Biological enzymes significantly speed up chemical reactions in living organisms. The complex environment within cells has long been appreciated as a major regulator of enzymatic activities. Recent advances in the rapidly evolving field of biological condensates, which are spontaneously formed by macromolecules through phase separation, suggest new possibilities for how enzymatic reactions may be modulated within cells. Here, we review the latest studies of enzymatic reactions in biological condensates focusing on basic concepts in enzymology and discussing some context-dependent roles of phase separation in regulating biochemical reactions.
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http://dx.doi.org/10.1016/j.jmb.2020.08.009 | DOI Listing |
Bioresour Technol
January 2025
University of Zagreb Faculty of Chemical Engineering and Technology, Marulićev trg 19, HR-10000 Zagreb, Croatia. Electronic address:
Efforts to reduce the impact of chemical processes on the environment are leading to a shift to enzymatic alternatives, with laccases standing out for their versatile substrate oxidation capabilities. This study addresses the improvement of biocatalytic reactions by deep eutectic solvents (DES), in particular DES-based aqueous two-phase systems (ATPS) for the extraction of biomolecules. Continuous laccase extraction from crude samples was achieved using a DES-based ATPS, which was first optimized in a batch extractor and later intensified in a microextractor.
View Article and Find Full Text PDFFront Biosci (Landmark Ed)
January 2025
Department of Cytobiology and Proteomics, Medical University of Lodz, 92-215 Lodz, Poland.
Background: Androgenic anabolic steroids (AASs) are synthetic drugs structurally related to testosterone, with the ability to bind to androgen receptors. Their uncontrolled use by professional and recreational sportspeople is a widespread problem. AAS abuse is correlated with severe damage to the cardiovascular system, including changes in homeostasis and coagulation disorders.
View Article and Find Full Text PDFBiomolecules
January 2025
Institute of Biochemistry and Signal Transduction, University Medical Center Hamburg-Eppendorf, 20246 Hamburg, Germany.
The Src homology 2 domain-containing inositol 5-phosphatase 1 (SHIP1) is a multidomain protein consisting of two protein-protein interaction domains, the Src homology 2 (SH2) domain, and the proline-rich region (PRR), as well as three phosphoinositide-binding domains, the pleckstrin homology-like (PHL) domain, the 5-phosphatase (5PPase) domain, and the C2 domain. SHIP1 is commonly known for its involvement in the regulation of the PI3K/AKT signaling pathway by dephosphorylation of phosphatidylinositol-3,4,5-trisphosphate (PtdIns(3,4,5)P) at the D5 position of the inositol ring. However, the functional role of each domain of SHIP1 for the regulation of its enzymatic activity is not well understood.
View Article and Find Full Text PDFNat Commun
January 2025
The Picower Institute for Learning and Memory, MIT, Cambridge, MA, USA.
Many essential proteins require pyridoxal 5'-phosphate, the active form of vitamin B6, as a cofactor for their activity. These include enzymes important for amino acid metabolism, one-carbon metabolism, polyamine synthesis, erythropoiesis, and neurotransmitter metabolism. A third of all mammalian pyridoxal 5'-phosphate-dependent enzymes are localized in the mitochondria; however, the molecular machinery involved in the regulation of mitochondrial pyridoxal 5'-phosphate levels in mammals remains unknown.
View Article and Find Full Text PDFSheng Wu Gong Cheng Xue Bao
January 2025
Key Laboratory of Industrial Fermentation Microbiology, Ministry of Education, College of Bioengineering, Tianjin University of Science & Technology, Tianjin 300457, China.
-methyl-L-cysteine sulfoxide (SMCO) is a non-protein sulfur-containing amino acid with a variety of functions. There are few reports on the enzymes catalyzing the biosynthesis of SMCO from -methyl-L-cysteine (SMC). In this study, the flavin-containing monooxygenase gene derived from () was heterologously expressed in BL21(DE3) and the enzymatic properties of the expressed protein were analyzed.
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