Fructose-2,6-bisphosphate 2-phosphatase
| fructose-2,6-bisphosphate 2-phosphatase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 3.1.3.46 | ||||||||
| CAS no. | 81611-75-8 | ||||||||
| Databases | |||||||||
| BRENDA | enzyme data | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | enzyme entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| Rhea | reactions | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
The enzyme fructose-2,6-bisphosphate 2-phosphatase ({EC 3.1.3.46) catalyzes the reversible reaction
The enzyme characterised from rat liver hydrolyses fructose 2,6-bisphosphate to D-fructose 6-phosphate and orthophosphate.[1] In Arabidopsis thaliana and rice, where it has a role in salt tolerance, the reaction catalysed is reversible, and in the direction from the monophosphate to the biphosphate is equivalent to phosphofructokinase 2, requiring adenosine triphosphate to provide the phosphate group.[2][3] These reactions help regulate fatty acid biosynthesis in plants.[4]
This enzyme is a hydrolase, specifically one acting on phosphoric monoester bonds. The systematic name is β-D-fructose-2,6-bisphosphate 2-phosphohydrolase. Other names in common use include fructose-2,6-bisphosphatase, and D-fructose-2,6-bisphosphate 2-phosphohydrolase.[5]
Structural studies
As of late 2007, 13 structures have been solved for this class of enzymes, with PDB accession codes PDB: 1BIF, PDB: 1C7Z, PDB: 1C80, PDB: 1C81, PDB: 1FBT, PDB: 1K6M, PDB: 1TIP, PDB: 2AXN, PDB: 2BIF, PDB: 2DWO, PDB: 2DWP, PDB: 2I1V, and PDB: 3BIF.
References
- ↑ van Schaftingen E, Davies DR, Hers HG (1982). "Fructose-2,6-bisphosphatase from rat liver". Eur. J. Biochem. 124 (1): 143–9. doi:10.1111/j.1432-1033.1982.tb05917.x. PMID 6282585.
- ↑ Furumoto, Tsuyoshi; Teramoto, Maki; Inada, Noriko; Ito, Masaki; Nishida, Ikuo; Watanabe, Akira (2001). "Phosphorylation of a Bifunctional Enzyme, 6-Phosphofructo-2-kinase/Fructose-2,6-bisphosphate 2-phosphatase, is Regulated Physiologically and Developmentally in Rosette Leaves of Arabidopsis thaliana". Plant and Cell Physiology. 42 (10): 1044–1048. doi:10.1093/pcp/pce161. PMID 11673618.
- ↑ Udomchalothorn, Thanikarn; Maneeprasobsuk, Somporn; Bangyeekhun, Eakaphan; Boon-Long, Preeda; Chadchawan, Supachitra (2009). "The role of the bifunctional enzyme, fructose-6-phosphate-2-kinase/Fructose-2,6-bisphosphatase, in carbon partitioning during salt stress and salt tolerance in Rice (Oryza sativa L.)". Plant Science. 176 (3): 334–341. doi:10.1016/j.plantsci.2008.11.009.
- ↑ Zhai, Zhiyang; Keereetaweep, Jantana; Liu, Hui; Xu, Changcheng; Shanklin, John (2021). "The Role of Sugar Signaling in Regulating Plant Fatty Acid Synthesis". Frontiers in Plant Science. 12 643843. doi:10.3389/fpls.2021.643843. PMC 8020596. PMID 33828577.
- ↑ Enzyme 3.1.3.46 at KEGG Pathway Database.