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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

Accepted Name
Bacterial luciferase.
Alternative Name(s)
Aldehyde monooxygenase.
Alkanal monooxygenase (FMN-linked).
Reaction catalysed
A long-chain aldehyde + FMNH(2) + O(2) <=> a long-chain fatty acid + FMN + H(2)O + light
  • The reaction sequence starts with the incorporation of a molecule of oxygen into reduced FMN bound to the enzyme, forming luciferase peroxyflavin.
  • The peroxyflavin interacts with an aliphatic long-chain aldehyde, producing a highly fluorescent species believed to be luciferase hydroxyflavin.
  • The enzyme is highly specific for reduced FMN and for long-chain aliphatic aldehydes with eight carbons or more.
  • The highest efficiency is achieved with tetradecanal.
  • Cf. EC
PRIAM enzyme-specific profiles1.14.14.3
KEGG Ligand Database for Enzyme Nomenclature1.14.14.3
IUBMB Enzyme Nomenclature1.14.14.3
MEDLINEFind literature relating to
P09140, LUXA1_PHOLE;  P19839, LUXA1_PHOLU;  P29238, LUXA2_PHOLE;  
P23146, LUXA2_PHOLU;  P19907, LUXA_ALIFS;  P18299, LUXA_KRYAS;  
Q7N575, LUXA_PHOLL;  P24113, LUXA_PHOPO;  P24114, LUXA_VIBAB;  
P07740, LUXA_VIBHA;  P09141, LUXB1_PHOLE;  P19840, LUXB1_PHOLU;  
P29239, LUXB2_PHOLE;  P23147, LUXB2_PHOLU;  P19908, LUXB_ALIFS;  
P18300, LUXB_KRYAS;  Q7N574, LUXB_PHOLL;  P12744, LUXB_PHOPO;  
P07739, LUXB_VIBHA;  

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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 1.14.14.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 1.14.-.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 1.-.-.-