EC Number   |
General Information |
Reference |
|---|
    3.1.3.11 | drug target |
potential drug target against Leishmania parasites |
751333 |
| 3.1.3.11 | drug target |
potential drug target for type 2 diabetes |
749493 |
| 3.1.3.11 | drug target |
the enzyme (FBPase-1) is considered to be a new target for the control of diabetes |
-, 749848 |
| 3.1.3.11 | evolution |
chloroplastic FBPase isoenzymes are widely distributed in photosynthetic organisms, i.e. bacteria, blue-green and green algae, lichens, and plants |
-, 749737 |
| 3.1.3.11 | evolution |
FBPases are homotetrameric enzymes with three different isoforms present in plants, two in chloroplasts (cFBP1 and cFBP2) and one in the cytosol (cyFBP). Only cFBP1 needs to be redox activated in order to be fully active, whilst cFBP2 is not redox regulated and, despite its activity, resists higher oxidant concentrations than cFBP1 |
752149 |
| 3.1.3.11 | evolution |
structural comparison of class I versus class II FBPases |
-, 749502 |
| 3.1.3.11 | evolution |
structures of Leishmania fructose-1,6-bisphosphatase (FBPase) reveal species-specific differences in the mechanism of allosteric inhibition of FBPases |
751333 |
| 3.1.3.11 | evolution |
the amino acid sequence of EgFBPaseIII shows low identity (35%) with EgFBPaseI and II, while it shows higher identity of 51-52% with other cytosolic FBPases from plants. EgFBPaseIII has an additional sequence at the N-terminus that other cytosolic FBPases do not possess, this N-terminal region contains no signal peptide or known domain architecture |
-, 750092 |
| 3.1.3.11 | evolution |
the archaeal enzyme belongs to the class V of fructose-1, 6-bisphosphatases. Gene expression of class V FBPase is regulated at the transcription level. The substrate binding residues, including Tyr229, Lys232, and Tyr358, and the residues involved in metal binding, including Asp11, His18, Asp52, Asp53, Gln95, Asp132, Asp233, and Glu357 are completely conserved in all the archaeal FBPases |
-, 747723 |
| 3.1.3.11 | evolution |
the FBP/SBPase found in Thermosynechococcus elongatus is a type II FBPase, a member of the larger Li+-sensitive phosphatase superfamily. It shares 80% sequence identity with the Synechocystis sp. PCC 6803 FBP/SBPase |
749507 |
