The preferred configuration of the active substrate for rabbit liver fructose 1,6 diphosphatase has been determined by techniques based on rapid quench kinetics to be the α anomer of fructose 1,6 P 2. Utilization of the β anomer, however, is also catalyzed by the enzyme with a rate coefficient 5 to 10 fold less than that for the α anomer.
|Original language||English (US)|
|Number of pages||2|
|Journal||Journal of Biological Chemistry|
|Publication status||Published - Jan 1 1974|
All Science Journal Classification (ASJC) codes
- Molecular Biology
- Cell Biology