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Virtually all enzymes catalyse more than one reaction, a phenomenon known as enzyme promiscuity. It is unclear whether promiscuous enzymes are more often generalists that catalyse multiple reactions at similar rates or specialists that catalyse one reaction much more efficiently than other reactions. In addition, the factors that shape whether an enzyme evolves to be a generalist or a specialist are poorly understood. To address these questions, we follow a three-pronged approach. First, we examine the distribution of promiscuity in empirical enzymes reported in the BRENDA database. We find that the promiscuity distribution of empirical enzymes is bimodal. In other words, a large fraction of promiscuous enzymes are either generalists or specialists, with few intermediates. Second, we demonstrate that enzyme biophysics is not sufficient to explain this bimodal distribution. Third, we devise a constraint-based model of promiscuous enzymes undergoing duplication and facing selection pressures favouring subfunctionalization. The model posits the existence of constraints between the catalytic efficiencies of an enzyme for different reactions and is inspired by empirical case studies. The promiscuity distribution predicted by our constraint-based model is consistent with the empirical bimodal distribution. Our results suggest that subfunctionalization is possible and beneficial only in certain enzymes. Furthermore, the model predicts that conflicting constraints and selection pressures can cause promiscuous enzymes to enter a 'frustrated' state, in which competing interactions limit the specialisation of enzymes. We find that frustration can be both a driver and an inhibitor of enzyme evolution by duplication and subfunctionalization. In addition, our model predicts that frustration becomes more likely as enzymes catalyse more reactions, implying that natural selection may prefer catalytically simple enzymes. In sum, our results suggest that frustration may play an important role in enzyme evolution.
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http://dx.doi.org/10.1007/s00239-024-10161-4 | DOI Listing |
Angew Chem Int Ed Engl
September 2025
Department of Chemical and Pharmaceutical Biology, University of Groningen, Antonius Deusinglaan 1, Groningen, 9713AV, The Netherlands.
Type III polyketide synthases (T3PKSs) are enzymes that produce diverse compounds of ecological and clinical importance. While well-studied in plants, only a handful of T3PKSs from fungi have been characterised to date. Here, we developed a comprehensive workflow for kingdom-wide characterisation of T3PKSs.
View Article and Find Full Text PDFPhilos Trans R Soc Lond B Biol Sci
September 2025
Department of Biosciences, Durham University, Durham DH1 3LE, UK.
Bacteriophages (phages), viral predators of bacteria, generate selection pressure that causes bacteria to evolve defence systems. Type I, II and III restriction enzymes cleave incoming non-modified phage DNAs. Phages have evolved to defend against these restriction systems by modifying their DNA so that they are no longer suitable substrates.
View Article and Find Full Text PDFACS Synth Biol
September 2025
Departamento de Ingeniería Química y Bioprocesos, Escuela de Ingeniería, Pontificia Universidad Católica de Chile, Santiago 7820436, Chile.
β-Carotene is a high-value compound with multiple commercial applications as a pigment and due to its antioxidant properties. For its industrial production, precision fermentation using engineered microorganisms has been proposed as an attractive alternative given consumer concerns and technical limitations of traditional production methods such as chemical synthesis and extraction from plants. However, the factors limiting microbial production are complex and remain poorly understood, hindering bioprocess scale-up.
View Article and Find Full Text PDFAngew Chem Int Ed Engl
September 2025
Department of Chemical and Biological Engineering, University of Colorado, Boulder, 3415 Colorado Avenue, Boulder, CO, 80303, USA.
Assembly-line enzymes carry out multistep synthesis of important metabolites by using acyl carrier proteins (ACPs) to shuttle intermediates along defined sequences of active sites. Despite longstanding interest in reprogramming these systems for metabolic engineering and biosynthetic chemistry, the mechanisms underlying their reaction order remain poorly understood and difficult to control. Here we describe a β-ketoacyl-ACP reductase from Pseudomonas putida (PpFabG4) with an unusual selectivity for medium chains and use it to explore the molecular basis of substrate specificity in enzymes that pull intermediates from fatty acid synthesis, a common route to specialized products.
View Article and Find Full Text PDFAngew Chem Int Ed Engl
August 2025
Department of Biochemistry, Vanderbilt University School of Medicine-Basic Science, Department of Chemistry, Vanderbilt University, Nashville, TN, 37232, USA.
Amino acids undergo numerous enzymatic modifications. However, the broad applicability of amino acid-modifying enzymes for synthetic purposes is limited by narrow substrate scope and often unknown regulatory or accessory factor requirements. Here, we characterize ChlH, a flavin-dependent halogenase (FDH) from the chlorolassin biosynthetic gene cluster.
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