PMID:5335916
Wolfenden, R, Sharpless, TK and Allan, R (1967) Substrate binding by adenosine deaminase. Specificity, pH dependence, and competition by mercurials.J. Biol. Chem. 242:977-83
| Abstract | No abstract in PubMed |
| Links | PubMed |
Significance
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After purification of Ada, there was found to be no complicating metal or cofactor requirements, a broad pH activity range, and also a broad substrate specificity. The enzyme functioned within the pH ranges of 2.7 to 9.5 in .1M glycine buffers, and was insensitive to the concentration of the buffer. The Mercury atom proved to be a competitive inhibitor in mammalian Ada.
Useful Materials and Methods
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Annotations
| Gene product | Qualifier | GO ID | GO term name | Evidence Code | with/from | Aspect | Notes | Status |
|---|---|---|---|---|---|---|---|---|
|
Add |
GO:0004000 |
adenosine deaminase activity |
ISS: Inferred from Sequence or Structural Similarity |
F |
Seen in Figure 3, adenosine deaminase was irreversibly inactive below pKa 3.7 and above pKa 8.9. Also, in Figure 4, a reciprocal graph shows the rate of deamination of adenosine in the presence of different concentrations of mersalyl acid, a mercurial diuretic. The graph clearly shows a decrease in activity of Ada with increasing amounts of mersalyl acid. |
complete | ||
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