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Literature summary for 1.13.12.13 extracted from

  • Inouye, S.; Sato, J.; Sahara-Miura, Y.; Yoshida, S.; Hosoya, T.
    Luminescence enhancement of the catalytic 19 kDa protein (KAZ) of Oplophorus luciferase by three amino acid substitutions (2014), Biochem. Biophys. Res. Commun., 445, 157-162 .
    View publication on PubMed
Search for more literature for 1.13.12.13

Cloned(Commentary)

Cloned (Comment) Organism
recombinant expression and secretion, using the signal peptide sequence of Gaussia luciferase, of catalytic 19 kDa protein KAZ of Oplophorus luciferase and its mutants in Escherichia coli and recombinant expression of His-tagged wild-type and mutant enzymes and KAZs in CHO-K1 cells Oplophorus gracilirostris

Protein Variants

Protein Variants Comment Organism
A33N site-directed mutagenesis, mutation of the catalytic subunit, the mutant shows increased bioluminesce intensity compared to the wild-type Oplophorus gracilirostris
A4E site-directed mutagenesis, mutation of the catalytic subunit, the mutant shows wild-type bioluminesce intensity Oplophorus gracilirostris
A54I site-directed mutagenesis, mutation of the catalytic subunit, the mutant shows increased bioluminesce intensity compared to the wild-type Oplophorus gracilirostris
A54I/Y138I site-directed mutagenesis, mutation of the catalytic subunit, the mutant shows increased bioluminesce intensity compared to the wild-type Oplophorus gracilirostris
F68D site-directed mutagenesis, mutation of the catalytic subunit, the mutant shows wild-type bioluminesce intensity Oplophorus gracilirostris
I90V site-directed mutagenesis, mutation of the catalytic subunit, the mutant shows increased bioluminesce intensity compared to the wild-type Oplophorus gracilirostris
K43R site-directed mutagenesis, mutation of the catalytic subunit, the mutant shows wild-type bioluminesce intensity Oplophorus gracilirostris
L27V site-directed mutagenesis, mutation of the catalytic subunit, the mutant shows reduced bioluminesce intensity compared to the wild-type Oplophorus gracilirostris
L72Q site-directed mutagenesis, mutation of the catalytic subunit, the mutant shows increased bioluminesce intensity compared to the wild-type Oplophorus gracilirostris
M75K site-directed mutagenesis, mutation of the catalytic subunit, the mutant shows increased bioluminesce intensity compared to the wild-type Oplophorus gracilirostris
additional information 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 Oplophorus gracilirostris
N166R site-directed mutagenesis, mutation of the catalytic subunit, the mutant shows increased bioluminesce intensity compared to the wild-type Oplophorus gracilirostris
P115E site-directed mutagenesis, mutation of the catalytic subunit, the mutant shows increased bioluminesce intensity compared to the wild-type Oplophorus gracilirostris
Q11R site-directed mutagenesis, mutation of the catalytic subunit, the mutant shows increased bioluminesce intensity compared to the wild-type Oplophorus gracilirostris
Q124K site-directed mutagenesis, mutation of the catalytic subunit, the mutant shows increased bioluminesce intensity compared to the wild-type Oplophorus gracilirostris
Q18L site-directed mutagenesis, mutation of the catalytic subunit, the mutant shows wild-type bioluminesce intensity Oplophorus gracilirostris
V44I site-directed mutagenesis, mutation of the catalytic subunit, the mutant shows increased bioluminesce intensity compared to the wild-type Oplophorus gracilirostris
V44I/A54I site-directed mutagenesis, mutation of the catalytic subunit, the mutant shows the mutant shows increased bioluminesce intensity compared to the wild-type Oplophorus gracilirostris
V44I/A54I/Y138I 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 Oplophorus gracilirostris
V44I/Y138I site-directed mutagenesis, mutation of the catalytic subunit, the mutant shows wild-type bioluminesce intensity Oplophorus gracilirostris
Y138I site-directed mutagenesis, mutation of the catalytic subunit, the mutant shows increased bioluminesce intensity compared to the wild-type Oplophorus gracilirostris

Localization

Localization Comment Organism GeneOntology No. Textmining
extracellular the enzyme is secreted Oplophorus gracilirostris
-
-

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
106000
-
 full-length enzyme Oplophorus gracilirostris

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
coelenterazine + O2 Oplophorus gracilirostris
-
 coelenteramide + CO2 + hv
-
 ?
additional information Oplophorus gracilirostris Oplophorus luciferase shows broad substrate specificities for various coelenterazine analogues, and the substrate specificity is distinct from other coelenterazine-type luciferases including Renilla and Gaussia luciferases and the Ca2+-binding photoprotein aequorin ?
-
 ?
Oplophorus luciferin + O2 Oplophorus gracilirostris
-
 oxidized Oplophorus luciferin + CO2 + hv
-
 ?

Organism

Organism UniProt Comment Textmining
Oplophorus gracilirostris Q9GV45 AND Q9GV46 catalytic and noncatalytic subunit
-

Purification (Commentary)

Purification (Comment) Organism
recombinant His-tagged catalytic wild-type and mutant enzymes and catalytic subunits from Escherichia coli by nickel affinity chromatgraphy Oplophorus gracilirostris

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
6h-coelenterazine + O2
-
 Oplophorus gracilirostris ? + CO2 + hv
-
 ?
6h-f-coelenterazine + O2
-
 Oplophorus gracilirostris ? + CO2 + hv
-
 ?
bis-coelenterazine + O2
-
 Oplophorus gracilirostris ? + CO2 + hv
-
 ?
coelenterazine + O2
-
 Oplophorus gracilirostris coelenteramide + CO2 + hv
-
 ?
f-coelenterazine + O2
-
 Oplophorus gracilirostris ? + CO2 + hv
-
 ?
furimazine + O2
-
 Oplophorus gracilirostris ? + CO2 + hv
-
 ?
h-coelenterazine + O2
-
 Oplophorus gracilirostris ? + CO2 + hv
-
 ?
additional information Oplophorus luciferase shows broad substrate specificities for various coelenterazine analogues, and the substrate specificity is distinct from other coelenterazine-type luciferases including Renilla and Gaussia luciferases and the Ca2+-binding photoprotein aequorin Oplophorus gracilirostris ?
-
 ?
Oplophorus luciferin + O2
-
 Oplophorus gracilirostris oxidized Oplophorus luciferin + CO2 + hv
-
 ?

Subunits

Subunits Comment Organism
heterooligomer x * 19000, catalytic subunit, + x * 35000, noncatalytic subunit, SDS-PAGE Oplophorus gracilirostris

Synonyms

Synonyms Comment Organism
KAZ catalytic enzyme subunit Oplophorus gracilirostris
Oplophorus luciferase
-
 Oplophorus gracilirostris

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.6
-
 assay at Oplophorus gracilirostris

General Information

General Information Comment Organism
physiological function the secreted luciferase of the deep-sea shrimp Oplophorus gracilirostris catalyzes the oxidation of coelenterazine to emit blue light (lambda_max = 460 nm) Oplophorus gracilirostris