| Autor: |
Issakidis, Emmanuelle, Decottignies, Paulette, Miginiac-Maslow, Myroslawa |
| Zdroj: |
FEBS Letters; April 1993, Vol. 321 Issue: 1 p55-58, 4p |
| Abstrakt: |
A triple cysteine mutant of sorghum leaf NADP‐malate dehydrogenase has been constructed by site‐directed mutagenesis, combining the previously obtained mutation of the two N‐terminal cysteines with the mutation of the most internal of the two C‐terminal cysteines. The construct, over‐expressed in E. coli, yielded an always active, dithiol‐insensitive enzyme. It can be concluded that the dithiol activation of the unmodified enzyme involves a maximum of two different disulfides per subunit, and that none of the mutated cysteines is implicated in catalysis. |
| Databáze: |
Supplemental Index |
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