|PROSITE documentation PDOC00114|
Fructose-1,6-bisphosphatase (EC 184.108.40.206) (FBPase) , a regulatory enzyme in gluconeogenesis, catalyzes the hydrolysis of fructose 1,6-bisphosphate to fructose 6-phosphate. It is involved in many different metabolic pathways and found in most organisms.
Sedoheptulose-1,7-bisphosphatase (EC 220.127.116.11) (SBPase)  is an enzyme found plant chloroplast and in photosynthetic bacteria that catalyzes the hydrolysis of sedoheptulose 1,7-bisphosphate to sedoheptulose 7-phosphate, a step in the Calvin's reductive pentose phosphate cycle. It is functionally and structurally related to FBPase.
In mammalian FBPase, a lysine residue has been shown to be involved in the catalytic mechanism . The region around this residue is highly conserved and can be used as a signature pattern for FBPase and SBPase. It must be noted that, in some bacterial FBPase sequences, the active site lysine is replaced by an arginine.Last update:
December 2001 / Pattern and text revised.
PROSITE method (with tools and information) covered by this documentation:
|1||Authors||Benkovic S.J. DeMaine M.M.|
|Title||Mechanism of action of fructose 1,6-bisphosphatase.|
|Source||Adv. Enzymol. 53:45-82(1982).|
|2||Authors||Raines C.A. Lloyd J.C. Willingham N.M. Potts S. Dyer T.A.|
|Title||cDNA and gene sequences of wheat chloroplast sedoheptulose-1,7-bisphosphatase reveal homology with fructose-1,6-bisphosphatases.|
|Source||Eur. J. Biochem. 205:1053-1059(1992).|
|3||Authors||Ke H.M. Thorpe C.M. Seaton B. Lipscomb W.N. Marcus F.|
|Title||Structure refinement of fructose-1,6-bisphosphatase and its fructose 2,6-bisphosphate complex at 2.8 A resolution.|
|Source||J. Mol. Biol. 212:513-539(1990).|