From a series of rapid quench kinetic experiments, it has been demonstrated that muscle D fructose bisphosphate aldolase catalyzes the cleavage of β D fructose 1,6 bisphosphate but not that of the α anomer, although the α anomer may be tightly bound. Yeast D fructose bisphosphate aldolase appears to utilize both α and β anomers of the substrate, with yeast apoaldolase catalyzing the interconversion of the α and β forms.
|Original language||English (US)|
|Number of pages||5|
|Journal||Journal of Biological Chemistry|
|State||Published - 1975|
All Science Journal Classification (ASJC) codes
- Molecular Biology
- Cell Biology