Article
Biochemistry & Molecular Biology
Anthony P. Young, Vahe Bandarian
Summary: This study investigates the role of the enzyme TYW1 in catalyzing the oxidative cleavage of the C-1-C-2 bond of pyruvate and determining the fate of C-1 in the process. The findings suggest a new role for the auxiliary cluster in TYW1 and shed light on the preference for transforming CO2 over formate to oxaloacetate (OAA) in the catalytic cycle.
Article
Plant Sciences
Raquel Martins-Noguerol, Sebastien Acket, M. Adrian Troncoso-Ponce, Rafael Garces, Brigitte Thomasset, Monica Venegas-Caleron, Joaquin J. Salas, Enrique Martinez-Force, Antonio J. Moreno-Perez
Summary: In this study, the sunflower L1P1 and L1P2 genes were successfully isolated, sequenced, cloned, and characterized, with their expression in different tissues and impact on fatty acid and glycerolipid composition evaluated. Lipidomic studies in Arabidopsis revealed lipid remodeling in lines overexpressing these enzymes, indicating the potential regulatory role of these sunflower proteins on lipid metabolism.
FRONTIERS IN PLANT SCIENCE
(2021)
Article
Chemistry, Multidisciplinary
Patrick H. Donnan, Steven O. Mansoorabadi
Summary: A study using density functional theory evaluated several structural models of Omega and found that the proposed organometallic structure is inconsistent with experimental results. Instead, a near-attack conformer of SAM bound to the [4Fe-4S] cluster was found to be more consistent with experimental results, suggesting a new understanding of the structure of the ubiquitous Omega intermediate and the mechanism of SAM cleavage by members of the radical SAM superfamily.
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
(2022)
Review
Biochemistry & Molecular Biology
Andreas Kirschning
Summary: This report provides a comprehensive approach to understanding the evolution of coenzyme biosynthetic pathways. The analysis of various pathways reveals that coenzymes requiring a large number of coenzyme-mediated reactions likely appeared later in biological evolution, while the biosyntheses of pyridoxal phosphate (PLP) and nicotinamide (NAD(+)) are ancient pathways that require little additional coenzymatic support.
NATURAL PRODUCT REPORTS
(2022)
Article
Multidisciplinary Sciences
Wen Fang, Liu Jiang, Yibing Zhu, Sen Yang, Hong Qiu, Jiou Cheng, Qingxi Liang, Zong-cai Tu, Cunqi Ye
Summary: Methionine restriction (MR) provides metabolic benefits in many organisms. Here, the authors report that MR is sensed by yeast mitochondria as a sign of SAM deprivation; in response, the mitochondria redirect carbon metabolism to fuel nitrogen anabolism in a lipoate-dependent mechanism.
NATURE COMMUNICATIONS
(2023)
Article
Multidisciplinary Sciences
Cameron D. Fyfe, Noelia Bernardo-Garcia, Laura Fradale, Stephane Grimaldi, Alain Guillot, Clemence Brewee, Leonard M. G. Chavas, Pierre Legrand, Alhosna Benjdia, Olivier Berteau
Summary: Methyl-coenzyme M reductase plays a central role in regulating global methane levels. The study of Methanosarcina acetivorans' Mmp10 provides insights into its unique enzyme structure and catalytic control mechanism, as well as the structural changes prior to catalysis. This research is important for understanding the catalytic mechanism of the emerging superfamily of B-12-dependent radical SAM enzymes.
Article
Chemistry, Multidisciplinary
Feryel Soualmia, Alain Guillot, Nazarii Sabat, Clemence Brewee, Xavier Kubiak, Michael Haumann, Xavier Guinchard, Alhosna Benjdia, Olivier Berteau
Summary: B-12-dependent radical SAM enzyme TsrM has been found to catalyze both C- and N-methyl transfer reactions, and has the unique ability to directly transfer a methyl group to the benzyl core of tryptophan.
CHEMISTRY-A EUROPEAN JOURNAL
(2022)
Review
Biochemistry & Molecular Biology
Brian M. Hoffman, William E. Broderick, Joan B. Broderick
Summary: Radical S-adenosylmethionine (SAM) enzymes use a [4Fe-4S] cluster and SAM to initiate radical reactions, leading to the liberation of the 5'-deoxyadenosyl (5'-dAdo) radical. They form the largest enzyme superfamily with over 700,000 unique sequences. The diverse range of reactions catalyzed by these enzymes is remarkable, and the review focuses on their common radical initiation mechanism, involving an organometallic intermediate called Omega.
