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PROSITE documentation PDOC00114 [for PROSITE entry PS00124]

Fructose-1-6-bisphosphatase active site





Description

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.

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 https://prosite.expasy.org/prosite_license.html --------------------------------------------------------------------------------.

Last update:

December 2001 / Pattern and text revised.

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Technical section

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

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


References

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



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.

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