The N-terminal domain is a composite domain and plays a major trimer stabilising role by contacting the catalytic domain of the symmetry related alpha-subunit.
This family of enzymes are a a large metal dependent hydrolase superfamily [1]. The family includes Adenine deaminase EC:3.5.4.2 that hydrolyses adenine to form hypoxanthine and ammonia. Adenine deaminases reaction is important for adenine utilisatio ...
This family of enzymes are a a large metal dependent hydrolase superfamily [1]. The family includes Adenine deaminase EC:3.5.4.2 that hydrolyses adenine to form hypoxanthine and ammonia. Adenine deaminases reaction is important for adenine utilisation as a purine and also as a nitrogen source [2]. This family also includes dihydroorotase and N-acetylglucosamine-6-phosphate deacetylases, EC:3.5.1.25 These enzymes catalyse the reaction N-acetyl-D-glucosamine 6-phosphate + H2O <=> D-glucosamine 6-phosphate + acetate. This family includes the catalytic domain of urease alpha subunit [3]. Dihydroorotases (EC:3.5.2.3) are also included [4-5].
Ureases hydrolyse urea into ammonia and carbamate. Ureases have been isolated from a wide range of bacteria, fungi and higher plants where it allows the organism to use urea as a nitrogen source. Ureases uses an almost unique bi-nickel catalytic centre which is liganded by a carbamylated lysine.
The mechanism of this enzyme has been subject to debate since the early 1920s and the precise steps in catalysis remain unclear [PMID:20471401].
Defined by 10 residues: HIS:C-134HIS:C-136LYS:C-217HIS:C-219ASP:C-221HIS:C-246HIS:C-272HIS:C-320ARG:C-336ASP:C-360
