Hydrolases;
Acting on carbon-nitrogen bonds, other than peptide bonds;
In linear amides
BRITE hierarchy

urea amidohydrolase

urea + 2 H2O = hydrogen carbonate + 2 NH3 (overall reaction) [RN:R13420];
(1a) urea + H2O = carbamate + NH3 [RN:R13421];
(1b) carbamate + H2O = hydrogen carbonate + NH3 (spontaneous) [RN:R12185]

R12185 R13420 R13421;
(other) R00131 R06134
Reaction

urea [CPD:C00086];
H2O [CPD:C00001];
carbamate [CPD:C01563]

A nickel protein. Urease catalyses the hydrolysis of urea to yield ammonia and carbamate, which spontaneously hydrolyses to form carbonic acid and a second molecule of ammonia. In aqueous solutions the products convert to ammonium and hydrogen carbonate. The enzyme is widespread and is found in many bacteria, some archaea, and many eukaryotes, including plants, some invertebrates, and numerous eukaryotic microorganisms. Urease is one of the earlier enzymes to be studied, first obtained In 1874 [1,2], and named urease in 1890 [3]. The crystallization of urease in 1926 was a significant landmark in biochemistry, showing for the first time ever that enzymes are proteins and can be crystallized [4]. In 1975 it was found that the enzyme contains nickel ions in its active site [5,6].

EC 3.5.1.5 created 1961, modified 2024