Proteus mirabilis urease: histidine 320 of UreC is essential for urea hydrolysis and nickel ion binding within the native enzyme
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منابع مشابه
Proteus mirabilis urease: histidine 320 of UreC is essential for urea hydrolysis and nickel ion binding within the native enzyme.
Proteus mirabilis urease, a nickel-containing enzyme, has been established as a critical virulence determinant in urinary tract infection. An amino acid sequence (residues 308 to 327: TVDEHLDMLMVCHHLDPSIP) within the large urease subunit, UreC, is highly conserved for every urease examined thus far and has been suggested to reside within the enzyme active site. Histidine residues have been post...
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Proteus mirabilis, a common agent of nosocomially acquired and catheter-associated urinary tract infection, is the most frequent cause of infection-induced bladder and kidney stones. Urease-catalyzed urea hydrolysis initiates stone formation in urine and can be inhibited by acetohydroxamic acid and other structural analogs of urea. Since P. mirabilis urease is inducible with urea, there has bee...
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Expression of Proteus mirabilis urease is governed by UreR, an AraC-like positive transcriptional activator. A poly(A) tract nucleotide sequence, consisting of A(6)TA(2)CA(2)TGGTA(5)GA(6)TGA(5), is located 16 bp upstream of the sigma(70)-like ureR promoter P2. Since poly(A) tracts of DNA serve as binding sites for the gene repressor histone-like nucleoid structuring protein (H-NS), we measured ...
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The majority of recent temperature studies which have been made on enzyme systems indicate that their rate, like that of chemical reactions, increases exponentially with the absolute temperature in accordance with the Arrhenius equation. With enzymes, however, this temperature activation ceases above the inactivation temperature of the enzyme. For a specific enzyme system the energy of activati...
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ژورنال
عنوان ژورنال: Infection and Immunity
سال: 1993
ISSN: 0019-9567,1098-5522
DOI: 10.1128/iai.61.6.2570-2577.1993