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:2.7.1.28
Description:Triokinase.
Alternative Name: Triose kinase.

3D structure

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References

External Links

UniProtKB Enzyme Link: UniProtKB 2.7.1.28
BRENDA Enzyme Link: BRENDA 2.7.1.28
KEGG Enzyme Link: KEGG2.7.1.28
BioCyc Enzyme Link: BioCyc 2.7.1.28
ExPASy Enzyme Link: ExPASy2.7.1.28
EC2PDB Enzyme Link: EC2PDB 2.7.1.28
ExplorEnz Enzyme Link: ExplorEnz 2.7.1.28
PRIAM enzyme-specific profiles Link: PRIAM 2.7.1.28
IntEnz Enzyme Link: IntEnz 2.7.1.28
MEDLINE Enzyme Link: MEDLINE 2.7.1.28
MSA:

2.7.1.28;

Phylogenetic Tree:

2.7.1.28;

Uniprot:
M-CSA:
RHEA:13941 ATP + D-glyceraldehyde = ADP + D-glyceraldehyde 3-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
Purification and characterization of triokinase from porcine kidney.Miwa I, Kito Y, Okuda J1994 Nov7831203
Enzymes involved in fructose metabolism in lir and the glyceraldehyde metabolic crossroads.Sillero MA, Sillero A, Sols A1969 Sep5823111
Dihydroxyacetone metabolism by human erythrocytes: demonstration of triokinase activity and its characterization.Beutler E, Guinto E1973 Apr4688871
Bifunctional homodimeric triokinase/FMN cyclase: contribution of protein domains to the activities of the human enzyme and molecular dynamics simulation of domain movements.Rodrigues JR, Couto A, Cabezas A, Pinto RM, Ribeiro JM, Canales J, Costas MJ, Cameselle JC2014 Apr 1124569995
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