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The plasmid encoding His-tagged organophosphorus hydrolase (OPH) cloned from Sphingobium fuliginis was modified to be transferred back to this bacterium. The replication function of S. amiense plasmid was inserted at downstream of OPH gene, and S. fuliginis was transformed with this plasmid. The transformant produced larger amount of active OPH with His-tag than E. coli.
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http://dx.doi.org/10.1080/09168451.2015.1123606 | DOI Listing |
J Biomol Struct Dyn
September 2025
Enzyme and Microbial Technology Research Center, Faculty of Biotechnology and Biomolecular Sciences, Universiti Putra Malaysia, Serdang, Selangor, Malaysia.
A thermostable paraoxonase (S3wahi-PON) from sp. strain S3wahi was recently characterised and shown to possess stability across a broad temperature range. This study expands upon the initial biochemical characterisation of S3wahi-PON by investigating the structural determinants and conformational adaptability that contribute to its thermostability, using an integrated approach that combines biophysical techniques and molecular dynamics (MD) simulations across a temperature range of 10 °C to 90 °C.
View Article and Find Full Text PDFBMC Pulm Med
September 2025
Department of Medical Biochemistry, Faculty of Medicine, İstanbul Atlas University, 34403, Istanbul, Turkey.
Background: Chronic obstructive pulmonary disease (COPD) is a chronic and progressive condition that develops due to a genetic predisposition, with the dysfunction of antioxidants and anti-protease systems triggered by factors such as smoking. In this study, we aimed to determine the effects of smoking on serum 8-hydroxy-2' deoxyguanosine (8-OHdG) as a marker of oxidative DNA damage, malondialdehyde (MDA) to indicate lipid peroxidation, protein carbonyl (PCO) as a marker of protein damage, and paraoxonase (PON)1 levels as a measure of antioxidant activity involved in maintaining cellular redox balance in COPD patients.
Methods: We conducted a cross-sectional study involving 141 patients with COPD (70 smokers, 71 non-smokers) and 140 healthy controls (70 smokers, 70 non-smokers) recruited from the Acibadem Mehmet Ali Aydinlar University outpatient clinic.
Int J Mol Sci
August 2025
Laboratorio de Contaminación y Toxicología Ambiental, Secretaría de Investigación y Posgrado, Universidad Autónoma de Nayarit, Tepic 63000, Nayarit, Mexico.
Paraoxonase 1 (PON1) is an antioxidant enzyme that plays physio-pathological roles. Prior in silico analysis revealed the presence of response elements of the nuclear receptor superfamily in the promoter, comparable to glucocorticoid receptors (GR), the vitamin D receptor (VDR), and the pregnenolone X receptor (PXR). The aim of this study was to evaluate the effects of 1α,25-dihydroxyvitamin D, a ligand specific to VDR, on the expression and activity of PON1 in hepatocarcinoma cells (HepG2 cells).
View Article and Find Full Text PDFArch Endocrinol Metab
August 2025
Laizhou People's Hospital of Shandong Province Department of Nephrology Laizhou Shandong 261400 China Department of Nephrology, Laizhou People's Hospital of Shandong Province, Laizhou, Shandong 261400, China.
Objective: To investigate the role of PON1 in diabetic nephropathy and elucidate the underlying mechanisms using a cellular model.
Materials And Methods: A diabetic nephropathy model was established using high glucose-induced HK-2 cells. Potential target genes and signaling pathways were identified through bioinformatics databases, and PON1 expression was manipulated to interfere with these pathways.
Chem Biol Interact
October 2025
University of Ljubljana, Faculty of Medicine, Institute of Biochemistry and Molecular Genetics, Vrazov trg 2, 1000, Ljubljana, Slovenia. Electronic address:
Paraoxonase 1 (PON1) is a metalloenzyme that requires calcium ions at both catalytic and structural binding sites to hydrolyze the substrates. The enzyme is efficiently inhibited by several metal ions, especially transition metals, which tend to bind non-specifically to oxygen, nitrogen, and sulfur ligands of amino acid residues on the PON1 surface. In contrast, several lanthanide ions can specifically replace isomorphous Ca ions from many protein binding sites, making them among the most potent metal inhibitors of PON1.
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