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coelenterazine + O2
coelenteramide + CO2 + hnu
-
-
-
?
h-coelenterazine + O2
h-coelenteramide + CO2 + hnu
-
-
-
?
[aequorin] 1,2-dioxetan-3-one
[aequorin] coelenteramide + CO2 + hnu
reaction in presence of Ca2+
-
-
?
[apoaequorin] + coelenterazine + O2
[aequorin] 1,2-dioxetan-3-one
-
-
-
?
[apoaequorin] + coelenterazine + O2
[apoaequorin] + coelenteramide + CO2 + hnu
-
-
-
?
[apoaequorin] + coelenterazine + O2 + 3 Ca2+
[excited state blue fluorescent protein] + CO2
[apoaequorin] + cp-coelenterazine + O2 + 3 Ca2+
[excited state blue fluorescent protein] + CO2
-
-
-
?
[apoaequorin] + f-coelenterazine + O2 + 3 Ca2+
[excited state blue fluorescent protein] + CO2
-
-
-
?
[apoaequorin] + h-coelenterazine + O2 + 3 Ca2+
[excited state blue fluorescent protein] + CO2
-
-
-
?
[apoaequorin] + hcp-coelenterazine + O2 + 3 Ca2+
[excited state blue fluorescent protein] + CO2
-
-
-
?
additional information
?
-
[apoaequorin] + coelenterazine + O2 + 3 Ca2+
[excited state blue fluorescent protein] + CO2
-
-
-
?
[apoaequorin] + coelenterazine + O2 + 3 Ca2+
[excited state blue fluorescent protein] + CO2
-
-
-
?
[apoaequorin] + coelenterazine + O2 + 3 Ca2+
[excited state blue fluorescent protein] + CO2
flash type light emission
-
-
?
[apoaequorin] + coelenterazine + O2 + 3 Ca2+
[excited state blue fluorescent protein] + CO2
the specific bioluminescence activities of five recombinant hydromedusan Ca2+-regulated photoproteins - aequorin, mitrocomin, clytin and obelins from Obelia longissima and Obelia geniculata is compared. Along with bioluminescence spectra, kinetics of light emission reactions and sensitivities to calcium, these photoproteins also differ in specific activities and consequently in quantum yields of biox02luminescent reactions. The highest specific activities are found for obelins and mitrocomin, whereas those of aequorin and clytin are lower
-
-
?
[apoaequorin] + coelenterazine + O2 + 3 Ca2+
[excited state blue fluorescent protein] + CO2
the interaction between C-terminal Tyr208 and Tyr13 of the berovin first alpha-helix is essential for the stabilization and proper orientation of the 2-hydroperoxy adduct of coelenterazine within the internal cavity as well as for supporting its closed conformation. In contrast to hydromedusan photoproteins, in berovin the interplay between Tyr residues is conditioned rather by the pi-pi interaction of their phenyl rings than by the formation of hydrogen bonds between OH-groups
-
-
?
[apoaequorin] + coelenterazine + O2 + 3 Ca2+
[excited state blue fluorescent protein] + CO2
-
-
-
?
[apoaequorin] + coelenterazine + O2 + 3 Ca2+
[excited state blue fluorescent protein] + CO2
the specific bioluminescence activities of five recombinant hydromedusan Ca2+-regulated photoproteins - aequorin, mitrocomin, clytin and obelins from Obelia longissima and Obelia geniculata is compared. Along with bioluminescence spectra, kinetics of light emission reactions and sensitivities to calcium, these photoproteins also differ in specific activities and consequently in quantum yields of biox02luminescent reactions. The highest specific activities are found for obelins and mitrocomin, whereas those of aequorin and clytin are lower
-
-
?
[apoaequorin] + coelenterazine + O2 + 3 Ca2+
[excited state blue fluorescent protein] + CO2
-
-
-
?
[apoaequorin] + coelenterazine + O2 + 3 Ca2+
[excited state blue fluorescent protein] + CO2
the specific bioluminescence activities of five recombinant hydromedusan Ca2+-regulated photoproteins - aequorin, mitrocomin, clytin and obelins from Obelia longissima and Obelia geniculata is compared. Along with bioluminescence spectra, kinetics of light emission reactions and sensitivities to calcium, these photoproteins also differ in specific activities and consequently in quantum yields of biox02luminescent reactions. The highest specific activities are found for obelins and mitrocomin, whereas those of aequorin and clytin are lower
-
-
?
[apoaequorin] + coelenterazine + O2 + 3 Ca2+
[excited state blue fluorescent protein] + CO2
-
-
-
?
