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Literature summary for 2.7.1.29 extracted from

  • Cabezas, A.; Costas, M.J.; Pinto, R.M.; Couto, A.; Cameselle, J.C.
    Identification of human and rat FAD-AMP lyase (cyclic FMN forming) as ATP-dependent dihydroxyacetone kinases (2005), Biochem. Biophys. Res. Commun., 338, 1682-1689.
    View publication on PubMed
Search for more literature for 2.7.1.29

Cloned(Commentary)

Cloned (Comment) Organism
expression in BL21 cells Homo sapiens

Inhibitors

Inhibitors Comment Organism Structure
FAD inhibits the dihydroxyacetone kinase activity Homo sapiens
FAD inhibits the dihydroxyacetone kinase activity Rattus norvegicus

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
59400
-
 x * 59400, SDS-PAGE Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens Q3LXA3
-
-
Rattus norvegicus
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Rattus norvegicus
-
 Homo sapiens

Source Tissue

Source Tissue Comment Organism Textmining
brain
-
 Homo sapiens
-
liver
-
 Rattus norvegicus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
dihydroxyacetone + ATP
-
 Rattus norvegicus dihydroxyacetone phosphate + ADP
-
 ?
dihydroxyacetone + ATP
-
 Homo sapiens dihydroxyacetone phosphate + ADP
-
 ?

Subunits

Subunits Comment Organism
? x * 59400, SDS-PAGE Homo sapiens

Synonyms

Synonyms Comment Organism
FMN cyclase/dha kinase bifunctional enzyme Rattus norvegicus
FMN cyclase/dha kinase bifunctional enzyme Homo sapiens