| EC Tree |
| 2. Transferases |
| 2.7 Transferring phosphorus-containing groups |
| 2.7.1 Phosphotransferases with an alcohol group as acceptor |
| ID: | 2.7.1.29 |
|---|---|
| Description: | Glycerone kinase. |
| Alternative Name: |
Dihydroxyacetone kinase. |
| Cath: | 3.30.1180.20; 1.25.40.340; 3.40.50.10440; |
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 2.7.1.29 |
| BRENDA Enzyme Link: | BRENDA 2.7.1.29 |
| KEGG Enzyme Link: | KEGG2.7.1.29 |
| BioCyc Enzyme Link: | BioCyc 2.7.1.29 |
| ExPASy Enzyme Link: | ExPASy2.7.1.29 |
| EC2PDB Enzyme Link: | EC2PDB 2.7.1.29 |
| ExplorEnz Enzyme Link: | ExplorEnz 2.7.1.29 |
| PRIAM enzyme-specific profiles Link: | PRIAM 2.7.1.29 |
| IntEnz Enzyme Link: | IntEnz 2.7.1.29 |
| MEDLINE Enzyme Link: | MEDLINE 2.7.1.29 |
| RHEA:15773 | ATP + dihydroxyacetone = ADP + dihydroxyacetone phosphate + H(+) |
| RULE(radius=1) | [*:1]-[OH;+0:2].[*:3]=[P;H0;+0:4](-[*:5])(-[*:6])-[O;H0;+0:7]-[*:8]>>[*:8]-[OH;+0:7].[*:3]=[P;H0;+0:4](-[*:5])(-[*:6])-[O;H0;+0:2]-[*:1] |
| Reaction | ![]() |
| Core-to-Core | No scaffolds atoms were exchanged as a result of the reaction |
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| Biochemical and molecular characterization of the oxidative branch of glycerol utilization by Citrobacter freundii. | Daniel R, Stuertz K, Gottschalk G | 1995 Aug | 7635824 |
| Crystal structure of the Citrobacter freundii dihydroxyacetone kinase reveals an eight-stranded alpha-helical barrel ATP-binding domain. | Siebold C, Arnold I, Garcia-Alles LF, Baumann U, Erni B | 2003 Nov 28 | 12966101 |
| Purification and characterization of triokinase from porcine kidney. | Miwa I, Kito Y, Okuda J | 1994 Nov | 7831203 |
| Dihydroxyacetone metabolism by human erythrocytes: demonstration of triokinase activity and its characterization. | Beutler E, Guinto E | 1973 Apr | 4688871 |
| Identification of human and rat FAD-AMP lyase (cyclic FMN forming) as ATP-dependent dihydroxyacetone kinases. | Cabezas A, Costas MJ, Pinto RM, Couto A, Cameselle JC | 2005 Dec 30 | 16289032 |