| Sumario: | The article reports that to appreciate the power of an enzyme as a catalyst, and its potential sensitivity to inhibition by an ideal transition-state analogue, it is useful to know the rate of the spontaneous reaction in the absence of a catalyst. According to the authors, it would be of interest to know how these rate enhancements compare with those produced by other hydrolases that may be related in their mechanism of action. Urease appears to be unique among hydrolases in containing two nickel atoms, which presumably assist this enzyme in grappling effectively with this unusually simple substrate.
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