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TLP hydrolytic activity in the presence of divalent metal ions.

By Sarah C. Hennebry (292188), Leanne C. Sait (292189), Raju Mantena (292190), Thomas J. Humphrey (292191), Ji Yang (114503), Timothy Scott (292193), Andreas Kupz (32399), Samantha J. Richardson (195834) and Richard A. Strugnell (105051)


<p>The production and hydrolysis of 5-HIU was measured at 312 nm and is shown over a 10 minute period. Enzyme reactions were performed as described in the text. Briefly, 0.04 U uricase was equilibrated in 50 mM potassium phosphate buffer, pH 7.8 in the presence or absence of 100 µM divalent metal ions (Cu<sup>2+</sup>; results for other divalent metal cations not shown). Enzyme reactions were initiated with the addition of 100 µM freshly diluted uric acid (at time 0). Reactions were performed at 22°C in a Biorad spectrophotometer. Open squares (□): production of 5-HIU in the absence of metal ions. Closed squares (▪): production of 5-HIU in the presence of Cu<sup>2+</sup>. After approximately 3 minutes, the amount of 5-HIU peaked and underwent slow, spontaneous decomposition. Open circles (○): addition of 5.2 nM recombinant <i>S.</i> Typhimurium TLP at time 2.5 minutes in the absence of metal ions resulted in rapid hydrolysis of 5-HIU. Closed circles (•): in the presence of Cu<sup>2+</sup> no hydrolysis occurred following addition of TLP. (Data for other metal ions not shown).</p

Topics: Microbiology, hydrolytic, divalent
Year: 2013
DOI identifier: 10.1371/journal.pone.0046675.g004
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Provided by: FigShare
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