## Abstract Reversible unfolding of rat testis fructose 6‐phosphate, 2‐kinase:fructose 2,6‐bisphosphatase in guanidine hydrochloride was monitored by following enzyme activities as well as by fluorescence methodologies (intensity, emission maximum, polarization, and quenching), using both intrinsic
Cloning, characterization and expression of a bifunctional fructose-6-phosphate, 2-kinase/fructose-2,6-bisphosphatase from potato
✍ Scribed by Henriette Draborg; Dorthe Villadsen; Tom Hamborg Nielsen
- Book ID
- 110232125
- Publisher
- Springer
- Year
- 1999
- Tongue
- English
- Weight
- 233 KB
- Volume
- 39
- Category
- Article
- ISSN
- 0167-4412
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## Abstract In order to determine environments around four tryptophan residues, located in the N‐terminus, in the kinase and in the phosphatase domains of rat testis Fru 6‐P,2‐kinase:Fru 2,6‐bisphosphatase, mutant enzymes containing a single tryptophan were constructed by site‐directed mutagenesis.
Photosynthetic cells require fructose-1,6-bisphosphatase (FBPase) (EC 3.1.3.11) activity in the chloroplast as well as in the cytoplasm [ 1,11 ]. In both cases the enzyme catalyzes the hydrolysis of fructose-l,6-bisphosphate (F1,6P2) to fructose-6-phosphate (F6P) and inorganic phosphate (Pi). The ch
Both the synthesis and the degradation of Fru-2,6-P2 are catalyzed by a single enzyme protein; ie, the enzyme is bihnctional. This protein, which we have designated 6-phosphofructo 2-kinase/fructose 2,6-bisphosphatase is an important enzyme in the regulation of hepatic carbohydrate metabolism since