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1.14.14.3: bacterial luciferase

This is an abbreviated version!
For detailed information about bacterial luciferase, go to the full flat file.

Word Map on EC 1.14.14.3

Reaction

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

Synonyms

4a-hydroperoxy-4a,5-dihydroFMN intermediate luciferase, aldehyde monooxygenase, alkanal monooxygenase (FMN), bacterial luciferase, COB, Gluc luciferase, HFOOH, luciferase, Lux, LuxA, LuxAB, LuxB, LuxCDABE, LuxF, Vibrio fischeri luciferase, Vibrio harveyi luciferase

ECTree

     1 Oxidoreductases
         1.14 Acting on paired donors, with incorporation or reduction of molecular oxygen
             1.14.14 With reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen into the other donor
                1.14.14.3 bacterial luciferase

Crystallization

Crystallization on EC 1.14.14.3 - bacterial luciferase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
apo-enzyme, to 1.85 A resolution. Apo-LuxF possesses four preorganized binding sites for 6-(3'-(R)-myristyl)-FMN
comparison of the conformational transitions of luciferases from Vibrio harveyi and Photobacterium leiognathi during equilibrium unfolding with urea. Vibrio harveyi luciferase in its native state demonstrates a higher fluorescence intensity per one protein molecule, but a shorter fluorescence lifetime, than Photobacterium leiognathi luciferase. During the first stage of denaturation (at more than 2 M of urea), for V. harveyi luciferase, the fluorescence lifetimes tau1 and tau2 show an increase, while for the P. leiognathi enzyme, the lifetime components decrease. This stage includes the unfolding of the C-terminal domain of the luciferase alpha-subunit. Subunit dissociation does not influence the optical characteristics of either of the luciferases. The unfolding of the subunits occurs in the same way for the two proteins
bacterial luciferase/FMN complex, by the hanging drop method, at 2.3 A resolution. Crystals of recombinant luciferase are grown at room temperature prior to soaking with millimolar concentrations of FMN. Belongs to space group P212121. The isoalloxazine ring is coordinated by an unusual cis-Ala-Ala peptide bond. The reactive sulfhydryl group of Cys106 projects toward position C-4a, the site of flavin oxygenation. Mobile loop that is crystallographically disordered, appears to be a boundary between solvent and the active center. Within this portion of the protein, there is a single contact between Phe272 of the R subunit and Tyr151 of the beta subunit
comparison of the conformational transitions of luciferases from Vibrio harveyi and Photobacterium leiognathi during equilibrium unfolding with urea. Vibrio harveyi luciferase in its native state demonstrates a higher fluorescence intensity per one protein molecule, but a shorter fluorescence lifetime, than Photobacterium leiognathi luciferase. During the first stage of denaturation (at more than 2 M of urea), for V. harveyi luciferase, the fluorescence lifetimes tau1 and tau2 show an increase, while for the P. leiognathi enzyme, the lifetime components decrease. This stage includes the unfolding of the C-terminal domain of the luciferase alpha-subunit. Subunit dissociation does not influence the optical characteristics of either of the luciferases. The unfolding of the subunits occurs in the same way for the two proteins
structure is determined in absence of substrate at low-salt concentrations
-