EC Number |
BRENDA No. |
Title |
Journal |
Volume |
Pages |
Year |
Organism |
PubMed ID |
---|
4.6.1.15 | 730035 |
Bifunctional homodimeric triokinase/FMN cyclase: contribution of protein domains to the activities of the human enzyme and molecular dynamics simulation of domain movements |
J. Biol. Chem. |
289 |
10620-10636 |
2014 |
Homo sapiens |
24569995 |
4.6.1.15 | 441635 |
Enzymic formation of riboflavin 4',5'-cyclic phosphate from FAD: evidence for a specific low-Km FMN cyclase in rat liver |
Biochem. J. |
330 |
881-888 |
1998 |
Rattus norvegicus |
- |
4.6.1.15 | 663888 |
Identification of human and rat FAD-AMP lyase (cyclic FMN forming) as ATP-dependent dihydroxyacetone kinases |
Biochem. Biophys. Res. Commun. |
338 |
1682-1689 |
2005 |
Rattus norvegicus |
16289032 |
4.6.1.15 | 663888 |
Identification of human and rat FAD-AMP lyase (cyclic FMN forming) as ATP-dependent dihydroxyacetone kinases |
Biochem. Biophys. Res. Commun. |
338 |
1682-1689 |
2005 |
Homo sapiens |
16289032 |
4.6.1.15 | 441636 |
Purification, characterization, and substrate and inhibitor structure-activity studies of rat liver FAD-AMP lyase (cyclizing): Preference for FAD and specificity for splitting ribonucleoside diphosphate-X into ribonucleotide and a five-atom cyclic phosphodiester of X, either a monocyclic compound or a cis-bicyclic phosphodiester-pyranose fusion |
Biochemistry |
40 |
13710-13722 |
2001 |
Rattus norvegicus |
11695920 |