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Literature summary for 3.5.1.5 extracted from

  • Mazzei, L.; Cianci, M.; Benini, S.; Bertini, L.; Musiani, F.; Ciurli, S.
    Kinetic and structural studies reveal a unique binding mode of sulfite to the nickel center in urease (2016), J. Inorg. Biochem., 154, 42-49 .
    View publication on PubMed
Search for more literature for 3.5.1.5

Crystallization (Commentary)

Crystallization (Comment) Organism
hanging-drop method at 20°C Sporosarcina pasteurii

Inhibitors

Inhibitors Comment Organism Structure
sulfite competitive inhibitor. The structure of the urease-sulfite complex, determined at 1.65 A resolution, shows the inhibitor bound to the dinuclear Ni(II) center of urease in a tridentate mode involving bonds between the two Ni(II) ions in the active site and all three oxygen atoms of the inhibitor Sporosarcina pasteurii

Metals/Ions

Metals/Ions Comment Organism Structure
Ni2+ the enzyme uses two Ni(II) ions in the active site 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
-
-
Sporosarcina pasteurii DSM 33 P41022
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 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
-
 ?

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
0.19
-
 sulfite pH 7.0, 25°C Sporosarcina pasteurii

General Information

General Information Comment Organism
physiological function urease is a virulence factor in several human pathogens, while causing severe environmental and agronomic problems Sporosarcina pasteurii