Urease from Canavalia ensiformis (Jack bean)

Subunit molecular weight: ~90,770
Composed of six subunits with total molecular weight: ~544,620

Urease is a nickel-dependent metalloenzyme , found in various plants, bacteria, fungi, and algae. It contains two distinct subunits-UreA(26.5 kDa) and UreB (60.3–61.6 kDa).

Urease aids in the bioavailability of nitrogen in plants. It is implicated in defense mechanism and exhibits insecticidal activity. In addition, urease exhibits antifungal activity by retarding growth and affecting membrane integrity of filamentous fungi and yeasts.

Urease was shown to induce vacuolation in Hela cells, an effect dependent on the ability of urease to convert urea to ammonia.

One micromolar unit will liberate 1.0 μmole of NH₃ from urea per min at pH 7.0 at 25 °C. It is equivalent to 1.0 I.U. or 0.054 Sumner unit (1.0 mg ammonia nitrogen in 5 minutes at pH 7.0 at 20 °C)