[apoaequorin] + coelenterazine + O2 + 3 Ca2+
[excited state blue fluorescent protein] + CO2
the reaction mechanism of the bioluminescent protein mnemiopsin1 is revealed by X-ray crystallography and QM/MM simulations. A water molecule in the coelenteramide binding cavity is identified that forms a hydrogen bond with the amide nitrogen atom of coelenteramide, which, in turn, is hydrogen-bonded via another water molecule to Tyr-131. This observation supports the hypothesis that the function of the coelenteramide-bound water molecule is to catalyze the 2-hydroperoxycoelenterazine decarboxylation reaction by protonation of a dioxetanone anion, thereby triggering the bioluminescence reaction
-
-
?
[apoaequorin] + coelenterazine + O2 + 3 Ca2+
[excited state blue fluorescent protein] + CO2
-
-
-
?
[apoaequorin] + coelenterazine + O2 + 3 Ca2+
[excited state blue fluorescent protein] + CO2
the specific bioluminescence activities of five recombinant hydromedusan Ca2+-regulated photoproteins - aequorin, mitrocomin, clytin and obelins from Obelia longissima and Obelia geniculata is compared. Along with bioluminescence spectra, kinetics of light emission reactions and sensitivities to calcium, these photoproteins also differ in specific activities and consequently in quantum yields of biox02luminescent reactions. The highest specific activities are found for obelins and mitrocomin, whereas those of aequorin and clytin are lower
-
-
?
[apoaequorin] + coelenterazine + O2 + 3 Ca2+
[excited state blue fluorescent protein] + CO2
-
-
-
?
[apoaequorin] + coelenterazine + O2 + 3 Ca2+
[excited state blue fluorescent protein] + CO2
the specific bioluminescence activities of five recombinant hydromedusan Ca2+-regulated photoproteins - aequorin, mitrocomin, clytin and obelins from Obelia longissima and Obelia geniculata is compared. Along with bioluminescence spectra, kinetics of light emission reactions and sensitivities to calcium, these photoproteins also differ in specific activities and consequently in quantum yields of biox02luminescent reactions. The highest specific activities are found for obelins and mitrocomin, whereas those of aequorin and clytin are lower
-
-
?
additional information
?
-
aequorin exhibits an absorption near 454 nm. The native chromophore is Renilla luciferin or a nearly identical derivative. The binding of calcium ion to the photoprotein brings about a conformational change in the protein which results in the chromophore reacting with a protein side chain hydroperoxide to yield a protein bound luciferin hydroperoxide intermediate. This intermediate then decomposes to CO2 and an electronic excited state of the corresponding protein-oxyluciferin monoanion complex which leads to light emission
-
-
?
additional information
?
-
no substrates: bisdeoxycoelenterazine, C6-methoxycoelenterazine, e-coelenterazine
-
-
?
additional information
?
-
poor substrates: n-coelenterazine, bis-coelenterazine, methoxy-coelenterazine, e-coelenterazine
-
-
?
additional information
?
-
the luminescence peak of aequorin is found at 472 nm. In presence of high concentrations of green fluorescent protein, the peak shifts to 509 nm
-
-
?
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A123D
-
mutant shows Ca2+-dependent chemiluminescence
C145S
61% of wild-type activity
C145S/C152S
1% of wild-type activity
C145S/C152S/C180S
21% of wild-type activity. Contrary to wild-type, 49% residual activity in absence of 2-mercaptoethanol. The regeneration of the triple mutant aequorin is sharply inhibited by 2-mercaptoethanol
C145S/C180S
68% of wild-type activity. Contrary to wild-type, 28% residual activity in absence of 2-mercaptoethanol
C152S
46% of wild-type activity
C152S/C180S
17% of wild-type activity. Contrary to wild-type, 14% residual activity in absence of 2-mercaptoethanol
C180S
13% of wild-type activity
D119A
-
mutant is an active photoprotein, Ca2+ affinity is reduced by a factor of 20 compared to the wild type
D153G
shift of maximum luminescence to shorter wavelengths. t1/2 is decreased with respect to the half-life time of the native protein (0.7 s). Mutation results in a significant decrease in stability at 65°C
F149
residue participates in stabilization of the coelenterazine peroxide and the triggering of photon emission by linking the third EF-hand to Trp-129 and His-169 coelenterazine binding residues
H169A
1.1% of wild-type activity
H169F
modification leads to complete loss of activity
H169W
modification leads to complete loss of activity
H16A
26% of wild-type activity
H16F
0.1% of wild-type activity
H18A
20% of wild-type activity
H27A
70% of wild-type activity
H27N
18fold increase of wild-type activity
H27N/Q168R
13fold increase of wild-type activity
H27P
67% of wild-type activity
H58F
1.4% of wild-type activity
H58Y
15% of wild-type activity
K17R
13fold increase of wild-type activity
K17R/H27N/Q168R
11fold increase of wild-type activity
K17R/L170I
8fold increase of wild-type activity
K17R/N26D
14fold increase of wild-type activity
K17R/N26D/Q168R
14fold increase of wild-type activity
K17R/Q168R
25fold increase of wild-type activity
K30E
-
mutant shows Ca2+-dependent chemiluminescence
L170I
16fold increase of wild-type activity, an increase of the photoprotein lifetime at 37°C and increased thermostability
