Probing the functional role of two conserved active site aspartates in mouse adenosine deaminase.

@article{Sideraki1996ProbingTF,
  title={Probing the functional role of two conserved active site aspartates in mouse adenosine deaminase.},
  author={Vera Sideraki and Khalid Mohamedali and David K Wilson and Zhen Chang and Rodney E. Kellems and Florante A. Quiocho and Frederick B. Rudolph},
  journal={Biochemistry},
  year={1996},
  volume={35 24},
  pages={
          7862-72
        }
}
Two adjacent aspartates, Asp 295 and Asp 296, playing major roles in the reaction catalyzed by mouse adenosine deaminase (mADA) were altered using site-directed mutagenesis. These mutants were expressed and purified from an ADA-deficient bacterial strain and characterized. Circular dichroism spectroscopy shows the mutants to have unperturbed secondary structure. Their zinc content compares well to that of wild-type enzyme. Changing Asp 295 to a glutamate decreases the kcat but does not alter… CONTINUE READING
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