KEGG ENZYME: 1.14.14.3

ENZYME: 1.14.14.3

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

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)

R10551

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

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

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

DBGET integrated database retrieval system