Proteus mirabilis urease. Partial purification and inhibition by boric acid and boronic acids

Proteus mirabilis urease. Partial purification and inhibition by boric acid and boronic acids.

Urease was purified 800-fold and partially characterized from Proteus mirabilis, the predominant microorganism associated with urinary stones. Boric acid is a rapid reversible competitive inhibitor of urease. The pH-dependence of inhibition exhibited pKa values of 6.25 and 9.3, where the latter value is probably due to the inherent pKa of boric acid. Three boronic acids also were shown to inhib...

Purification and properties of glucosaminephosphate isomerase of Proteus mirabilis.

A glucosamine-P isomerase has been identified in Proteus mirabilis. The 113-fold purified enzyme exhibits a pH optimum of 7.5 with a secondary maximum at 8.5 and a temperature optimum at 37 degrees C. The apparent Km was 13.3 mM for fructose-6-P and 18.8 mM for L-glutamine. Molecular weight of the enzyme has been estimated as 120 000 and the protein can be dissociated in four subunits by SDS-po...

Plasmids and Putative Virulence Characters in Proteus mirabilis

Bacteriophage typing of Proteus mirabilis, Proteus vulgaris, and Proteus morganii.

A bacteriphage typing scheme for differentiating Proteus isolated from clinical specimens was developed. Twenty-one distinct patterns of lysis were seen when 15 bacteriophages isolated on 8 Proteus mirabilis, 1 P. vulgaris, and 1 P. morganii were used to type 162 of 189 (85.7%) P. mirabilis and P. vulgaris isolates. Seven phages isolated on 3 P. morganii were used to type 13 of 19 (68.4%) P. mo...

Interaction of Proteus mirabilis urease apoenzyme and accessory proteins identified with yeast two-hybrid technology.

Proteus mirabilis, a gram-negative bacterium associated with complicated urinary tract infections, produces a metalloenzyme urease which hydrolyzes urea to ammonia and carbon dioxide. The apourease is comprised of three structural subunits, UreA, UreB, and UreC, assembled as a homotrimer of individual UreABC heterotrimers (UreABC)(3). To become catalytically active, apourease acquires divalent ...