1.13.12.13: Oplophorus-luciferin 2-monooxygenase
This is an abbreviated version!
For detailed information about Oplophorus-luciferin 2-monooxygenase, go to the full flat file.
Word Map on EC 1.13.12.13
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1.13.12.13
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bioluminescence
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luminescence
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firefly
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luciferases
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gracilirostris
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nanobit
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furimazine
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lgbit
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renilla
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brightest
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coelenterazine
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gaussia
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molecular biology
- 1.13.12.13
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bioluminescence
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luminescence
- firefly
- luciferases
- gracilirostris
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nanobit
- furimazine
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lgbit
- renilla
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brightest
- coelenterazine
- gaussia
- molecular biology
Reaction
Synonyms
19kOLase, CXXC-Oluc, imidazopyrazinone-type luciferase, KAZ, luciferase, nanoKAZ, NanoLuc, Oluc-19, Oplophorus luciferase
ECTree
Advanced search results
Engineering
Engineering on EC 1.13.12.13 - Oplophorus-luciferin 2-monooxygenase
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A33N
Q9GV45; Q9GV46
site-directed mutagenesis, mutation of the catalytic subunit, the mutant shows increased bioluminesce intensity compared to the wild-type
A4E
Q9GV45; Q9GV46
site-directed mutagenesis, mutation of the catalytic subunit, the mutant shows wild-type bioluminesce intensity
A4E/Q11R/A33K/V44I/A54F/P115E/Q124K/Y138I
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mutant is 29000fold brighter than mutant N166R. Western blot analysis shows that mutant A4E/Q11R/A33K/V44I/A54F/P115E/Q124K/Y138I is produced more efficiently than mutant N166R in cells. The increased expression is consistent with improved enzyme stability at 37°C, where the half-life of activity retention is increased 65fold over that of mutant N166R
A4E/Q11R/A33K/V44I/A54F/P115E/Q124K/Y138I/Q18L/F54I/F68Y/L72Q/M75K/I90V/L27V/K33N/K43R/Y68D
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mutant Nluc: Nluc paired with furimazine produces 2.5 millionfold brighter luminescence in mammalian cells relative to Oluc-19 with coelenterazine. The luminescence produced by Nluc decays with a half-life more than 2 h, significantly longer than for mutant A4E/Q11R/A33K/V44I/A54F/P115E/Q124K/Y138I. Nluc increased luminescence is gained mostly through improvements in protein stability, where Nluc shows markedly greater retention of activity in lysates following incubation at 37°C
A4E/Q11R/Q18L/L27V/A33N/K43R/V44I/A54I/F68D/L72Q/M75K/I90V/P115E/Q124K/Y138I/N166R
Q9GV45; Q9GV46
construction of mutant nanoKAZ, a mutant with 16 amino acid substitutions of the catalytic subunit, by site-directed mutagenesis, the mutant nanoKAZ lacks the amino-terminal signal peptide, crystal structure determination and analysis, structure-function relationship in nanoKAZ, overview. The truncation of 10 amino acid residues at N- and C-terminal regions of nanoKAZ causes a complete loss of luminescence activity. Both the alpha1-helix and beta11-strand in the nanoKAZ molecule might serve to stabilize the molecule, which is essential in catalyzing the luminescence reaction
A54I
Q9GV45; Q9GV46
site-directed mutagenesis, mutation of the catalytic subunit, the mutant shows increased bioluminesce intensity compared to the wild-type
A54I/Y138I
Q9GV45; Q9GV46
site-directed mutagenesis, mutation of the catalytic subunit, the mutant shows increased bioluminesce intensity compared to the wild-type
C164A
