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- W2071304873 abstract "Escherichia coli asparaginase II catalyzes the hydrolysis of L-asparagine to L-aspartate via a threonine-bound acyl-enzyme intermediate. A nearly inactive mutant in which one of the active site threonines, Thr-89, was replaced by valine was constructed, expressed, and crystallized. Its structure, solved at 2.2 A resolution, shows high overall similarity to the wild-type enzyme, but an aspartyl moiety is covalently bound to Thr-12, resembling a reaction intermediate. Kinetic analysis confirms the deacylation deficiency, which is also explained on a structural basis. The previously identified oxyanion hole is described in more detail." @default.
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- W2071304873 date "1996-07-22" @default.
- W2071304873 modified "2023-10-18" @default.
- W2071304873 title "A covalently bound catalytic intermediate in <i>Escherichia coli</i> asparaginase : Crystal structure of a Thr‐89‐Val mutant" @default.
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- W2071304873 doi "https://doi.org/10.1016/0014-5793(96)00660-6" @default.
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