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Literature summary for 3.5.1.5 extracted from

  • Benini, S.; Cianci, M.; Mazzei, L.; Ciurli, S.
    Fluoride inhibition of Sporosarcina pasteurii urease: structure and thermodynamics (2014), J. Biol. Inorg. Chem., 19, 1243-1261.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
free enzyme and enzyme in complex with inhibitor fluoride, analysis of the different crystal structures Sporosarcina pasteurii

Inhibitors

Inhibitors Comment Organism Structure
fluoride two fluoride anions are coordinated to the Ni(II) ions in the active site, in terminal and bridging positions. One fluoride competitively binds to the Ni(II) ion proposed to coordinate urea in the initial step of the catalytic mechanism, while another fluoride uncompetitively substitutes the Ni(II)-bridging hydroxide, blocking its nucleophilic attack on urea. Kinetic studies on the fluoride-induced inhibition of urease, mixed competitive and predominant uncompetitive mechanism that increases by increasing the pH, and a lesser competitive inhibition that increases by lowering the pH, overview Sporosarcina pasteurii

Metals/Ions

Metals/Ions Comment Organism Structure
Ni2+ nickel-dependent enzyme, active site bound Sporosarcina pasteurii

Organism

Organism UniProt Comment Textmining
Sporosarcina pasteurii
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining

General Information

General Information Comment Organism
physiological function the enzyme is a virulence factor for ureolytic bacterial human pathogens, but it is also necessary to convert urea, the most worldwide used fertilizer, into forms of nitrogen that can be taken up by crop plants Sporosarcina pasteurii