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1.13.12.5: Renilla-type luciferase

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

Word Map on EC 1.13.12.5

Reaction

coelenterazine h
+
O2
=
coelenterazine h dioxetanone

Synonyms

19kOLase, aequorin, aequorin-1, BFP-aq, blue fluorescent protein from the calcium-binding photoprotein aequorin, Caussia princeps luciferase, clytin, extGLuc, extRLuc, firefly luciferase, fluc, Gaussia luciferase, Gaussia luciferase enzyme, Gaussia princeps luciferase, Gaussia-luciferase, GFP-aq, GLase, GLuc, Luc, luciferase, luciferase (Renilla luciferin), m-Rluc8, membrane-anchored RLUc, Oplophorus luciferase, PI-Rluc, R-Luc, Renilla luciferase, Renilla luciferase-547, Renilla luciferin 2-monooxygenase, Renilla muelleri luciferase, Renilla reniformis luciferase, Renilla-luciferase, Renilla-luciferin 2-monooxygenase, Renilla-type luciferase, RLase, RLase-547, RLuc, RLuc8, short peptide-inserted-Renilla luciferase

ECTree

     1 Oxidoreductases
         1.13 Acting on single donors with incorporation of molecular oxygen (oxygenases)
             1.13.12 With incorporation of one atom of oxygen (internal monooxygenases or internal mixed-function oxidases)
                1.13.12.5 Renilla-type luciferase

Temperature Stability

Temperature Stability on EC 1.13.12.5 - Renilla-type luciferase

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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30
Rluc remaining activity in the absence and presence of 0.6 M and 1.2 M of trehalose, and 1.2 M of sucrose at 30°C is 15%, about 50%, around 100%, and almost 60%, respectively, after 60 min
30 - 52
the F116L/I137V mutant shows a transition starting at 30°C, which is 5°C lower than the wild-type, and ending at 52°C, which is 5°C higher than the wild type. N178D mutant has almost the same denaturation profile
35 - 47
purified recombinant His-tagged wild-type RLuc retains full activity up to 35°C and is inactivated at 47°C
39
temperature for 50% inactivation of aequorin bioluminescence by a 30-min heat shock, mutant enzyme F149S
4 - 50
at 50°C after 30 min incubation time only 20% residual activity, at 40°C after 1 h incubation time complete loss of activity
40
in the absence and presence of 0.6 M of trehalose, the remaining activity is only about 2% and 6%, respectively, although it increases about 70fold upon incubation of the enzyme solution in a buffer containing 1.2 M of trehalose. It also seems that the remaining activity in the presence of 1.2 M of sucrose in the first 10 min is slightly better than in its absence, and a little activity is seen even after 60 min
40 - 47
the stability of the purified recombinant His-tagged N264S/S287P mutant is maintains at a temperature that is 5°C higher than the wild-type.
44
temperature for 50% inactivation of aequorin bioluminescence by a 30-min heat shock, wild-type enzyme and mutant enzyme E35G
46
temperature for 50% inactivation of aequorin bioluminescence by a 30-min heat shock, mutant enzyme E128G
48
temperature for 50% inactivation of aequorin bioluminescence by a 30-min heat shock, mutant enzyme L170I
49
temperature for 50% inactivation of aequorin bioluminescence by a 30-min heat shock, mutant enzyme D117G
50 - 70
engineered enzyme C-SRLuc8 shows significant stability, retaining about 20% of its initial activity after incubation at 70°C for 5 min, while wild-type SRLuc8 completely loses its activity after incubation at this temperature
51
temperature for 50% inactivation of aequorin bioluminescence by a 30-min heat shock, mutant enzyme D153G
52
temperature for 50% inactivation of aequorin bioluminescence by a 30-min heat shock, mutant enzyme Q168AR/L170M, Q168A/L170V and Q168K/L170V
53
temperature for 50% inactivation of aequorin bioluminescence by a 30-min heat shock, mutant enzyme Q168R
57
temperature for 50% inactivation of aequorin bioluminescence by a 30-min heat shock, mutant enzymes Q68R/L170I and Q168R/L179V
65
the residual activity of modified enzyme C-SRLuc8 is approximately 20% after incubation at 65°C for 5 min
72
melting temperature
77
melting temperature, presence of 1 M NaCl
95
-
3 min in the presence of DTT and then cooling on ice, over 93% of the luminescence activity of BFP-aq with coelenterazine is recovered
additional information
Renilla sp.
-
at 37°C reduced activity compared with remaining activity at 25°C