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 |