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ALDH Enzymes and Hematological Diseases: A Scoping Review of Literature.
Discov Med
December 2024
Department of Biological Hematology, Tours University Hospital, 37000 Tours, France.
Aldehyde dehydrogenases (ALDHs) constitute a group of enzymes that catalyze the oxidation of aldehydes to carboxylic acids. The human ALDH superfamily, including 19 different isoenzymes (ALDH1A1, ALDH1A2, ALDH1A3, AHDH1B1, ALDH1L1, ALDH1L2, ALDH2, ALDH3A1, ALDH3A2, ALDH3B1, ALDH3B2, ALDH4A1, ALDH5A1, ALDH6A1, ALDH7A1, ALDH8A1, ALDH9A1, ALDHA16A1, ALDH18A1), displays different key physiological and toxicological functions, with specific tissue expression and substrate specificity. Several studies have established that ALDH are interesting markers for the identification and quantification of human hematopoietic stem cells and cancer stem cells, notably leukemic stem cells.
View Article and Find Full Text PDFHybrid Enzyme-Electrocatalyst Cascade Modified Gas-Diffusion Electrodes for Methanol Formation from Carbon Dioxide.
Angew Chem Int Ed Engl
December 2024
Analytical Chemistry - Center for Electrochemical Sciences (CES), Faculty of Chemistry and Biochemistry, Ruhr University Bochum, Universitätsstr. 150, D-44780, Bochum, Germany.
We propose a hybrid electrocatalytic-bioelectrocatalytic reaction cascade integrated on a gas diffusion electrode for CO reduction under selective formation of methanol. Ag-BiO selectively reduces gaseous CO to formate at neutral pH conditions. A subsequent enzymatic cascade comprising formaldehyde dehydrogenase and alcohol dehydrogenase, which are both nicotinamide adenine dinucleotide (NAD)-dependent, further reduce formate sequentially to formaldehyde and methanol.
View Article and Find Full Text PDFClosing the Loop in the Carbon Cycle: Enzymatic Reactions Housed in Metal-Organic Frameworks for CO Conversion to Methanol.
Appl Biochem Biotechnol
November 2024
Department of Chemical Sciences, Midlands State University, P. Bag 9055, Senga Road, Gweru, Zimbabwe.
The preparation of value-added chemicals from carbon dioxide (CO) can act as a way of reducing the greenhouse gas from the atmosphere. Industrially significant C1 chemicals like methanol (CHOH), formic acid (HCOOH), and formaldehyde (HCHO) can be formed from CO. One sustainable way of achieving this is by connecting the reactions catalyzed by the enzymes formate dehydrogenase (FDH), formaldehyde dehydrogenase (FALDH), and alcohol dehydrogenase (ADH) into a single cascade reaction where CO is hydrogenated to CHOH.
View Article and Find Full Text PDFEnhancing S-nitrosoglutathione reductase decreases S-nitrosylation of ERO1α and reduces neuronal death in secondary traumatic brain injury.
Nitric Oxide
February 2025
Department of Neurosurgery & Brain and Nerve Research Laboratory, The First Affiliated Hospital of Soochow University, Soochow University, Suzhou, 215006, China; Institute of Stroke Research, Soochow University, Suzhou, 215006, China. Electronic address:
Traumatic brain injury (TBI) has the highest incidence of all common neurological disorders, along with high mortality and disability rates. Pathological conversion of excess nitric oxide (NO) to S-nitrosoglutathion (GSNO) after TBI leads to high S-nitrosylation of intracellular proteins, causing nitrative stress. GSNO reductase (GSNOR) plays an important role by regulating GSNO and SNO-proteins (PSNOs) and as a redox regulator of the nervous system.
View Article and Find Full Text PDFDisrupted nitric oxide homeostasis impacts fertility through multiple processes including protein quality control.
Plant Physiol
December 2024
Department of Biochemistry and Molecular Biology, University of Massachusetts Amherst, Amherst, MA 01003, USA.
Plant fertility is fundamental to plant survival and requires the coordinated interaction of developmental pathways and signaling molecules. Nitric oxide (NO) is a small, gaseous signaling molecule that plays crucial roles in plant fertility as well as other developmental processes and stress responses. NO influences biological processes through S-nitrosation, the posttranslational modification of protein cysteines to S-nitrosocysteine (R-SNO).
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