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Hexosediphosphatase
1.Acting on ester bonds
3.Phosphoric monoester hydrolases
D-fructose
6-P + PSedoheptulose 1,7-bi-P
H2O
Sedoheptulose 7-P
ortho-P
The animal enzyme also acts on sedoheptulose 1,7-bisphosphate.
Fructose-1,6-bisphosphatase, 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) 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.
Reference