  
Hubert Vaudry ◽  
Jérôme Leprince ◽  
...  
Keyword(s):  
Bond Formation ◽  
Radical Sam ◽  
Radical Sam Enzymes ◽  
Radical Sam Enzyme ◽  
Synthetic Approaches

The radical SAM enzyme AlbA has been reported to catalyze the formation of a thioether bond in the antibiotic subtilosin A. By modeling, biochemical and synthetic approaches, we propose novel mechanistic perspectives on this emerging group of enzymes.

scholarly journals The PqqD homologous domain of the radical SAM enzyme ThnB is required for thioether bond formation during thurincin H maturation

FEBS Letters ◽  
2015 ◽  
Vol 589 (15) ◽  
pp. 1802-1806 ◽  
Author(s):  
Beata M. Wieckowski ◽  
Julian D. Hegemann ◽  
Andreas Mielcarek ◽  
Linda Boss ◽  
Olaf Burghaus ◽  
...  
Keyword(s):  
Bond Formation ◽  
Radical Sam ◽  
Radical Sam Enzyme ◽  
Thurincin H

Two [4Fe-4S] Clusters Containing Radical SAM Enzyme SkfB Catalyze Thioether Bond Formation during the Maturation of the Sporulation Killing Factor

2013 ◽  
Vol 135 (3) ◽  
pp. 959-962 ◽  
Author(s):  
Leif Flühe ◽  
Olaf Burghaus ◽  
Beata M. Wieckowski ◽  
Tobias W. Giessen ◽  
Uwe Linne ◽  
...  
Keyword(s):  
Bond Formation ◽  
Radical Sam ◽  
Radical Sam Enzyme

scholarly journals Erratum: The radical SAM enzyme AlbA catalyzes thioether bond formation in subtilosin A

2012 ◽  
Vol 8 (8) ◽  
pp. 737-737 ◽  
Author(s):  
Leif Flühe ◽  
Thomas A Knappe ◽  
Michael J Gattner ◽  
Antje Schäfer ◽  
Olaf Burghaus ◽  
...  
Keyword(s):  
Bond Formation ◽  
Radical Sam ◽  
Radical Sam Enzyme

scholarly journals Accumulation of an unprecedented 5′-deoxyadenos-4′-yl radical unmasks the kinetics of the radical-mediated C-C bond formation step in MoaA catalysis

2020 ◽  
Author(s):  
Haoran Pang ◽  
Edward A. Lilla ◽  
Pan Zhang ◽  
Du Zhang ◽  
Thomas P. Shields ◽  
...  
Keyword(s):  
Biochemical Characterization ◽  
Bond Formation ◽  
Kinetic Characterization ◽  
Amino Acid Residues ◽  
Radical Sam ◽  
Radical Sam Enzymes ◽  
Rate Acceleration ◽  
Radical Sam Enzyme ◽  
Radical Catalysis

AbstractRadical S-adenosyl-L-methionine (SAM) enzymes catalyze various free radical-mediated reactions. In these enzymes, the rate-determining SAM cleavage kinetically masks all the subsequent steps. Due to this kinetic masking, detailed mechanistic characterization of radical transformations catalyzed by these enzymes is very difficult. Here, we report a successful kinetic characterization of the radical C-C bond formation catalyzed by a MoaA radical SAM enzyme. MoaA catalyzes an unprecedented 3′,8-cyclization of GTP into 3′,8-cyclo-7,8-dihydro-GTP (3′,8-cH2GTP) during the molybdenum cofactor (Moco) biosynthesis. Through a series of EPR and biochemical characterization, we found that MoaA accumulates a 5′-deoxyadenos-4′-yl radical (5′-dA-C4′•) under the turnover conditions, and forms (4′S)-5′-deoxyadenosine ((4′S)-5′-dA), which is a C-4′ epimer of the naturally occurring (4′R)-5′-dA. Together with kinetic characterizations, these observations revealed the presence of a shunt pathway in which an on-pathway intermediate, GTP C-3′ radical, abstracts H-4′ atom from 5′-dA to transiently generate 5′-dA-C4′• that is subsequently reduced stereospecifically to yield (4′S)-5′-dA. Detailed kinetic characterization of the shunt and the main pathways provided the comprehensive view of MoaA kinetics, and determined the rate of the on-pathway 3′,8-cyclization step as 2.7 ± 0.7 s−1. Together with DFT calculations, this observation suggested that the 3′,8-cyclization is accelerated by 6 ∼ 9 orders of magnitude by MoaA. Potential contributions of the active-site amino acid residues, and their potential relationships with human Moco deficiency disease are discussed. This is the first determination of the magnitude of catalytic rate acceleration by a radical SAM enzyme, and provides the foundation for understanding how radical SAM enzymes achieve highly specific radical catalysis.

Characterization and Mechanistic Study of the Radical SAM Enzyme ArsS Involved in Arsenosugar Biosynthesis

2021 ◽  
Author(s):  
Jinduo Cheng ◽  
Wenjuan Ji ◽  
Suze Ma ◽  
Xinjian Ji ◽  
Zixin Deng ◽  
...  
Keyword(s):  
Mechanistic Study ◽  
Radical Sam ◽  
Radical Sam Enzyme

Characterization of the DNA repair spore photoproduct lyase enzyme from Clostridium acetobutylicum: A radical-SAM enzyme

2007 ◽  
Vol 10 (8) ◽  
pp. 756-765 ◽  
Author(s):  
Alexia Chandor ◽  
Thierry Douki ◽  
Didier Gasparutto ◽  
Serge Gambarelli ◽  
Yannis Sanakis ◽  
...  
Keyword(s):  
Dna Repair ◽  
Clostridium Acetobutylicum ◽  
Radical Sam ◽  
Spore Photoproduct Lyase ◽  
Radical Sam Enzyme ◽  
Spore Photoproduct
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