Enzyme

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     4. Lyases
        4.6 Phosphorus-oxygen lyases
            4.6.1 Phosphorus-oxygen lyases (only sub-subclass identified to date)
ID:4.6.1.15
Description:FAD-AMP lyase (cyclizing).
Alternative Name: FMN cyclase.

3D structure

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References

External Links

UniProtKB Enzyme Link: UniProtKB 4.6.1.15
BRENDA Enzyme Link: BRENDA 4.6.1.15
KEGG Enzyme Link: KEGG4.6.1.15
BioCyc Enzyme Link: BioCyc 4.6.1.15
ExPASy Enzyme Link: ExPASy4.6.1.15
EC2PDB Enzyme Link: EC2PDB 4.6.1.15
ExplorEnz Enzyme Link: ExplorEnz 4.6.1.15
PRIAM enzyme-specific profiles Link: PRIAM 4.6.1.15
IntEnz Enzyme Link: IntEnz 4.6.1.15
MEDLINE Enzyme Link: MEDLINE 4.6.1.15
MSA:

4.6.1.15;

Phylogenetic Tree:

4.6.1.15;

Uniprot:
M-CSA:
RHEA:13729 FAD = AMP + H(+) + riboflavin cyclic-4',5'-phosphate
RULE(radius=1) ([*:1]-[OH;+0:2].[*:3]-[P;H0;+0:4](=[*:5])(-[*:6])-[O;H0;+0:7]-[*:8])>>[*:1]-[O;H0;+0:2]-[P;H0;+0:4](-[*:3])(=[*:5])-[*:6].[*:8]-[OH;+0:7]
Reaction
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References

TitleAuthorsDatePubMed ID
Enzymic formation of riboflavin 4',5'-cyclic phosphate from FAD: evidence for a specific low-Km FMN cyclase in rat liver1.Fraiz FJ, Pinto RM, Costas MJ, Aavalos M, Canales J, Cabezas A, Cameselle JC1998 Mar 19480905
Dihydroxyacetone metabolism by human erythrocytes: demonstration of triokinase activity and its characterization.Beutler E, Guinto E1973 Apr4688871
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.Cabezas A, Pinto RM, Fraiz F, Canales J, González-Santiago S, Cameselle JC2001 Nov 1311695920