| EC Tree |
| 3. Hydrolases |
| 3.1 Acting on ester bonds |
| 3.1.3 Phosphoric-monoester hydrolases |
| ID: | 3.1.3.24 |
|---|---|
| Description: | Sucrose-phosphate phosphatase. |
| Alternative Name: |
Sucrose-6-phosphate phosphatase. Sucrose phosphatase. SPP. |
| Cath: | 3.90.1070.10; 3.40.50.1000; 3.40.50.20; 3.40.50.200; 3.40.50.2000; |
Click one PDB to see exact 3D structure provided by NGL.
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.| UniProtKB Enzyme Link: | UniProtKB 3.1.3.24 |
| BRENDA Enzyme Link: | BRENDA 3.1.3.24 |
| KEGG Enzyme Link: | KEGG3.1.3.24 |
| BioCyc Enzyme Link: | BioCyc 3.1.3.24 |
| ExPASy Enzyme Link: | ExPASy3.1.3.24 |
| EC2PDB Enzyme Link: | EC2PDB 3.1.3.24 |
| ExplorEnz Enzyme Link: | ExplorEnz 3.1.3.24 |
| PRIAM enzyme-specific profiles Link: | PRIAM 3.1.3.24 |
| IntEnz Enzyme Link: | IntEnz 3.1.3.24 |
| MEDLINE Enzyme Link: | MEDLINE 3.1.3.24 |
| RHEA:19289 | H2O + sucrose 6(F)-phosphate = phosphate + sucrose |
| RULE(radius=1) | [*:1]-[CH;+0:2](-[*:3])-[O;H0;+0:4]-[CH;+0:5](-[*:6]-[OH;+0:7])-[O;H0;+0:8]-[C;H0;+0:9]1(-[CH2;+0:10]-[OH;+0:11])-[*:12]-[*:13]-[CH;+0:14](-[*:15]-[O;H0;+0:16]-[P;H0;+0:17](=[*:18])(-[*:19])-[*:20])-[O;H0;+0:21]-1.[OH2;+0:22]>>[*:1]-[C;H0;+0:2](-[*:3])(-[O;H0;+0:4]-[CH;+0:10]1-[O;H0;+0:11]-[CH;+0:14](-[*:15]-[OH;+0:16])-[*:13]-[*:12]-[CH;+0:9]-1-[OH;+0:21])-[O;H0;+0:7]-[*:6]-[CH2;+0:5]-[OH;+0:8].[*:18]=[P;H0;+0:17](-[*:19])(-[*:20])-[OH;+0:22] |
| Reaction | ![]() |
| Core-to-Core | No scaffolds atoms were exchanged as a result of the reaction |
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| The structure of a cyanobacterial sucrose-phosphatase reveals the sugar tongs that release free sucrose in the cell. | Fieulaine S, Lunn JE, Borel F, Ferrer JL | 2005 Jul | 15937230 |
| New complexities in the synthesis of sucrose. | Lunn JE, MacRae E | 2003 Jun | 12753969 |
| Purification, molecular cloning, and sequence analysis of sucrose-6F-phosphate phosphohydrolase from plants. | Lunn JE, Ashton AR, Hatch MD, Heldt HW | 2000 Nov 7 | 11050182 |