PROSITE documentation PDOC00114Fructose-1-6-bisphosphatase active site
Fructose-1,6-bisphosphatase (EC 3.1.3.11) (FBPase) [1], 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 3.1.3.37) (SBPase) [2] 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 [3]. 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). | |
| PubMed ID | 6277165 |
| 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). | |
| PubMed ID | 1374332 |
| 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). | |
| PubMed ID | 2157849 |
PROSITE is copyrighted by the SIB Swiss Institute of Bioinformatics and distributed under the Creative Commons Attribution-NonCommercial-NoDerivatives (CC BY-NC-ND 4.0) License, see prosite_license.html.
View entry in original PROSITE document format
View entry in raw text format (no links)