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) |
Cobalt cation or Mn(2+).
|
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 |
Rhea expert-curated reactions | 4.6.1.15 |
UniProtKB/Swiss-Prot |
|
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ENZYME /
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