Literature summary for 3.5.1.5 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.

Crystallization (Commentary)

Crystallization (Comment)	Organism
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

Crystallization (Comment)

Organism

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

Inhibitors	Comment	Organism	Structure
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

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

Natural Substrates/ Products (Substrates)

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

Organism

Organism	UniProt	Comment	Textmining
Sporosarcina pasteurii	P41022 AND P41021 AND P41020	P41022 i.e. subunit A, P41021 i.e. subunit B, P41020 i.e. subunit C	-
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)

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

Substrates and Products (Substrate)

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

pH Optimum

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

General Information

General Information	Comment	Organism
metabolism	the enzyme catalyses the rapid hydrolysis of urea during the last step of the organic nitrogen mineralization	Sporosarcina pasteurii
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