EC Tree |
4. Lyases |
4.6 Phosphorus-oxygen lyases |
4.6.1 Phosphorus-oxygen lyases (only sub-subclass identified to date) |
ID: | 4.6.1.15 |
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Description: | FAD-AMP lyase (cyclizing). |
Alternative Name: |
FMN cyclase. |
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Note: Use your mouse to drag, rotate, and zoom in and out of the structure. Mouse-over to identify atoms and bonds. Mouse controls documentation.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 |
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 | ![]() |
Core-to-Core | |
Core-to-Core |
Title | Authors | Date | PubMed ID |
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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 JC | 1998 Mar 1 | 9480905 |
Dihydroxyacetone metabolism by human erythrocytes: demonstration of triokinase activity and its characterization. | Beutler E, Guinto E | 1973 Apr | 4688871 |
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 JC | 2001 Nov 13 | 11695920 |