A Flavoprotein Dioxygenase Steers Bacterial Tropone Biosynthesis via Coenzyme A-Ester Oxygenolysis and Ring Epoxidation.
Ying Duan,Marina Toplak,Anwei Hou,Nelson L. Brock,Jeroen S. Dickschat,Jeroen S. Dickschat,Robin Teufel +6 more
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TLDR
In this article, the authors showed that the bacterial tropone natural products such as tropolone, tropodithietic acid, or roseobacticides play crucial roles in various terrestrial and marine symbiotic interactions as virulence factors.Abstract:
Bacterial tropone natural products such as tropolone, tropodithietic acid, or the roseobacticides play crucial roles in various terrestrial and marine symbiotic interactions as virulence factors, antibiotics, algaecides, or quorum sensing signals. We now show that their poorly understood biosynthesis depends on a shunt product from aerobic CoA-dependent phenylacetic acid catabolism that is salvaged by the dedicated acyl-CoA dehydrogenase-like flavoenzyme TdaE. Further characterization of TdaE revealed an unanticipated complex catalysis, comprising substrate dehydrogenation, noncanonical CoA-ester oxygenolysis, and final ring epoxidation. The enzyme thereby functions as an archetypal flavoprotein dioxygenase that incorporates both oxygen atoms from O2 into the substrate, most likely involving flavin-N5-peroxide and flavin-N5-oxide species for consecutive CoA-ester cleavage and epoxidation, respectively. The subsequent spontaneous decarboxylation of the reactive enzyme product yields tropolone, which serves as a key virulence factor in rice panicle blight caused by pathogenic edaphic Burkholderia plantarii. Alternatively, the TdaE product is most likely converted to more complex sulfur-containing secondary metabolites such as tropodithietic acid from predominant marine Rhodobacteraceae (e.g., Phaeobacter inhibens).read more
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Role is in the eye of the beholder—the multiple functions of the antibacterial compound tropodithietic acid produced by marine Rhodobacteraceae
Nathalie N. S. E. Henriksen,L. L. Lindqvist,Mario Wibowo,Eva C. Sonnenschein,Mikkel Bentzon-Tilia,Lone Gram +5 more
TL;DR: The current understanding of the chemical ecology of T DA, including the environmental niches of TDA-producing bacteria, and the molecular mechanisms governing the function and regulation of Tda are summarized.
Journal ArticleDOI
OUP accepted manuscript
TL;DR: The tropone derivative tropodithietic acid (TDA) is a broad spectrum antimicrobial compound produced by several members of the Rhodobacteraceae family, a major marine bacterial lineage, within the genera Phaeobacter, Tritonibacter, and Pseudovibrio as mentioned in this paper .
Journal ArticleDOI
Catalytic Control of Spiroketal Formation in Rubromycin Polyketide Biosynthesis
TL;DR: In this article, the authors provide structural and mechanistic insights into the control of catalysis by a spiroketal synthase, which fulfills several important functions as reductase, monooxygenase, and presumably oxidase.
Journal ArticleDOI
Bacterial flavoprotein monooxygenase YxeK salvages toxic S-(2-succino)-adducts via oxygenolytic C-S bond cleavage
Arne Matthews,Julia Schönfelder,Simon Lagies,Erik Schleicher,Bernd Kammerer,Holly R. Ellis,Frederick Stull,Robin Teufel +7 more
TL;DR: In this paper, the role of the predicted flavoprotein monooxygenase YxeK in S-(2-succino)-adduct detoxification and sulfur metabolism was investigated.
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An acetyltransferase controls the metabolic flux in rubromycin polyketide biosynthesis by direct modulation of redox tailoring enzymes
TL;DR: A novel regulatory principle for natural products involving a dedicated acetyltransferase, which modifies a redox-tailoring enzyme and thereby enables pathway furcation and alternating pharmacophore assembly in rubromycin polyketide biosynthesis is reported.
References
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Journal ArticleDOI
Flavin dependent monooxygenases.
Mieke M.E. Huijbers,S. Montersino,Adrie H. Westphal,Dirk Tischler,Dirk Tischler,Willem J. H. van Berkel +5 more
TL;DR: An update of the classification of flavin-dependent monooxygenases is presented and the latest advances in the understanding of their catalytic and structural properties are summarized.
Journal ArticleDOI
The Jekyll-and-Hyde chemistry of Phaeobacter gallaeciensis
TL;DR: It is shown that P. gallaeciensis switches its secreted small molecule metabolism to the production of potent and selective algaecides, the roseobacticides, in response to p-coumaric acid, an algal lignin breakdown product that is symptomatic of aging algae.
Journal ArticleDOI
Bacterial phenylalanine and phenylacetate catabolic pathway revealed
Robin Teufel,Victoria Mascaraque,Wael Ismail,M. Voss,Julián Perera,Wolfgang Eisenreich,Wolfgang Haehnel,Georg Fuchs +7 more
TL;DR: This work elucidates the catabolic pathway functioning in 16% of all bacteria whose genome has been sequenced, including Escherichia coli and Pseudomonas putida, and provides insight into the natural remediation of man-made environmental contaminants such as styrene.
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Same Substrate, Many Reactions: Oxygen Activation in Flavoenzymes
TL;DR: The state of the art on a key area of research in flavin enzymology: the molecular basis for the activation of O2 by flavin-dependent oxidases and monooxygenases is summarized.
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Purification and biochemical characterization of phenylacetyl-CoA ligase from Pseudomonas putida. A specific enzyme for the catabolism of phenylacetic acid.
TL;DR: PA-CoA ligase was specifically induced by PAA when P. putida was grown in a chemically defined medium in which phenylacetic acid was the sole carbon source, suggesting that PA-Coa ligase is a specific enzyme involved in the utilization of PAA as energy source.