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Information on EC 1.13.12.13 - Oplophorus-luciferin 2-monooxygenase
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1.13.12.13 Oplophorus-luciferin 2-monooxygenaseIUBMB Comments
The luciferase from the deep sea shrimp Oplophorus gracilirostris is a complex composed of more than one protein. The enzyme's specificity is quite broad, with both coelenterazine and bisdeoxycoelenterazine being good substrates.
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Word Map
- 1.13.12.13
-
bioluminescence
-
luminescence
- firefly
- luciferases
- gracilirostris
-
nanobit
- furimazine
-
lgbit
- renilla
-
brightest
- coelenterazine
- gaussia
- molecular biology
The enzyme appears in viruses and cellular organisms
Synonyms
nanoluc, nanokaz, cxxc-oluc, 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
NanoLuc
Oplophorus luciferase
Oplophorus luciferase
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Oplophorus luciferin + O2 = oxidized Oplophorus luciferin + CO2 + hnu
-
-
-
-
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SYSTEMATIC NAME
IUBMB Comments
Oplophorus-luciferin:oxygen 2-oxidoreductase (decarboxylating)
The luciferase from the deep sea shrimp Oplophorus gracilirostris is a complex composed of more than one protein. The enzyme's specificity is quite broad, with both coelenterazine and bisdeoxycoelenterazine being good substrates.
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
3-hydroxy-2-methylimidazol[1,2-a]pyridine + O2
oxidized 3-hydroxy-2-methylimidazol[1,2-a]pyridine + CO2 + hn
-
-
-
-
?
3iso-coelenterazine + O2
oxidized 3iso-coelenterazine + CO2 + hn
-
luminescence intesity (Imax): 78.2%
-
-
?
3me-coelenterazine + O2
oxidized 3me-coelenterazine + CO2 + hn
-
luminescence intesity (Imax): 80%
-
-
?
3meo-coelenterazine + O2
oxidized 3meo-coelenterazine + CO2 + hn
-
luminescence intesity (Imax): 189%
-
-
?
6h-coelenterazine + O2
oxidized 6h-coelenterazine + CO2 + hnu
-
luminescence intensity (Imax): 0.8
-
-
?
6h-f-coelenterazine + O2
oxidized 6h-f-coelenterazine + CO2 + hnu
-
luminescence intensity (Imax): 10.1
-
-
?
alphameh-coelenterazine + O2
oxidized alphameh-coelenterazine + CO2 + hn
-
luminescence intesity (Imax): 15.7%
-
-
?
bis-coelenterazine + O2
oxidized bis-coelenterazine + CO2 + hnu
-
luminescence intensity (Imax): 10.3
-
-
?
bisdeoxycoelenterazine + O2
oxidized bisdeoxycoelenterazine + CO2 + hn
-
-
-
-
?
bisdeoxycoelenterazine + O2
oxidized bisdeoxycoelenterazine + CO2 + hnu
-
native enzyme, 79%, catalytic subunit 19kOLase, 114% of the activity with coelenterazine, respectively
-
-
?
cf3-coelenterazine + O2
oxidized cf3-coelenterazine + CO2 + hn
-
luminescence intesity (Imax): 49.5%
-
-
?
et-coelenterazine + O2
oxidized et-coelenterazine + CO2 + hn
-
luminescence intesity (Imax): 21.5%
-
-
?
h-coelenterazine + O2
oxidized h-coelenterazine + CO2 + hn
-
luminescence intesity (Imax): 68.4%
-
-
?
i-coelenterazine + O2
oxidized i-coelenterazine + CO2 + hn
-
luminescence intesity (Imax): 32.3%
-
-
?
me-coelenterazine + O2
oxidized me-coelenterazine + CO2 + hn
-
luminescence intesity (Imax): 46.6%
-
-
?
meo-coelenterazine + O2
oxidized meo-coelenterazine + CO2 + hn
-
luminescence intesity (Imax): 68.1%
-
-
?
coelenterazine + O2
oxidized coelenterazine + CO2 + hn
-
-
-
-
?
coelenterazine + O2
oxidized coelenterazine + CO2 + hn
-
luminescence intensity (Imax): 1.0
-
-
?
coelenterazine + O2
oxidized coelenterazine + CO2 + hn
-
luminescence intesity (Imax): 100%
-
-
?
f-coelenterazine + O2
oxidized f-coelenterazine + CO2 + hnu
-
native enzyme, 26%, catalytic subunit 19kOLase, 80% of the activity with coelenterazine, respectively
-
-
?
f-coelenterazine + O2
oxidized f-coelenterazine + CO2 + hnu
-
luminescence intensity (Imax): 19.5
-
-
?
h-coelenterazine + O2
oxidized h-coelenterazine + CO2 + hnu
-
native enzyme, 97%, catalytic subunit 19kOLase, 58% of the activity with coelenterazine, respcetively
-
-
?
h-coelenterazine + O2
oxidized h-coelenterazine + CO2 + hnu
-
luminescence intensity (Imax): 17
-
-
?
Oplophorus luciferin + O2
oxidized Oplophorus luciferin + CO2 + hv
-
-
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
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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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
additional information
?
