Mörsdorf G, Kaltwasser H
Fachrichtung Mikrobiologie der Universität des Saarlandes, F.R.G.
FEMS Microbiol Lett. 1990 Jan 1;54(1-3):67-73. doi: 10.1016/0378-1097(90)90260-w.
A fragment of chromosomal DNA from proteus vulgaris encoding urease was cloned and expressed in Escherichia coli. A 3 kbp region was sequenced and revealed three open reading frames with homology to jack bean (Canavalia ensiformis) urease. The smallest protein (11 kDa) was homologous to the N-terminus of the plant enzyme and the largest polypeptide (61 kDa) corresponded to the C-terminus. The large protein contained conserved regions and a cysteine residue which is known to be catalytically important in the plant enzyme. A protein of 12 kDa showed homology to residues 132 to 237 of jack bean urease.