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</script>Human serum albumin (HSA) is the most abundant protein in plasma, contributing actively to oncotic pressure maintenance and fluid distribution between body compartments. HSA acts as the main carrier of fatty acids, recognizes metal ions, affects pharmacokinetics of many drugs, provides the metabolic modification of some ligands, renders potential toxins harmless, accounts for most of the anti-oxidant capacity of human plasma, and displays esterase, enolase, glucuronidase, and peroxidase (pseudo)-enzymatic activities. HSA-based catalysis is physiologically relevant, affecting the metabolism of endogenous and exogenous compounds including proteins, lipids, cholesterol, reactive oxygen species (ROS), and drugs. Catalytic properties of HSA are modulated by allosteric effectors, competitive inhibitors, chemical modifications, pathological conditions, and aging. HSA displays anti-oxidant properties and is critical for plasma detoxification from toxic agents and for pro-drugs activation. The enzymatic properties of HSA can be also exploited by chemical industries as a scaffold to produce libraries of catalysts with improved proficiency and stereoselectivity for water decontamination from poisonous agents and environmental contaminants, in the so called “green chemistry” field. Here, an overview of the intrinsic and metal dependent (pseudo-)enzymatic properties of HSA is reported to highlight the roles played by this multifaced protein.
Ions, Aspirin, Molecular Conformation, Green Chemistry Technology, Serum Albumin, Human, Review, Heme, Ligands, Antioxidants, Catalysis, Rats, Fructose-Bisphosphate Aldolase, Phosphopyruvate Hydratase, Animals, Humans, Lipid Peroxidation, Reactive Oxygen Species, Biomarkers, Aldolase activity; Anti-oxidant activity; Enolase activity; Enzymatic properties; Esterase activity; Glucuronidase activity; Human serum albumin; Human serum heme-albumin; Peroxidase activity; Animals; Antioxidants; Aspirin; Biomarkers; Catalysis; Fructose-Bisphosphate Aldolase; Glucuronidase; Heme; Humans; Ions; Ligands; Lipid Peroxidation; Molecular Conformation; Phosphopyruvate Hydratase; Protein Binding; Rats; Serum Albumin, Human; Green Chemistry Technology; Reactive Oxygen Species, Glucuronidase, Protein Binding
Ions, Aspirin, Molecular Conformation, Green Chemistry Technology, Serum Albumin, Human, Review, Heme, Ligands, Antioxidants, Catalysis, Rats, Fructose-Bisphosphate Aldolase, Phosphopyruvate Hydratase, Animals, Humans, Lipid Peroxidation, Reactive Oxygen Species, Biomarkers, Aldolase activity; Anti-oxidant activity; Enolase activity; Enzymatic properties; Esterase activity; Glucuronidase activity; Human serum albumin; Human serum heme-albumin; Peroxidase activity; Animals; Antioxidants; Aspirin; Biomarkers; Catalysis; Fructose-Bisphosphate Aldolase; Glucuronidase; Heme; Humans; Ions; Ligands; Lipid Peroxidation; Molecular Conformation; Phosphopyruvate Hydratase; Protein Binding; Rats; Serum Albumin, Human; Green Chemistry Technology; Reactive Oxygen Species, Glucuronidase, Protein Binding
| citations This is an alternative to the "Influence" indicator, which also reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically). | 156 | |
| popularity This indicator reflects the "current" impact/attention (the "hype") of an article in the research community at large, based on the underlying citation network. | Top 1% | |
| influence This indicator reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically). | Top 10% | |
| impulse This indicator reflects the initial momentum of an article directly after its publication, based on the underlying citation network. | Top 0.1% |