-
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
-
-
?
Oplophorus luciferin + O2
oxidized Oplophorus luciferin + CO2 + hv
-
-
-
-
?
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2-[(5-ethylfuran-2-yl)methyl]-8-[(2-fluorophenyl)methyl]-6-phenylimidazo[1,2-a]pyrazin-3(7H)-one
Q9GV45; Q9GV46
-
-
2-[(5-ethylfuran-2-yl)methyl]-8-[(3-fluorophenyl)methyl]-6-phenylimidazo[1,2-a]pyrazin-3(7H)-one
Q9GV45; Q9GV46
-
-
2-[(5-methylfuran-2-yl)methyl]-8-[(3-fluorophenyl)methyl]-6-phenylimidazo[1,2-a]pyrazin-3(7H)-one
Q9GV45; Q9GV46
-
-
6-(2-fluorophenyl)-8-[(4-fluorophenyl)methyl]-2-[(5-methylfuran-2-yl)methyl]imidazo[1,2-a]pyrazin-3(7H)-one
Q9GV45; Q9GV46
-
-
8-benzyl-2-[(furan-2-yl)methyl]-6-(3-hydroxyphenyl)imidazo[1,2-a]pyrazin-3(7H)-one
Q9GV45; Q9GV46
-
-
8-benzyl-2-[[3-(furan-2-yl)phenyl]methyl]-6-(4-hydroxyphenyl)imidazo[1,2-a]pyrazin-3(7H)-one
Q9GV45; Q9GV46
-
-
8-benzyl-6-(3-hydroxyphenyl)-2-[(4-hydroxyphenyl)methyl]imidazo[1,2-a]pyrazin-3(7H)-one
Q9GV45; Q9GV46
-
-
8-benzyl-6-(4-hydroxyphenyl)-2-[(5-methylfuran-2-yl)methyl]imidazo[1,2-a]pyrazin-3(7H)-one
Q9GV45; Q9GV46
-
-
8-[(2,3-difluorophenyl)methyl]-2-[(5-methylfuran-2-yl)methyl]-6-phenylimidazo[1,2-a]pyrazin-3(7H)-one
Q9GV45; Q9GV46
-
-
8-[(2-fluorophenyl)methyl]-2-[(5-methylfuran-2-yl)methyl]-6-phenylimidazo[1,2-a]pyrazin-3(7H)-one
Q9GV45; Q9GV46
-
-
8-[(3,5-difluorophenyl)methyl]-2-[(5-methylfuran-2-yl)methyl]-6-phenylimidazo[1,2-a]pyrazin-3(7H)-one
Q9GV45; Q9GV46
-
-
8-[(3,5-difluorophenyl)methyl]-2-[(furan-2-yl)methyl]-6-phenylimidazo[1,2-a]pyrazin-3(7H)-one
Q9GV45; Q9GV46
-
-
iodoacetamide
-
1 mM, catalytic subunit kOLase, 50% residual activity, native enzyme, 80% residual activity
N-ethylmaleimide
-
0.1 mM, catalytic subunit kOLase, 1% residual activity, native enzyme, 81% residual activity
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Amyotrophic Lateral Sclerosis
A highly sensitive assay of IRE1 activity using the small luciferase NanoLuc: Evaluation of ALS-related genetic and pathological factors.
Amyotrophic Lateral Sclerosis
SOD1 dimerization monitoring using a novel split NanoLuc, NanoBit.
Arthritis
Bioluminescent Ross River Virus Allows Live Monitoring of Acute and Long-Term Alphaviral Infection by In Vivo Imaging.
Border Disease
Development of a High-Throughput Serum Neutralization Test Using Recombinant Pestiviruses Possessing a Small Reporter Tag.
Brain Neoplasms
Detection of Brain Tumors and Systemic Metastases Using NanoLuc and Fluc for Dual Reporter Imaging.
Bronchitis
Development of HiBiT-Tagged Recombinant Infectious Bronchitis Coronavirus for Efficient in vitro and in vivo Viral Quantification.
Carcinogenesis
A kinome-wide screen using a NanoLuc LATS luminescent biosensor identifies ALK as a novel regulator of the Hippo pathway in tumorigenesis and immune evasion.
Carcinoma, Hepatocellular
Apaf1 nanoLuc biosensors identified lentinan as a potent synergizer of cisplatin in targeting hepatocellular carcinoma cells.
Carcinoma, Hepatocellular
Novel reporter system to monitor early stages of the hepatitis B virus life cycle.
Cholangiocarcinoma
Discovery of a chemical compound that suppresses expression of BEX2, a dormant cancer stem cell-related protein.
Classical Swine Fever
Development of a High-Throughput Serum Neutralization Test Using Recombinant Pestiviruses Possessing a Small Reporter Tag.
Colonic Neoplasms
Using ?-Lactamase and NanoLuc Luciferase Reporter Gene Assays to Identify Inhibitors of the HIF-1 Signaling Pathway.
Cysts
Methionyl-tRNA synthetase inhibitor has potent in vivo activity in a novel Giardia lamblia luciferase murine infection model.
