EC 1.14.14.3 - Bacterial luciferase

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IntEnz Enzyme Nomenclature
EC 1.14.14.3

Names

Accepted name:
bacterial luciferase
Other names:
Vibrio fischeri luciferase
aldehyde monooxygenase
alkanal monooxygenase (FMN-linked)
luciferase
alkanal,reduced-FMN:oxygen oxidoreductase (1-hydroxylating, luminescing)
alkanal,FMNH2:oxygen oxidoreductase (1-hydroxylating, luminescing)
aldehyde,FMNH2:oxygen oxidoreductase (1-hydroxylating, luminescing)
Systematic name:
long-chain-aldehyde,FMNH2:oxygen oxidoreductase (1-hydroxylating, luminescing)

Reaction

Comments:

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.

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ERGO , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Protein domains and families: PROSITE:PDOC00397
Structural data: CSA , EC2PDB
Gene Ontology: GO:0047646
CAS Registry Number: 9014-00-0
UniProtKB/Swiss-Prot: (19) [show] [UniProt]

References

  1. Hastings, J.W.
    Bacterial bioluminescence light emission in the mixed function oxidation of reduced flavin and fatty aldehyde.
    Crit. Rev. Biochem. 5: 163-184 (1978). [PMID: 363350]
  2. Hastings, J.W. and Nealson, K.H.
    Bacterial bioluminescence.
    Annu. Rev. Microbiol. 31: 549-595 (1977). [PMID: 199107]
  3. Hastings, J.W. and Presswood, R.P.
    Bacterial luciferase: FMNH2-aldehyde oxidase.
    Methods Enzymol. 53: 558-570 (1978). [PMID: 309549]
  4. Nealson, K.H. and Hastings, J.W.
    Bacterial bioluminescence: its control and ecological significance.
    Microbiol. Rev. 43: 496-518 (1979). [PMID: 396467]
  5. Suzuki, K., Kaidoh, T., Katagiri, M. and Tsuchiya, T.
    O2 incorporation into a long-chain fatty-acid during bacterial luminescence.
    Biochim. Biophys. Acta 722: 297-301 (1983).
  6. Kurfurst, M., Ghisla, S., Hastings, J. W.
    Characterization and postulated structure of the primary emitter in the bacterial luciferase reaction.
    Proc. Natl. Acad. Sci. U.S.A. 81: 2990-2994 (1984). [PMID: 16593462]

[EC 1.14.14.3 created 1981, modified 2016]