KEGG   ENZYME: 1.14.14.3Help
Entry
EC 1.14.14.3                Enzyme                                 

Name
bacterial luciferase;
aldehyde monooxygenase;
luciferase;
Vibrio fischeri luciferase;
alkanal,reduced-FMN:oxygen oxidoreductase (1-hydroxylating, luminescing);
alkanal,FMNH2:oxygen oxidoreductase (1-hydroxylating, luminescing);
alkanal monooxygenase (FMN);
aldehyde,FMNH2:oxygen oxidoreductase (1-hydroxylating, luminescing)
Class
Oxidoreductases;
Acting on paired donors, with incorporation or reduction of molecular oxygen;
With reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen into the other donor
BRITE hierarchy
Sysname
long-chain-aldehyde,FMNH2:oxygen oxidoreductase (1-hydroxylating, luminescing)
Reaction(IUBMB)
a long-chain aldehyde + FMNH2 + O2 = a long-chain fatty acid + FMN + H2O + hnu [RN:R10551]
Reaction(KEGG)
Substrate
long-chain aldehyde [CPD:C00609];
FMNH2 [CPD:C01847];
O2 [CPD:C00007]
Product
long-chain fatty acid [CPD:C00638];
FMN [CPD:C00061];
H2O [CPD:C00001];
hnu [CPD:C00205]
Comment
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, dinoflagellate luciferase.
History
EC 1.14.14.3 created 1981, modified 2016
Orthology
K00494  alkanal monooxygenase alpha chain
K15854  alkanal monooxygenase beta chain
Genes
PLU: plu2081(luxA) plu2082(luxB)
PAY: PAU_02511(luxB) PAU_02512(luxA)
PTT: VY86_20590 VY86_20595
VHA: VIBHAR_06241 VIBHAR_06242
VCA: M892_20835 M892_20840
VFI: VF_A0920(luxB) VF_A0921(luxA)
VFM: VFMJ11_A1038 VFMJ11_A1039
VSA: VSAL_II0961(luxB) VSAL_II0962(luxA)
SWD: Swoo_3635 Swoo_3636
Taxonomy
Reference
1  [PMID:199107]
  Authors
Hastings JW, Nealson KH.
  Title
Bacterial bioluminescence.
  Journal
Annu Rev Microbiol 31:549-95 (1977)
DOI:10.1146/annurev.mi.31.100177.003001
Reference
2  [PMID:363350]
  Authors
Hastings JW.
  Title
Bacterial bioluminescence light emission in the mixed function oxidation of reduced flavin and fatty aldehyde.
  Journal
CRC Crit Rev Biochem 5:163-84 (1978)
Reference
3  [PMID:309549]
  Authors
Hastings JW, Presswood RP.
  Title
Bacterial luciferase: FMNH2-aldehyde oxidase.
  Journal
Methods Enzymol 53:558-70 (1978)
Reference
4  [PMID:396467]
  Authors
Nealson KH, Hastings JW.
  Title
Bacterial bioluminescence: its control and ecological significance.
  Journal
Microbiol Rev 43:496-518 (1979)
Reference
5
  Authors
Suzuki, K., Kaidoh, T., Katagiri, M. and Tsuchiya, T.
  Title
O2 incorporation into a long-chain fatty-acid during bacterial luminescence.
  Journal
Biochim Biophys Acta 722:297-301 (1983)
Reference
6  [PMID:16593462]
  Authors
Kurfurst M, Ghisla S, Hastings JW
  Title
Characterization and postulated structure of the primary emitter in the bacterial luciferase reaction.
  Journal
Proc Natl Acad Sci U S A 81:2990-4 (1984)
DOI:10.1073/pnas.81.10.2990
Other DBs
ExplorEnz - The Enzyme Database: 1.14.14.3
IUBMB Enzyme Nomenclature: 1.14.14.3
ExPASy - ENZYME nomenclature database: 1.14.14.3
BRENDA, the Enzyme Database: 1.14.14.3
CAS: 9014-00-0

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