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3.5.1.5: urease

This is an abbreviated version!
For detailed information about urease, go to the full flat file.

Word Map on EC 3.5.1.5

Reaction

Urea
+
H2O
=
CO2
 + 2 NH3

Synonyms

acid urease, Arthritogenic cationic 19 kDa antigen, BPU, canatoxin, embryo-specific soybean urease, Eu1, Eu4, HPU, jack bean urease, JBU, JBURE-II, More, PMU, urea amido hydrolase, Urea amidohydrolase, urease, urease JBURE-IIb, UreC

ECTree

     3 Hydrolases
         3.5 Acting on carbon-nitrogen bonds, other than peptide bonds
             3.5.1 In linear amides
                3.5.1.5 urease

Crystallization

Crystallization on EC 3.5.1.5 - urease

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
urease is crystallized and the resulting crystals are diffracted to 2.05 A resolution using synchrotron radiation. The crystals belong to the hexagonal space group P6(3)322, with unit-cell parameters a = b = 138.57, c = 198.36 A
-
urease is crystallized at 2.05 A resolution. The active-site architecture of JBU is similar to that of bacterial ureases containing a bi-nickel center. JBU has a bound phosphate and covalently modified residue (Cys592) by beta-mercaptoethanol at its active site. By correlating the structural information of JBU with the available biophysical and biochemical data on insecticidal properties of plant ureases, it is hypothesized that the amphipathic beta-hairpin located in the entomotoxic peptide region of plant ureases might form a membrane insertion beta-barrel as found in beta-poreforming toxins
crystal structure determined at 2.2 A
-
urease is inactive in the crystalline form, possibly due to conformational restrictions associated with a lid covering the active site
-
wild-type and mutant enzyme
-
crystal structure determined at 2.0 A
-
free enzyme and enzyme in complex with inhibitor citrate, hanging drop vapour diffusion method, mixing of 0.001 ml of 11 mg/mL urease in 20 mM sodium N-(2-hydroxyethyl)piperazine-N'-ethanesulphonic acid sodium salt solution, pH 7.5, containing 50 mM Na2SO3, with 0.001 ml of the precipitant solution, equilibration by 1 ml of the precipitant solution, 20°C, the cryoprotectant solution contains 20% ethylene glycol, 2.4 M ammonium sulphate, 100 mM sodium citrate and 50 mM Na2SO3, X-ray diffraction structure determination and analysis at 1.5 A resolution
free enzyme and enzyme in complex with inhibitor fluoride, analysis of the different crystal structures
-
hanging-drop method at 20°C
hanging-drop method at 20°C, the crystal structure of the enzyme-catechol complex, determined at 1.50 A resolution, reveals the structural details of the enzyme inhibition