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mutation does not significantly affect catalytic activity of subunit kOLase
C164G
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mutation does not significantly affect catalytic activity of subunit kOLase
C164S
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mutation does not significantly affect catalytic activity of subunit kOLase
F68D
Q9GV45; Q9GV46
site-directed mutagenesis, mutation of the catalytic subunit, the mutant shows wild-type bioluminesce intensity
I90V
Q9GV45; Q9GV46
site-directed mutagenesis, mutation of the catalytic subunit, the mutant shows increased bioluminesce intensity compared to the wild-type
K43R
Q9GV45; Q9GV46
site-directed mutagenesis, mutation of the catalytic subunit, the mutant shows wild-type bioluminesce intensity
L27V
Q9GV45; Q9GV46
site-directed mutagenesis, mutation of the catalytic subunit, the mutant shows reduced bioluminesce intensity compared to the wild-type
L72Q
Q9GV45; Q9GV46
site-directed mutagenesis, mutation of the catalytic subunit, the mutant shows increased bioluminesce intensity compared to the wild-type
M75K
Q9GV45; Q9GV46
site-directed mutagenesis, mutation of the catalytic subunit, the mutant shows increased bioluminesce intensity compared to the wild-type
N166R
P115E
Q9GV45; Q9GV46
site-directed mutagenesis, mutation of the catalytic subunit, the mutant shows increased bioluminesce intensity compared to the wild-type
Q11R
Q9GV45; Q9GV46
site-directed mutagenesis, mutation of the catalytic subunit, the mutant shows increased bioluminesce intensity compared to the wild-type
Q124K
Q9GV45; Q9GV46
site-directed mutagenesis, mutation of the catalytic subunit, the mutant shows increased bioluminesce intensity compared to the wild-type
Q18L
Q9GV45; Q9GV46
site-directed mutagenesis, mutation of the catalytic subunit, the mutant shows wild-type bioluminesce intensity
V44I
Q9GV45; Q9GV46
site-directed mutagenesis, mutation of the catalytic subunit, the mutant shows increased bioluminesce intensity compared to the wild-type
V44I/A54I
Q9GV45; Q9GV46
site-directed mutagenesis, mutation of the catalytic subunit, the mutant shows the mutant shows increased bioluminesce intensity compared to the wild-type
V44I/A54I/Y138I
Q9GV45; Q9GV46
site-directed mutagenesis, mutation of the catalytic subunit, catalytic subunit mutant, that shows 7fold higher activity than 16-aa-mutant nanoKAZ using coelenterazine, but these substitutions does not stimulate protein secretion from mammalian cells, nanoKAZ possessing the signal peptide sequence of Gaussia luciferase for secretion expressed efficiently into the culture medium of CHO-K1 cells
V44I/Y138I
Q9GV45; Q9GV46
site-directed mutagenesis, mutation of the catalytic subunit, the mutant shows wild-type bioluminesce intensity
Y138I
Q9GV45; Q9GV46
site-directed mutagenesis, mutation of the catalytic subunit, the mutant shows increased bioluminesce intensity compared to the wild-type
additional information
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mutant shows 50% increased stability at 37°C and 3fold higher luminescence intensity
N166R
Q9GV45; Q9GV46
site-directed mutagenesis, mutation of the catalytic subunit, the mutant shows increased bioluminesce intensity compared to the wild-type
Q9GV45; Q9GV46
construction of mutant nanoKAZ, a mutant with 16 amino acid substitutions of the catalytic subunit. Mutant nanoKAZ lacks the amino-terminal signal peptide, is expressed in the cytoplasm, translocated to the cell membrane, and released into the culture medium through an endoplasmic reticulum-Golgi-independent pathway, Construction of other DELTA1-15 truncated mutants of the catalytic subunit KAZ, i.e. DN2T, DN3L, DN4E, DN5D, DN6F, DN7V, DN8G, DN9D, DN10W, DN15G, and DN20Q. The mutant enzyme activity is dependent on the mutation and the type of expression vector, overview. Secretory expression of nanoKAZ from mammalian cells in the absence of the N-terminal signal peptide
additional information
Q9GV45; Q9GV46
construction of mutant nanoKAZ, a mutant with 16 amino acid substitutions of the catalytic subunit. Secretory expression and luminescence activity of single amino acid substituted KAZ mutants in CHO-K1 cells, overview