ANNUAL REVIEW OF BIOCHEMISTRY
(2023)
Article
Chemistry, Multidisciplinary
Leon P. Jenner, Mickael Cherrier, Patricia Amara, Luis M. Rubio, Yvain Nicolet
Summary: The nitrogenase MoFe protein contains two different FeS centers, the P-cluster and the iron-molybdenum cofactor (FeMo-co). NifB is an important enzyme in FeMo-co assembly. Recent crystal structures of NifB proteins show the plasticity of the protein and suggest how ligand reorganization would accommodate cluster loading and fusion in the time-course of NifB-co synthesis.
Review
Plant Sciences
Luca Pedroletti, Anna Moseler, Andreas J. Meyer
Summary: Significant efforts have been made to examine the nature of the autonomous iron-sulfur (Fe-S) cluster assembly machinery in mitochondria. The synthesis and assembly of Fe-S clusters occur in two distinct steps, but the transfer and distribution among their respective apoproteins are still not well understood. This review explores the mitochondrial assembly machinery of Arabidopsis and highlights the demand for cluster replenishment and the essential salvage pathway in plant mitochondria.
JOURNAL OF EXPERIMENTAL BOTANY
(2023)
Article
Chemistry, Multidisciplinary
Jinduo Cheng, Wenjuan Ji, Suze Ma, Xinjian Ji, Zixin Deng, Wei Ding, Qi Zhang
Summary: The study characterizes ArsS as a DDMAA synthase, revealing a key step in arsenosugar biosynthesis. Phylogenomic and biochemical analyses show that DDMAA synthases are widely distributed in different bacterial phyla, likely originating from cyanobacteria. This highlights the catalytic diversity of radical SAM enzymes.
ANGEWANDTE CHEMIE-INTERNATIONAL EDITION
(2021)
Article
Biotechnology & Applied Microbiology
David Lennox-Hvenekilde, Anne P. Bali, Luisa S. Gronenberg, Carlos Acevedo-Rocha, Morten O. A. Sommer, Hans J. Genee
Summary: Researchers have successfully engineered a cell factory to produce L-Lipoic acid (LA) from glucose in Escherichia coli. The optimized strain achieved a high yield of free LA by carefully balancing the expression of toxic enzymes and optimizing translation initiation rates. This study provides valuable insights for designing and balancing biosynthetic pathways containing toxic enzymes and protein-bound intermediates.
METABOLIC ENGINEERING
(2023)
Review
Biochemistry & Molecular Biology
Christopher T. Walsh
Summary: This article discusses the chemical strategies employed by enzymes in the maturation of scaffolds, including nonoxidative tailoring enzymes and oxidative tailoring enzymes. Nonoxidative tailoring enzymes modify scaffolds by transferring electrophilic fragments and functional groups, while oxidative tailoring enzymes rely on oxygen to generate reactive species for scaffold modification.
NATURAL PRODUCT REPORTS
(2023)
Review
Biochemistry & Molecular Biology
Joan B. Broderick, William E. Broderick, Brian M. Hoffman
Summary: Enzymes that use radical SAM reaction pathway are the largest enzyme superfamily and play a critical role in performing diverse transformations. Recent studies have revealed the mechanism of liberating the 5'-dAdo· radical through Fe-C5' bond homolysis. The presence and catalytic activity of 5'-dAdo· in radical SAM enzymes have been confirmed. The simplicity of SAM as a radical precursor and the precise control of 5'-dAdo· reactivity contribute to the pervasiveness of radical SAM enzymes in the tree of life.
Article
Chemistry, Multidisciplinary
Juneina Omeiri, Lydie Martin, Anthony Usclat, Mickael V. Cherrier, Yvain Nicolet
Summary: [FeFe]-hydrogenases efficiently catalyze the reversible oxidation of molecular hydrogen, thanks to the intricate H-cluster in their active site. The synthesis of this active site involves the assembly of multiple proteins. Despite the instability of complex B, a biomimetic analogue has been used to study its structure. By encapsulating and stabilizing the complex B product generated by HydG, the structure of complex B has been successfully determined, highlighting the transient interaction between HydG and HydE.
ANGEWANDTE CHEMIE-INTERNATIONAL EDITION
(2023)