Abstract
IT is now becoming obvious that the simple view of urease structure and function, current for half a century1, is inadequate. The enzyme is not absolutely specific for urea, and it has at least two additional substrates, hydroxyurea2 and dihydroxyurea3. Kinetic isotope data indicate multiple substrate sites that not only interact but also interconvert4, and multiple molecular forms have been frequently demonstrated by analytic ultracentrifugation and gel filtration techniques5. So far, however, the multiple forms have not been shown to be enzymatically active.
Published Version
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