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Literature summary for 4.6.1.15 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 4.6.1.15

Cloned(Commentary)

Cloned (Comment) Organism
expression in BL21 cells Homo sapiens

Inhibitors

Inhibitors Comment Organism Structure
ATP inhibits the FMN cyclase activity Homo sapiens
ATP inhibits the FMN cyclase 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
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
0.01 0.02 FMN cyclase activity, lysate supernatant of BL21 cells, pH7.5, 37°C Homo sapiens

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
FAD
-
 Rattus norvegicus AMP + riboflavin cyclic-4',5'-phosphate
-
 ?
FAD
-
 Homo sapiens AMP + riboflavin cyclic-4',5'-phosphate
-
 ?

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