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Unravelling the aromatic symphony: redirecting bifunctional mushroom synthases towards linalool monofunctionality.
Adv Biotechnol (Singap)
January 2025
Singapore Institute of Food and Biotechnology Innovation (SIFBI), Agency for Science, Technology and Research (A*STAR), Singapore, Republic of Singapore.
Enzymes are the cornerstone of biocatalysis, biosynthesis and synthetic biology. However, their applicability is often limited by low substrate selectivity. A prime example is the bifunctional linalool/nerolidol synthase (LNS) that can use both geranyl diphosphate (GPP) and farnesyl diphosphate (FPP) to produce linalool and nerolidol, respectively.
View Article and Find Full Text PDFA high-resolution view of RNA endonuclease cleavage in Bacillus subtilis.
Nucleic Acids Res
January 2025
Department of Biology, Massachusetts Institute of Technology, Cambridge, MA 02142, USA.
RNA endonucleases are the rate-limiting initiator of decay for many bacterial mRNAs. However, the positions of cleavage and their sequence determinants remain elusive even for the well-studied Bacillus subtilis. Here we present two complementary approaches-transcriptome-wide mapping of endoribonucleolytic activity and deep mutational scanning of RNA cleavage sites-that reveal distinct rules governing the specificity among B.
View Article and Find Full Text PDFDetermination of enzyme kinetic parameters of fast-acting Schizosaccharomyces pombe Ulp1 catalytic domain using Forster resonance energy transfer (FRET) assay.
Int J Biol Macromol
January 2025
Department of Microbiology, University of Delhi South Campus, New Delhi 110021, India. Electronic address:
The SUMO fusion technology has immensely contributed to the soluble production of therapeutics and other recombinant proteins in E. coli. The structure-based functionality of SUMO protease has remained the primary determinant for choosing SUMO as a solubility enhancer tag.
View Article and Find Full Text PDFSerine phosphorylation facilitates protein degradation by the human mitochondrial ClpXP protease.
Proc Natl Acad Sci U S A
February 2025
Princess Margaret Cancer Centre, University Health Network, Toronto, ON M5G 1L7, Canada.
ClpXP is a two-component mitochondrial matrix protease. The caseinolytic mitochondrial matrix peptidase chaperone subunit X (ClpX) recognizes and translocates protein substrates into the degradation chamber of the caseinolytic protease P (ClpP) for proteolysis. ClpXP degrades damaged respiratory chain proteins and is necessary for cancer cell survival.
View Article and Find Full Text PDFThe C-terminal structure of the N6-methyladenosine deaminase YerA and its role in deamination.
Biochem J
January 2025
The Sun Yat-Sen University, Guangzhou, China.
The N6-methyladenine (6mA) modification is an essential epigenetic marker and plays a crucial role in processes, such as DNA repair, replication, gene expression regulation, etc. YerA from Bacillus subtilis is considered a novel class of enzymes capable of catalyzing the deamination of 6mA to produce hypoxanthine. Despite the significance of this type of enzymes in bacterial self-defense systems and potential applications as a gene-editing tool, the substrate specificity, the catalytic mechanism and the physiological function of YerA are currently unclear due to the lack of structural information.
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