IUBMB Enzyme Nomenclature


Accepted name: bacterial luciferase

Reaction: a long-chain aldehyde + FMNH2 + O2 = a long-chain fatty acid + FMN + H2O +

Other name(s): 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)

Systematic name: long-chain-aldehyde,FMNH2:oxygen oxidoreductase (1-hydroxylating, luminescing)

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, dinoflagellate luciferase.

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9014-00-0


1. Hastings, J.W. and Nealson, K.H. Bacterial bioluminescence. Annu. Rev. Microbiol. 31 (1977) 549-595. [PMID: 199107]

2. Hastings, J.W. Bacterial bioluminescence light emission in the mixed function oxidation of reduced flavin and fatty aldehyde. Crit. Rev. Biochem. 5 (1978) 163-184. [PMID: 363350]

3. Hastings, J.W. and Presswood, R.P. Bacterial luciferase: FMNH2-aldehyde oxidase. Methods Enzymol. 53 (1978) 558-570. [PMID: 309549]

4. Nealson, K.H. and Hastings, J.W. Bacterial bioluminescence: its control and ecological significance. Microbiol. Rev. 43 (1979) 496-518. [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 (1983) 297-301.

6. Kurfurst, M., Ghisla, S. and Hastings, J.W. Characterization and postulated structure of the primary emitter in the bacterial luciferase reaction. Proc. Natl. Acad. Sci. USA 81 (1984) 2990-2994. [PMID: 16593462]

[EC created 1981, modified 2016]

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