PROSITE documentation PDOC00114
Fructose-1-6-bisphosphatase active site


Fructose-1,6-bisphosphatase (EC (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 (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.


Technical section

PROSITE method (with tools and information) covered by this documentation:

FBPASE, PS00124; Fructose-1-6-bisphosphatase active site  (PATTERN)


1AuthorsBenkovic S.J. DeMaine M.M.
TitleMechanism of action of fructose 1,6-bisphosphatase.
SourceAdv. Enzymol. 53:45-82(1982).
PubMed ID6277165

2AuthorsRaines C.A. Lloyd J.C. Willingham N.M. Potts S. Dyer T.A.
TitlecDNA and gene sequences of wheat chloroplast sedoheptulose-1,7-bisphosphatase reveal homology with fructose-1,6-bisphosphatases.
SourceEur. J. Biochem. 205:1053-1059(1992).
PubMed ID1374332

3AuthorsKe H.M. Thorpe C.M. Seaton B. Lipscomb W.N. Marcus F.
TitleStructure refinement of fructose-1,6-bisphosphatase and its fructose 2,6-bisphosphate complex at 2.8 A resolution.
SourceJ. Mol. Biol. 212:513-539(1990).
PubMed ID2157849

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