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A new class EC 7, Translocases, has been added to the EC list. It will be part of ENZYME from release 2018_10. Read more about EC 7 here.

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
BRENDA4.6.1.15
EC2PDB4.6.1.15
ExplorEnz4.6.1.15
PRIAM enzyme-specific profiles4.6.1.15
KEGG Ligand Database for Enzyme Nomenclature4.6.1.15
IUBMB Enzyme Nomenclature4.6.1.15
IntEnz4.6.1.15
MEDLINEFind literature relating to 4.6.1.15
MetaCyc4.6.1.15
UniProtKB/Swiss-Prot
Q58DK4, TKFC_BOVIN;  Q3LXA3, TKFC_HUMAN;  Q8VC30, TKFC_MOUSE;  
F1RKQ4, TKFC_PIG;  Q4KLZ6, TKFC_RAT;  

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All UniProtKB/Swiss-Prot entries referenced in this entry, with possibility to download in different formats, align etc.
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 4.6.1.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 4.6.-.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 4.-.-.-