1965
DOI: 10.1016/s0021-9258(18)97337-0
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Urease Catalysis

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Cited by 87 publications
(3 citation statements)
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“…In other words, we assume that for I trap above 1 mW/µm 2 , aggregations of urease were trapped. Note that the melting point of urease is around 140 • C, 54 which can be achieved at I trap beyond 8.0 mW/µm 2 based on Figure 2(d), therefore we did not exceed this value in any of our experiments. Finally, we investigated the average time taken to trap urease molecules as a function of the trapping laser intensity for different molecular concentrations (Figure 6(c)).…”
Section: Resultsmentioning
confidence: 69%
“…In other words, we assume that for I trap above 1 mW/µm 2 , aggregations of urease were trapped. Note that the melting point of urease is around 140 • C, 54 which can be achieved at I trap beyond 8.0 mW/µm 2 based on Figure 2(d), therefore we did not exceed this value in any of our experiments. Finally, we investigated the average time taken to trap urease molecules as a function of the trapping laser intensity for different molecular concentrations (Figure 6(c)).…”
Section: Resultsmentioning
confidence: 69%
“…Consideration must also be given to the pH optimum of the immobilized urease. An optimum pH of 6-7 has been reported by Fishbein et al (46) and Gorin et al ( 47), respectively, for urease. The stability and activity of urease drops off rapidly at pH values much greater than this.…”
Section: Resultsmentioning
confidence: 77%
“…9,10 To interfere with the urea hydrolysis reaction catalyzed by urease, a variety of both competitive and non-competitive urease inhibitors have been developed, including hydroxyurea, thiourea, acetohydroxamic acid (AHA), phosphoramidites, quinones, and Au(III) compound, and so on. [11][12][13][14][15][16][17][18][19][20][21][22][23][24][25][26] Among the known urease inhibitors, AHA and hydroxyurea are the substrate analog inhibitors. The common characteristics of their binding mechanism are that each of their carbonyl oxygen atoms is primarily coordinated with the Ni1 ion, and the Ni1-bound oxygen atom forms a hydrogen bond with a histidine residue nearby in the active site of the enzyme.…”
Section: Introductionmentioning
confidence: 99%