Results 151 to 160 of about 54,144 (194)
, 2017 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
openaire +3 more sources
, 2007 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
core +4 more sources
, 2021 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
openaire +2 more sources
, 2023 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.
core +4 more sources
Some of the next articles are maybe not open access.
Related searches:
Related searches:
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
openaire +2 more sources
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
Urological Research, 1979
Urinary stones form as a consequence of urinary supersaturation. Supersaturation occurs as a result of elevated concentrations of urinary solutes. Dietary, metabolic, endocrine, hereditary, and infectious processes alter urinary solute concentrations. Struvite (MgNH4PO.
openaire +2 more sources
Urinary stones form as a consequence of urinary supersaturation. Supersaturation occurs as a result of elevated concentrations of urinary solutes. Dietary, metabolic, endocrine, hereditary, and infectious processes alter urinary solute concentrations. Struvite (MgNH4PO.
openaire +2 more sources
Metal Ion Interactions with Urease and UreD-Urease Apoproteins
Biochemistry, 1996Klebsiella aerogenes urease in a Ni-containing enzyme (two Ni per alpha beta gamma unit) that is purified as an apoprotein from cells grown in Ni-free medium. Partial activation of urease and UreD-urease apoproteins is achieved in vitro by incubation in the presence of Ni(II) and CO2, whereas incubation of these proteins with Ni alone leads to the ...
I S, Park, R P, Hausinger
openaire +2 more sources
2013
Urease is a nickel-dependent enzyme that catalyzes the reaction of water with urea. The reaction initially produces ammonia and carbamate, which then spontaneously decomposes to yield another molecule of ammonia and hydrogen carbonate. The structure and function of ureases are described.
S. Benini +2 more
openaire +2 more sources
Urease is a nickel-dependent enzyme that catalyzes the reaction of water with urea. The reaction initially produces ammonia and carbamate, which then spontaneously decomposes to yield another molecule of ammonia and hydrogen carbonate. The structure and function of ureases are described.
S. Benini +2 more
openaire +2 more sources
Journal of the American Chemical Society, 2005
At the active site of urease, urea undergoes nucleophilic attack by water, whereas urea decomposes in solution by elimination of ammonia so that its rate of spontaneous hydrolysis is unknown. Quantum mechanical simulations have been interpreted as indicating that urea hydrolysis is extremely slow, compared with other biological reactions proceeding ...
Brian P, Callahan +2 more
openaire +2 more sources
At the active site of urease, urea undergoes nucleophilic attack by water, whereas urea decomposes in solution by elimination of ammonia so that its rate of spontaneous hydrolysis is unknown. Quantum mechanical simulations have been interpreted as indicating that urea hydrolysis is extremely slow, compared with other biological reactions proceeding ...
Brian P, Callahan +2 more
openaire +2 more sources
Soybean leaf urease: Comparison with seed urease
Physiologia Plantarum, 1983Soybeans, Glycine max (L.) Merr., from ureides for transport of nitrogen from the root nodule to the shoot. The most direct routes for ureide utilization include the degradation of ureide‐derived urea to NH3 and CO2. Ureolytic activity was found in leaf disks of soybean and exhbited optimal activity at pH 7 in the presence of a high concentration of ...
P. S. Kerr +3 more
openaire +1 more source