| Autor: |
C C, Chang, A, Laghai, M H, O'Leary, H G, Floss |
| Rok vydání: |
1982 |
| Předmět: |
|
| Zdroj: |
The Journal of biological chemistry. 257(7) |
| ISSN: |
0021-9258 |
| Popis: |
Aspartate beta-decarboxylase catalyzes abortive decarboxylation/transamination of [2-3H]aspartate with at least 17% internal transfer of tritium to the pro-S position at C-4' of the resulting pyridoxamine phosphate. In the normal beta-decarboxylation reaction, at least 1.06% of the tritium from the alpha-position of aspartate appears in the product alanine. The enzyme catalyzes slow hydrogen exchange from the beta-position of alanine but not aspartate. The replacement of the beta-carboxyl group of aspartate by hydrogen occurs in an inversion mode. These results are interpreted in terms of a two-base mechanism. |
| Databáze: |
OpenAIRE |
| Externí odkaz: |
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