EC number:3.1.3.46
Enzyme
Download| EC Tree |
| 3. Hydrolases |
| 3.1 Acting on ester bonds |
| 3.1.3 Phosphoric-monoester hydrolases |
3D structure
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Note: Use your mouse to drag, rotate, and zoom in and out of the structure. Mouse-over to identify atoms and bonds. Mouse controls documentation.| PDB |
1K6M;
6IC0;
6IBZ;
6IBY;
6IBX;
6HVJ;
6HVI;
6HVH;
5AK0;
5AJZ;
5AJY;
5AJX;
5AJW;
5AJV;
4MA4;
4D4M;
4D4L;
4D4K;
4D4J;
3QPW;
3QPV;
3QPU;
2I1V;
2DWP;
2DWO;
2AXN;
3NFY;
2H52;
2H4Z;
2H4X;
2F90;
2A9J;
1T8P;
1RII;
1E59;
1FZT;
5PGM;
4PGM;
1BQ4;
1BQ3;
3PGM;
1QHF;
3BIF;
6E4B;
5ZS8;
5ZRM;
5Y65;
5Y64;
5Y35;
5Y2U;
5Y2I;
4QIH;
4PZA;
4PZ9;
4GPI;
4EO9;
4EMB;
3LNT;
3GW8;
3GP5;
3GP3;
3FDZ;
3EZN;
3E9D;
3DCY;
1YJX;
1YFK;
1FBT;
1C81;
1C80;
1C7Z;
1BIF;
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References
External Links
| UniProtKB Enzyme Link: | UniProtKB 3.1.3.46 |
| BRENDA Enzyme Link: | BRENDA 3.1.3.46 |
| KEGG Enzyme Link: | KEGG3.1.3.46 |
| BioCyc Enzyme Link: | BioCyc 3.1.3.46 |
| ExPASy Enzyme Link: | ExPASy3.1.3.46 |
| EC2PDB Enzyme Link: | EC2PDB 3.1.3.46 |
| ExplorEnz Enzyme Link: | ExplorEnz 3.1.3.46 |
| PRIAM enzyme-specific profiles Link: | PRIAM 3.1.3.46 |
| IntEnz Enzyme Link: | IntEnz 3.1.3.46 |
| MEDLINE Enzyme Link: | MEDLINE 3.1.3.46 |
| RHEA:17289 | beta-D-fructose 2,6-bisphosphate + H2O = beta-D-fructose 6-phosphate + phosphate |
| RULE(radius=1) | [*:1]=[P;H0;+0:2](-[*:3])(-[*:4])-[O;H0;+0:5]-[*:6].[OH2;+0:7]>>[*:6]-[OH;+0:5].[*:1]=[P;H0;+0:2](-[*:3])(-[*:4])-[OH;+0:7] |
| Reaction |  |
| Core-to-Core | No scaffolds atoms were exchanged as a result of the reaction |
References
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| Structural and biochemical studies of TIGAR (TP53-induced glycolysis and apoptosis regulator). | Li H, Jogl G | 2009 Jan 16 | 19015259 |
| 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase: head-to-head with a bifunctional enzyme that controls glycolysis. | Rider MH, Bertrand L, Vertommen D, Michels PA, Rousseau GG, Hue L | 2004 Aug 1 | 15170386 |
| Critical switch of the metabolic fluxes by phosphofructo-2-kinase:fructose-2,6-bisphosphatase. A kinetic model. | Goldstein BN, Maevsky AA | 2002 Dec 18 | 12482582 |
| N-terminal truncation affects the kinetics and structure of fructose-6-phosphate 2-kinase/fructose-2,6-bisphosphatase from Arabidopsis thaliana. | Villadsen D, Nielsen TH | 2001 Nov 1 | 11672433 |
| Involvement of the chicken liver 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase sequence His444-Arg-Glu-Arg in modulation of the bisphosphatase activity by its kinase domain. | Zhu Z, Ling S, Yang QH, Li L | 2001 Jul 15 | 11439102 |
| Glutamate 325 is a general acid-base catalyst in the reaction catalyzed by fructose-2,6-bisphosphatase. | Sakurai M, Cook PF, Haseman CA, Uyeda K | 2000 Dec 26 | 11123954 |
| Mechanism of the bisphosphatase reaction of 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase probed by (1)H-(15)N NMR spectroscopy. | Okar DA, Live DH, Devany MH, Lange AJ | 2000 Aug 15 | 10933792 |