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Reference on EC 4.6.1.15 - FAD-AMP lyase (cyclizing)

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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Fraiz, F.J.; Pinto, R.M.; Costas, M.J.; Avalos, M.; Canales, J.; Cabezas, A.; Cameselle, J.C.
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
-
Manually annotated by BRENDA team
Cabezas, A.; Pinto, R.M.; Fraiz, F.; Canales, J.; Gonzalez-Santiago, S.; Cameselle, J.C.
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
Manually annotated by BRENDA team
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
Biochem. Biophys. Res. Commun.
338
1682-1689
2005
Rattus norvegicus, Homo sapiens (Q3LXA3), Homo sapiens
Manually annotated by BRENDA team
Rodrigues, J.R.; Couto, A.; Cabezas, A.; Pinto, R.M.; Ribeiro, J.M.; Canales, J.; Costas, M.J.; Cameselle, J.C.
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
Manually annotated by BRENDA team