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Literature summary extracted from

  • Benini, S.; Kosikowska, P.; Cianci, M.; Mazzei, L.; Vara, A.; Berlicki, L.; Ciurli, S.
    The crystal structure of Sporosarcina pasteurii urease in a complex with citrate provides new hints for inhibitor design (2013), J. Biol. Inorg. Chem., 18, 391-399.
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
3.5.1.5 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 Sporosarcina pasteurii

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.5.1.5 citrate binding of the ligand to the active site involves stabilizing interactions, such as a carboxylate group that binds the nickel ions at the active site and several hydrogen bonds with the surrounding residues Sporosarcina pasteurii

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.5.1.5 Ni2+ dependent on, active site bound Sporosarcina pasteurii

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.5.1.5 urea + H2O Sporosarcina pasteurii
-
 CO2 + 2 NH3
-
 ?
3.5.1.5 urea + H2O Sporosarcina pasteurii DSM 33
-
 CO2 + 2 NH3
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
3.5.1.5 Sporosarcina pasteurii P41022 AND P41021 AND P41020 P41022 i.e. subunit A, P41021 i.e. subunit B, P41020 i.e. subunit C
-
3.5.1.5 Sporosarcina pasteurii DSM 33 P41022 AND P41021 AND P41020 P41022 i.e. subunit A, P41021 i.e. subunit B, P41020 i.e. subunit C
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.5.1.5 native enzyme by gel filtration and anion exchange chromatography Sporosarcina pasteurii

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.5.1.5 urea + H2O
-
 Sporosarcina pasteurii CO2 + 2 NH3
-
 ?
3.5.1.5 urea + H2O
-
 Sporosarcina pasteurii DSM 33 CO2 + 2 NH3
-
 ?

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.5.1.5 6.5
-
 assay at Sporosarcina pasteurii

General Information

EC Number General Information Comment Organism
3.5.1.5 metabolism the enzyme catalyses the rapid hydrolysis of urea during the last step of the organic nitrogen mineralization Sporosarcina pasteurii
3.5.1.5 physiological function the enzyme that catalyses the hydrolysis of urea, is a virulence factor for a large number of ureolytic bacterial human pathogens Sporosarcina pasteurii