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<i>Eucalyptus camaldulensis</i> Extract Mediated Green Synthesis of Iron Oxide Nanoparticles and In Vitro and In Vivo Biological Screening, and Detailed Molecular Docking Analysis. [PDF]
Rauf A +11 more
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Ionophore PBT2 as a novel approach to combat antibiotic-resistant <i>Helicobacter pylori</i>. [PDF]
Chen H +8 more
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Natural Bioactive Compounds from <i>Delonix regia</i> Seeds Revealed Through Integrated Phytochemical, Biomedical and In Silico Evaluation. [PDF]
Qanash H +8 more
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Alginate Beads Encapsulation Matrix for Urease and Polyethyleneglycol-Urease
Urease was immobilized activated PEG-5000 and encapsulated urease and PEG modified urease within alginate beads. Encapsulated urease and PEG-urease were thoroughly characterized for pH, temperature and stabilities and these properties were compared with free and PEG modified enzyme.
Baysal, Senay Hamarat, Baysal S.H.
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Urease is a nickel enzyme that catalyzes the hydrolysis of urea to ammonia and carbamate, with the latter decomposing spontaneously to yield another molecule of ammonia and bicarbonate, in the last step of organic nitrogen ...
Mazzei, Luca, Ciurli, Stefano
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Table of contents 1. Introduction 2. The structure of native urease 3. The structure of urease complexed with analogues of transition state and substrate 4. The structure-based mechanism 5. The structure of urease complexed with competitive inhibitors 6.
CIURLI, STEFANO LUCIANO
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Although the discovery of urease as the first enzyme for which nickel is essential for activity dates back to 1975, the rationale for Ni selection for the active site of this hydrolase has been only recently unraveled. The past 20 years have indeed witnessed impressive achievements in the understanding of the biological chemistry of Ni in urease, and ...
MAZZEI, LUCA +2 more
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Urease is a nickel-containing enzyme encoded by several microorganisms and plants since its physiological role, involving the conversion of urea into ammonia, is crucial for their survival and/or pathogenicity. The story of urease is rich in Guinness records, i.e., being the first enzyme crystallized, a milestone in the understanding of the protein ...
D'Agostino I., Carradori S.
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Coordination Chemistry Reviews, 2021
Conventional ureases possess dinuclear nickel active sites that are oxygen-stable and require a set of accessory proteins for metallocenter biosynthesis. By contrast, oxygen-labile ureases have active sites containing dual ferrous ions and lack a requirement for maturation proteins. The structures of the two types of urease are remarkably similar, with
Denis A. Proshlyakov +3 more
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Conventional ureases possess dinuclear nickel active sites that are oxygen-stable and require a set of accessory proteins for metallocenter biosynthesis. By contrast, oxygen-labile ureases have active sites containing dual ferrous ions and lack a requirement for maturation proteins. The structures of the two types of urease are remarkably similar, with
Denis A. Proshlyakov +3 more
openaire +2 more sources

