P. mirabilis

Tributyltin(IV) derivatives of six different pharmaceutically active carboxylates were synthesized and their antibacterial activities were tested using 10 different bacteria (B. cereus, C. diphtheria, E. C. ETEC, K. pneumonia, P. mirabilis, P. aeroginosa,... 

The LPS from Proteus species contain amino acids linked as amides to acidic sugars. Thus, L-lysine is linked by way of N-6 to a D-galacturonic acid residue (52) in the LPS from P. hauseri, but by way of N-2 to a D-glucu-ronic acid residue in the LPS from P. mirabilis 027. The latter LPS also contains L-alanine, linked to the carboxyl group of a D-galacturonic acid residue. 

Also Enterobacteria are able to synthesize unsaturated fatty acids and to incorporate these into the lipid A component. Thus, when grown at low temperature (10- 15°C) E. coli (143), Salmonella spp. (142), P. mirabilis (37), and Y. enterocolitica (145) are incorporated into the lipid A component unsaturated fatty acids that are not present in LPS of bacteria grown at 370 C. For E. coli and Salmonella strains grown at low temperatures, it was found that (Z)-A9-hexadecenoic acid (A9-16 1) was incorporated at the expense of 12 0 (142,143), however, not quantitatively. Further investigations of these lipid A by l.d.-m.s. revealed that the unsaturated fatty acid specifically replaced the 12 0 residue in 14 0[3-6>( 12 0)] that is bound to GlcN(II) (37). A similar effect of thermoadaptation, resulting in the formation of amide-bound 14 0[3-6>(A9-16 1)], was detected in P. mirabilis and Y. enterocolitica (145). 

Microorganisms extracts E. coli P. aeruginosa P. mirabilis K. pneumoinae A. baumannii S. aureus E. faecalis C. albicans C. parapsilosis... 

Lower respiratory tract infections Lower respiratory tract infections, including pneumonia and bronchitis caused by E. coli, K. pneumoniae, P. aeruginosa, Haemophilus influenzae, P. mirabilis, Enterobacter sp. and S. marcescens. Septicemia Septicemia caused by . coli, K. pneumoniae, P. aeruginosa, P. mirabilis, S. marcescens, and Enterobacter sp. 

Gynecologic infections Gynecologic infections, including endometritis and pelvic cellulitis caused by E. coli, K. pneumoniae, Enterobacter sp. including . cloacae, and P. mirabilis. 

Wide spectrum Penicillinase-susceptible Cephalosporins Ampicillin CarbemcHlm Similar to penicillin G also includes E. coli, P. mirabilis, and H. influenzcie. Gram-negative rods and especially useful for Pseudomonas spp. 

P aeruginosa—Pseudomonas aeruginosa P carinii—Pneumocystis carinii P kellicotti—Paragonimus kellicotti P mirabilis—Proteus mirabilis P vivax—Plasmodium vivax PABA— p-aminobenzoic acid PAS—para-aminosalicylic acid Pb—lead... 

A partially purified enzyme from P. mirabilis (72) was found to have a molecular weight of 151,000. The urease of P. rettgeri is an inducible enzyme that appears only when urea, but not its analogs, are present in the media (73). Proteus vulgaris urease was found to be inhibited in vitro by thiourea and two derivatives (74), and by hydroxamic acids (93). 

Although in no case has the enzyme been purified to homogeneity, much evidence exists that the ribonudeoside 2, 3 -cyclic phosphate diesterase activity and the 3 -nucleotidase activity reside in the same protein. Thus, in all cases the ratio of the two activities remained constant throughout purification which has varied from 130-fold for the P. mirabilis enzyme (4) to 2000-fold for the enzyme from V. alginolyticus (6). Anraku (S) found that both activities from E. coli B had the same optimal pH, both showed the same behavior to activators such as Co2+, and to inhibitors [Zn2+, Cu2+, ethylenediaminetetraacetate (EDTA)], both were activated simultaneously by heating at 55° for 5 min and... 

These were differently affected by different procedures. For example, when the enzyme was activated at 55°, the increment in ki was slight, but k2 increased 3.5-fold. Similarly, in the presence of EDTA, fc, and k2 values decreased independently, suggesting that the sites for both activities were different. Center and Behai (5) found that with the P. mirabilis enzyme, cyclic 2, 3 -UMP competitively inhibited the hydrolysis of bis(p-nitrophenyl) phosphate. The Ki was 40 pAf very close to the Km for the cyclic nucleotide (Km, 75 yM) which indicated that the two compounds could serve as alternate substrates being hydrolyzed at the same active site. In contrast, 3 -AMP was a mixed inhibitor of cyclic 2, 3 -UMP and bis(p-nitrophenyl) phosphate hydrolysis. Adenosine was a mixed inhibitor of bis(p-nitrophenyl) phosphate hydrolysis but a competitive inhibitor of 3 -AMP hydrolysis. From such kinetic studies Center and Behai (5) suggested that two separate and adjacent sites A and B are involved in the hydrolysis of the diester and phos-phomonoester substrates. Site A serves as a binding site for hydrolysis of ribonucleoside 2, 3 -cyclic phosphates and together with site B catalyzes the hydrolysis of the diester bond. During this reaction 3 -... 

Substituents of the ester-linked phosphate group Lipopolysaccharide of a Re-mutant of Proteus mirabilis (R45) is similar to the lipopolysaccharide of the Salmonella minnesota Re-mutant (R595) in that it contains a phosphate to glucosamine ratio of approximately 2.4 2.0 ((21), Fig. 2). When the degradation procedure described for Salmonella, however, was applied to P. mirabilis lipopolysaccharide, an unexpected result was obtained (Fig. 2). 

A similar distribution of fatty acids has also been detected in lipid A of other bacteria (Fig. 5). Thus, in Fusobacterium nucleatum, 2 moles of (R)-3-OH-14 0 are ester-bound, one of which is 3-O-acylated by 14 0. In amide linkage, (R)-3-0(14 0)-16 0 is present. In Vibrio cholerae, a dimer of (R)-3-OH-12 0 is bound as an ester while (R)-3-0-(14 0)-14 0 and (R)-3-0-(16 0)-14 0 are amide-linked. The lipid A component of Chromobacterium violaceum possesses 2 moles of (R)-3-OH-10 0 in ester linkage. The amide-bound acyl groups are represented by (R)-3-0H-12 0 residues which are 3-0-acylated by 12 0 and (S)-2-OH-12 0. In P. mirabilis, 3-0H-14 0 is, like in Salmonella, ester-and amide-bound. In this case, however, exclusively 14 0 substitutes the 3-hydroxyl groups of both 0- and N-linked 3-OH-14 0. 

Bacteria cultured for these tests were P. mirabilis, P. aeruginosa (59-1244/lux), and S. aureus (29213 or ATCCR 25923). 

---