EC |
1.14.14.3 |
Accepted name: |
bacterial luciferase |
Reaction: |
a long-chain aldehyde + FMNH2 + O2 = a long-chain fatty acid + FMN + H2O + hν |
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 1.13.12.18, dinoflagellate luciferase. |
Links to other databases: |
BRENDA, EXPASY, Gene, KEGG, MetaCyc, PDB, CAS registry number: 9014-00-0 |
References: |
1. |
Hastings, J.W. and Nealson, K.H. Bacterial bioluminescence. Annu. Rev. Microbiol. 31 (1977) 549–595. [DOI] [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. [DOI] [PMID: 16593462] |
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[EC 1.14.14.3 created 1981, modified 2016] |
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