N26D
13fold increase of wild-type activity
N26D/Q168R
8fold increase of wild-type activity
Q168
residue participates in stabilization of the coelenterazine peroxide and the triggering of photon emission by linking the third EF-hand to Trp-129 and His-169 coelenterazine binding residues
Q168R
11fold increase of wild-type activity, increase of the photoprotein lifetime at 37°C and increased thermostablility
Q168R/L170I
mutant displays increased thermostablility
V25A
10fold increase of wild-type activity
V25I/L170I
24fold increase of wild-type activity
V25I/Q168R
20fold increase of wild-type activity
W86F
shift of maximum luminescence to shorter wavelengths. The single mutant reaches the highest stability against thermal shock
W86F/D153G
decreased t1/2-value. Maximum emission spectrum at 401 nm. Mutation results in a significant decrease in stability at 65°C
Y82F/D153G
decreased t1/2-value. Maximum emission spectrum at 478 nm
Y82F/W86F
maximum emission spectrum at 400 nm. Y82F mutation results in shift of emission to longer wavelength, while the W86F mutation shifts the emission to shorter wavelengths. Compared to wild type aequorin, the Y82F/W86F variant displays a 2fold increase of light half-life. Mutation results in a significant decrease in stability at 65°C
E50G
the luminescence activity of the variant is about 17times greater than that of wild-type photoprotein. The activity of E50G variant increases as a result of more flexibility that is brought about by Gly essential for adopting the correct conformation for functional activity. In comparison with wild-type protein, the variant shows higher optimum temperature and calcium sensitivity as well as slower rate of luminesx02cence decay
E50G/D47N
mutation in loop I of mnemiopsin 2 leads to some conformational alterations in the secondary and tertiary structures which affect both the interaction of the photoprotein with the substrate and Ca2+ coordination
E50G/E53T
mutation in loop I of mnemiopsin 2 leads to some conformational alterations in the secondary and tertiary structures which affect both the interaction of the photoprotein with the substrate and Ca2+ coordination
F88H
mutation shifts the bioluminescence maximum from 482 nm for wild-type to 459 nm. 105% of wild-type bioluminescence yield
F88R
mutation shifts the bioluminescence maximum from 482 nm for wild-type to 474 nm. 99% of wild-type bioluminescence yield
F88W
mutation shifts the bioluminescence maximum from 482 nm for wild-type to 477 nm. 100% of wild-type bioluminescence yield
F88Y
mutation shifts the bioluminescence maximum from 482 nm for wild-type to 453 nm. 100% of wild-type bioluminescence yield
Y82F
mutation leads to removal of a H-bond from Tyr82 to the bound coelenteramide, and shifts its bioluminescence from 469 nm for wild-type to 501 nm. Mutant is stable with good activity and expressible in mammalian cells
Y82F
mutation shifts the peak towards longer wavelengths. Increased half time of initial light by 3.6 s. Mutation results in a significant decrease in stability at 65°C
additional information
mutation of all 3 Cys resiudes to Ser. Cys-free aequorin displays a two-fold lower specific bioluminescence activity but preserves similar activation properties and light emission kinetics compared to the wild-type aequorin. Mutant aequorin shows increased conformational flexibility
additional information
mutations with increased luminescence intensity neighbor the His-16 or His-169 coelenterazine binding residues or are located in the first EF-hand
additional information
replacement of the loop sequence of EF-hand I with other known loop sequences of Ca2+-binding proteins. Mutants replaced with the EF-hand I and EF-hand III from photoproteins show sufficient luminescence activity, but mutants replaced by EF-hands from Renilla luciferin-binding protein and calmodulin do not. The Ca2+-binding affinity to aequorin is reduced by a positive charge at the second position of the canonical EF-hand motif sequence
additional information
the C-terminal proline residue of aequorin is essential for the long-term stability of the bound coelenterazine. Aequorin lacking the proline residue has only 1% of the specific activity of the wild-type after 2 h, and is virtually inactive after 18 h. Replacement of the C-terminal proline residue with histidine or glutamic acid decreases the specific activity to 10 and 190% of that of the wild-type respectively, these variants show half-lives of 2.4 h and 2.3 h, respectively
additional information
mutation of all 5 Cys resiudes to Ser. Cys-free obelin retains only about 10% of the bioluminescence activity of wild-type obelin and binds coelenterazine and forms active photoprotein much less effectively. The mutation drastically changes the bioluminescence kinetics of obelin completely eliminating a fast component from the light signal decay curve. Replacement of Cys residues increases conformational flexibility
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Galactose-dependent expression of the recombinant Ca2(+)-binding photoprotein aequorin in yeast
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Aequorea victoria (P02592)
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19
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