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Determining why convergent traits use distinct versus shared genetic components is crucial for understanding how evolutionary processes generate and sustain biodiversity. However, the factors dictating the genetic underpinnings of convergent traits remain incompletely understood. Here, we use heterologous protein expression, biochemical assays, and phylogenetic analyses to confirm the origin of a luciferase gene from haloalkane dehalogenases in the brittle star Amphiura filiformis. Through database searches and gene tree analyses, we also show a complex pattern of the presence and absence of haloalkane dehalogenases across organismal genomes. These results first confirm parallel evolution across a vast phylogenetic distance, because octocorals like Renilla also use luciferase derived from haloalkane dehalogenases. This parallel evolution is surprising, even though previously hypothesized, because many organisms that also use coelenterazine as the bioluminescence substrate evolved completely distinct luciferases. The inability to detect haloalkane dehalogenases in the genomes of several bioluminescent groups suggests that the distribution of this gene family influences its recruitment as a luciferase. Together, our findings highlight how biochemical function and genomic availability help determine whether distinct or shared genetic components are used during the convergent evolution of traits like bioluminescence.
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http://dx.doi.org/10.1093/molbev/msaf081 | DOI Listing |
ACS Catal
August 2025
Department of Chemistry, University of Southern California, Los Angeles, California 90089, United States.
Chlorinated hydrocarbons are widely used as solvents and synthetic intermediates, but their chemical persistence can cause hazardous environmental accumulation. Haloalkane dehalogenase from (DhlA) is a bacterial enzyme that naturally converts toxic chloroalkanes into less harmful alcohols. Using a multiscale approach based on the empirical valence bond method, we investigate the catalytic mechanism of 1,2-dichloroethane dehalogenation within DhlA and its mutants.
View Article and Find Full Text PDFBioorg Chem
August 2025
School of Food Science and Pharmaceutical Engineering, Nanjing Normal University, NO. 1, Wenyuan Road, Nanjing 210023, PR China; State Key Laboratory of Microbial Technology, Nanjing Normal university, PR China. Electronic address:
Optically pure (S)-1-phenylethanol, a crucial synthetic intermediate widely applied in the pharmaceutical and food industries, is currently produced via well-established biological methods primarily relying on ketoreductase-mediated asymmetric synthesis and lipase-catalyzed kinetic resolution. This study presents a biocatalytic approach utilizing haloalkane dehalogenase DbjA for the kinetic resolution of racemic 1-chloro-1-phenylethane in organic solvents to synthesize (S)-1-phenylethanol. Following systematic optimization of reaction conditions, the system achieved an enantiomeric excess (ee) of 97 % for (S)-1-chloro-1-phenylethane and an (S)-1-phenylethanol yield of 46 % (ee > 99 %), demonstrating exceptional enantioselectivity (E = 536).
View Article and Find Full Text PDFJ Chem Inf Model
August 2025
Loschmidt Laboratories, Department of Experimental Biology and RECETOX, Faculty of Science, Masaryk University, Kotlarska 2, Brno 611 37, Czech Republic.
Modern computational tools can predict the mutational effects on protein stability, sometimes at the expense of activity or solubility. Here, we investigate two homologous computationally stabilized haloalkane dehalogenases: (i) the soluble thermostable DhaA115 ( = 74 °C) and (ii) the poorly soluble and aggregating thermostable LinB116 ( = 65 °C), together with their respective wild-type variants. The intriguing difference in the solubility of these highly homologous proteins has remained unexplained for three decades.
View Article and Find Full Text PDFInt J Mol Sci
June 2025
Center for Bio-Imaging & Translational Research and Bioimaging Data Curation Center, Korea Basic Science Institute (KBSI), Cheongju 28119, Republic of Korea.
Interactions between chemical drugs and their target proteins are fundamental to drug screening and precision therapy in modern clinical medicine. However, elucidating these interactions within living cells remains challenging due to the limited availability of efficient detection methods. Despite substantial efforts, technical limitations still impede the identification of direct interactors.
View Article and Find Full Text PDFBiosens Bioelectron
August 2025
Key Laboratory of Resource Biology and Biotechnology in Western China, Ministry of Education, College of Life Sciences, Northwest University, Xi'an, 710069, China. Electronic address:
Surface Plasmon Resonance (SPR) is a pivotal technique for measuring biomolecular interactions, with the sensor surface typically made of gold or silver and requiring proteins to be immobilized in a controlled manner. Traditional methods, such as random crosslinking via covalent amide bonds (EDC/NHS strategy), resulting in diverse protein orientations. Alternatively, site-specific immobilization strategies offer better orientation control, they are still challenged by the purification needs for protein of interests and steric hindrance produced by bulk protein tags.
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