Enzyme

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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;

3D structure

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References

External Links

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
MSA:

2.7.1.29;

Phylogenetic Tree:

2.7.1.29;

Uniprot:
M-CSA:
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

References

TitleAuthorsDatePubMed ID
Biochemical and molecular characterization of the oxidative branch of glycerol utilization by Citrobacter freundii.Daniel R, Stuertz K, Gottschalk G1995 Aug7635824
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 B2003 Nov 2812966101
Purification and characterization of triokinase from porcine kidney.Miwa I, Kito Y, Okuda J1994 Nov7831203
Dihydroxyacetone metabolism by human erythrocytes: demonstration of triokinase activity and its characterization.Beutler E, Guinto E1973 Apr4688871
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 JC2005 Dec 3016289032