ENZYME entry: EC 4.6.1.15
| Accepted Name |
|---|
| FAD-AMP lyase (cyclizing).
|
| Alternative Name(s) |
|---|
| FMN cyclase. |
| Reaction catalysed |
|---|
| FAD <=> AMP + riboflavin cyclic-4',5'-phosphate |
| Cofactor(s) |
|---|
| Manganese or cobalt.
|
| Comment(s) |
|---|
- While FAD was the best substrate tested the enzyme also splits
ribonucleoside diphosphate-X compounds in which X is an acyclic or
cyclic monosaccharide or derivative bearing an X-OH group that is
able to attack internally the proximal phosphorus with the geometry
necessary to form a P=X product; either a five-atom monocyclic
phosphodiester or a cis-bicyclic phosphodiester-pyranose fusion.
- The reaction is strongly inhibited by ADP or ATP but is unaffected by
the presence of the product, cFMN.
|
| Cross-references |
|---|
| BRENDA | 4.6.1.15 |
| EC2PDB | 4.6.1.15 |
| ExplorEnz | 4.6.1.15 |
| PRIAM enzyme-specific profiles | 4.6.1.15 |
| KEGG Ligand Database for Enzyme Nomenclature | 4.6.1.15 |
| IUBMB Enzyme Nomenclature | 4.6.1.15 |
| IntEnz | 4.6.1.15 |
| MEDLINE | Find literature relating to 4.6.1.15 |
| MetaCyc | 4.6.1.15 |
| UniProtKB/Swiss-Prot |
|
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