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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

General Stability

General Stability on EC 1.14.14.3 - bacterial luciferase

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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
citrate stabilizes against inactivation by proteases, heat, urea
diphosphate stabilizes against inactivation by proteases, heat, urea
inactivation by lyophilization
labile to proteases
longchain alkylresorcinol homologues exhibit a protective effect at micromolar concentrations only, while their millimolar concentrations increase the sensitivity of the model proteins to thermal treatment
no inactivation by repeated freezing/thawing
phosphate stabilizes against inactivation by proteases, heat, urea
repeated freezing/thawing causes inactivation of immobilized enzyme
-
sulfate stabilizes against inactivation by proteases, heat, urea
the wild-type enzyme belongs to the group of luciferases with slow decay, mutant E175G is turned into a luciferase with fast decay, the decay rate of the enzyme is determined by residue Glu175
-