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ENZYME

ENZYME entry: EC 1.14.14.3

Accepted Name
bacterial luciferase
Alternative Name(s)
aldehyde monooxygenase
alkanal monooxygenase (FMN-linked)
Reaction catalysed
a long-chain fatty aldehyde + FMNH2 + O2 <=> a long-chain fatty acid + FMN + 2 H(+) + H2O + hnu
Comment(s)
  • 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 1.13.12.18.
Cross-references
BRENDA1.14.14.3
EC2PDB1.14.14.3
ExplorEnz1.14.14.3
PRIAM enzyme-specific profiles1.14.14.3
KEGG Ligand Database for Enzyme Nomenclature1.14.14.3
IUBMB Enzyme Nomenclature1.14.14.3
IntEnz1.14.14.3
MEDLINEFind literature relating to 1.14.14.3
MetaCyc1.14.14.3
Rhea expert-curated reactions1.14.14.3
UniProtKB/Swiss-Prot
P09140, LUXA1_PHOLEP19839, LUXA1_PHOLUP29238, LUXA2_PHOLE
P23146, LUXA2_PHOLUP19907, LUXA_ALIFSP18299, LUXA_KRYAS
Q7N575, LUXA_PHOLLP24113, LUXA_PHOPOP24114, LUXA_VIBCL
P07740, LUXA_VIBHAP09141, LUXB1_PHOLEP19840, LUXB1_PHOLU
P29239, LUXB2_PHOLEP23147, LUXB2_PHOLUP19908, LUXB_ALIFS
P18300, LUXB_KRYASQ7N574, LUXB_PHOLLP12744, LUXB_PHOPO
P07739, LUXB_VIBHA

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