Front cover
Front cover
Metalloenzymes in natural product biosynthetic pathways
The Natural Product Reports themed issue on ‘Metalloenzymes in natural product biosynthetic pathways’ is introduced by the Guest Editors, Katherine Ryan and Catherine Drennan.
Following the electrons: peculiarities in the catalytic cycles of radical SAM enzymes
Electrons do not always go where you expect them to in the catalytic cycles of radical SAM enzymes. Herein, a number of examples are considered along with potential avenues for future investigation.
Cobalamin-dependent radical S-adenosyl-L-methionine enzymes in natural product biosynthesis
This highlight examines the functions of cobalamin-dependent radical S-adenosyl-L-methionine enzymes that catalyse chemically-challenging reactions in several bacterial natural product biosynthetic pathways.
Expanding the roles for 2-oxoglutarate-dependent oxygenases in plant metabolism
This review of 2-oxoglutarate-dependent oxygenases and other oxidases involved in plant metabolism provides a framework for continued enzyme discovery.
Rieske non-heme iron-dependent oxygenases catalyse diverse reactions in natural product biosynthesis
The role played by Rieske non-heme iron-dependent oxygenases in natural product biosyntheses is reviewed, with particular focus on experimentally characterised examples.
Review Article
Metabolic functions of the human gut microbiota: the role of metalloenzymes
Metalloenzymes play central roles in metabolic functions of the human gut microbiota that are associated with host health and disease.
Recent examples of α-ketoglutarate-dependent mononuclear non-haem iron enzymes in natural product biosyntheses
Proximal- and distal-type αKG binding to the Fe(II) centre might play a crucial role in fine-tuning the catalysis of αKG-dependent non-haem iron enzymes.
Review Article
Roles of 2-oxoglutarate oxygenases and isopenicillin N synthase in β-lactam biosynthesis
The 2OG oxygenases and IPNS contribute to the great structural diversity of β-lactam natural products, employing some remarkable mechanisms.
Review Article
Unrivalled diversity: the many roles and reactions of bacterial cytochromes P450 in secondary metabolism
This review highlights the scope of chemical transformations that cytochrome P450 enzymes catalyse within bacterial secondary metabolism.
C–C bond forming radical SAM enzymes involved in the construction of carbon skeletons of cofactors and natural products
An emerging group of radical SAM enzymes that catalyze C–C bond formations in natural product and cofactor biosynthesis are discussed.
Diiron monooxygenases in natural product biosynthesis
Two new families of diiron cluster-containing oxygenases serve as tailoring enzymes for NRPS and PKS biosynthetic systems.
Unique chemistry of non-heme iron enzymes in fungal biosynthetic pathways
Reactions by non-heme iron enzymes in structurally intriguing fungal natural products pathways are summarized and discussed.
Cytochromes P450 for natural product biosynthesis in Streptomyces: sequence, structure, and function
This review catalogues functionally characterized P450s from Streptomyces and discusses their sequences, structures, and functions in natural products biosynthesis.
About this collection
Natural Product Reports is delighted to present a themed issue dedicated to the role of metal-containing enzymes in natural product biosynthetic pathways, Guest Edited by Professors Catherine Drennan (MIT) and Katherine Ryan (The University of British Columbia).
Metal-containing enzymes are critical for catalysing challenging chemical transformations needed to build up structurally diverse natural products. In this themed issue, we will highlight the major classes of metalloenzymes that are used in natural products biosynthesis, including cytochrome P450s, radical SAM-dependent enzymes, and iron(II) α-keto-glutarate-dependent enzymes. These reviews discuss these enzymes in the context of pathways found in bacteria, fungi, and plants. The reviews also discuss the data key to unveiling the mechanisms of these enzymes and efforts to expand the chemistry of metalloenzymes from natural product biosynthesis using engineering approaches.