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
-
lgbit
- renilla
-
brightest
- coelenterazine
- gaussia
- molecular biology
Reaction
Synonyms
19kOLase, CXXC-Oluc, imidazopyrazinone-type luciferase, KAZ, luciferase, nanoKAZ, NanoLuc, Oluc-19, Oplophorus luciferase
ECTree
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Substrates Products
Substrates Products on EC 1.13.12.13 - Oplophorus-luciferin 2-monooxygenase
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REACTION DIAGRAM
3-hydroxy-2-methylimidazol[1,2-a]pyridine + O2
oxidized 3-hydroxy-2-methylimidazol[1,2-a]pyridine + CO2 + hn
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3iso-coelenterazine + O2
oxidized 3iso-coelenterazine + CO2 + hn
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luminescence intesity (Imax): 78.2%
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3me-coelenterazine + O2
oxidized 3me-coelenterazine + CO2 + hn
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luminescence intesity (Imax): 80%
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?
3meo-coelenterazine + O2
oxidized 3meo-coelenterazine + CO2 + hn
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luminescence intesity (Imax): 189%
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6h-coelenterazine + O2
oxidized 6h-coelenterazine + CO2 + hnu
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luminescence intensity (Imax): 0.8
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?
6h-f-coelenterazine + O2
oxidized 6h-f-coelenterazine + CO2 + hnu
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luminescence intensity (Imax): 10.1
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?
alphameh-coelenterazine + O2
oxidized alphameh-coelenterazine + CO2 + hn
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luminescence intesity (Imax): 15.7%
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?
bis-coelenterazine + O2
oxidized bis-coelenterazine + CO2 + hnu
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luminescence intensity (Imax): 10.3
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?
bisdeoxycoelenterazine + O2
oxidized bisdeoxycoelenterazine + CO2 + hn
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bisdeoxycoelenterazine + O2
oxidized bisdeoxycoelenterazine + CO2 + hnu
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native enzyme, 79%, catalytic subunit 19kOLase, 114% of the activity with coelenterazine, respectively
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cf3-coelenterazine + O2
oxidized cf3-coelenterazine + CO2 + hn
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luminescence intesity (Imax): 49.5%
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et-coelenterazine + O2
oxidized et-coelenterazine + CO2 + hn
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luminescence intesity (Imax): 21.5%
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h-coelenterazine + O2
oxidized h-coelenterazine + CO2 + hn
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luminescence intesity (Imax): 68.4%
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?
i-coelenterazine + O2
oxidized i-coelenterazine + CO2 + hn
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luminescence intesity (Imax): 32.3%
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me-coelenterazine + O2
oxidized me-coelenterazine + CO2 + hn
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luminescence intesity (Imax): 46.6%
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meo-coelenterazine + O2
oxidized meo-coelenterazine + CO2 + hn
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luminescence intesity (Imax): 68.1%
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oxidized coelenterazine + CO2 + hn
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coelenterazine + O2
oxidized coelenterazine + CO2 + hn
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luminescence intensity (Imax): 1.0
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coelenterazine + O2
oxidized coelenterazine + CO2 + hn
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luminescence intesity (Imax): 100%
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oxidized f-coelenterazine + CO2 + hnu
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native enzyme, 26%, catalytic subunit 19kOLase, 80% of the activity with coelenterazine, respectively
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f-coelenterazine + O2
oxidized f-coelenterazine + CO2 + hnu
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luminescence intensity (Imax): 19.5
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?
oxidized h-coelenterazine + CO2 + hnu
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native enzyme, 97%, catalytic subunit 19kOLase, 58% of the activity with coelenterazine, respcetively
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?
h-coelenterazine + O2
oxidized h-coelenterazine + CO2 + hnu
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luminescence intensity (Imax): 17
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Oplophorus luciferin + O2
oxidized Oplophorus luciferin + CO2 + hv
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luminescence intensity of the catalytic subunit 19kOLase alone is seven times lower for coelenterazine and three times lower for biscoelenterazine than that of native Oplophorus luciferase, respectively
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additional information
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Q9GV45; Q9GV46
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
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