Dermatitis, Phototoxic
Phototoxicity of flavoprotein miniSOG induced by bioluminescence resonance energy transfer in genetically encoded system NanoLuc-miniSOG is comparable with its LED-excited phototoxicity.
Distemper
Recovery of NanoLuc Luciferase-Tagged Canine Distemper Virus for Facilitating Rapid Screening of Antivirals in vitro.
Fragile X Syndrome
One-Step Generation of Seamless Luciferase Gene Knockin Using CRISPR/Cas9 Genome Editing in Human Pluripotent Stem Cells.
Glioblastoma
Detection of Brain Tumors and Systemic Metastases Using NanoLuc and Fluc for Dual Reporter Imaging.
Hepatitis B
Novel reporter system to monitor early stages of the hepatitis B virus life cycle.
Infections
A sensitive and reproducible cell-based assay via secNanoLuc to detect neutralizing antibody against adeno-associated virus vector capsid.
Infections
Generation of recombinant rabies viruses encoding NanoLuc luciferase for antiviral activity assays.
Infections
Identification of KX2-391 as an inhibitor of HBV transcription by a recombinant HBV-based screening assay.
Infections
In Vivo Live Imaging of Oncolytic Mammalian Orthoreovirus Expressing NanoLuc Luciferase in Tumor Xenograft Mice.
Infections
NanoBiT System and Hydrofurimazine for Optimized Detection of Viral Infection in Mice-A Novel in Vivo Imaging Platform.
Infections
Nanoluciferase-Based Method for Detecting Gene Expression in Caenorhabditis elegans.
Infections
The Vaginal Acquisition and Dissemination of HIV-1 Infection in a Novel Transgenic Mouse Model Is Facilitated by Coinfection with Herpes Simplex Virus 2 and Is Inhibited by Microbicide Treatment.
Influenza, Human
A Luciferase-fluorescent Reporter Influenza Virus for Live Imaging and Quantification of Viral Infection.
Influenza, Human
Visualizing real-time influenza virus infection, transmission and protection in ferrets.
Leishmaniasis, Cutaneous
Evaluation of NanoLuc, RedLuc and Luc2 as bioluminescent reporters in a cutaneous leishmaniasis model.
Leukemia
Nanoluciferase as a novel quantitative protein fusion tag: Application for overexpression and bioluminescent receptor-binding assays of human leukemia inhibitory factor.
Melanoma, Experimental
The influences of a novel anti-adhesion device, thermally cross-linked gelatin film on peritoneal dissemination of tumor cells: The in vitro and in vivo experiments using murine carcinomatous peritonitis models.
Metrorrhagia
Development of a Paper-Based Luminescence Bioassay for Therapeutic Monitoring of Aminoglycosides: a Proof-of-Concept Study.
Neoplasm Metastasis
Detection of Brain Tumors and Systemic Metastases Using NanoLuc and Fluc for Dual Reporter Imaging.
Neoplasms
A 3D Heterotypic Multicellular Tumor Spheroid Assay Platform to Discriminate Drug Effects on Stroma versus Cancer Cells.
Neoplasms
A kinome-wide screen using a NanoLuc LATS luminescent biosensor identifies ALK as a novel regulator of the Hippo pathway in tumorigenesis and immune evasion.
Neoplasms
Detection of Brain Tumors and Systemic Metastases Using NanoLuc and Fluc for Dual Reporter Imaging.
Neoplasms
Evaluation of chemical chaperones based on the monitoring of Bip promoter activity and visualization of extracellular vesicles by real-time bioluminescence imaging.
Neoplasms
Flavoprotein miniSOG Cytotoxisity Can Be Induced By Bioluminescence Resonance Energy Transfer.
Neoplasms
In Vivo Live Imaging of Oncolytic Mammalian Orthoreovirus Expressing NanoLuc Luciferase in Tumor Xenograft Mice.
Neoplasms
pHLuc, a Ratiometric Luminescent Reporter for in vivo Monitoring of Tumor Acidosis.
Neoplasms
Phototoxicity of flavoprotein miniSOG induced by bioluminescence resonance energy transfer in genetically encoded system NanoLuc-miniSOG is comparable with its LED-excited phototoxicity.
Neoplasms
The influences of a novel anti-adhesion device, thermally cross-linked gelatin film on peritoneal dissemination of tumor cells: The in vitro and in vivo experiments using murine carcinomatous peritonitis models.
Neuroblastoma
Molecular Function Analysis of Rabies Virus RNA Polymerase L Protein by Using an L Gene-Deficient Virus.
Pseudorabies
A NanoLuc Luciferase Reporter Pseudorabies Virus for Live Imaging and Quantification of Viral Infection.
Rabies
Generation of recombinant rabies viruses encoding NanoLuc luciferase for antiviral activity assays.
Uterine Cervical Neoplasms
Using ?-Lactamase and NanoLuc Luciferase Reporter Gene Assays to Identify Inhibitors of the HIF-1 Signaling Pathway.
Virus Diseases
A NanoLuc Luciferase Reporter Pseudorabies Virus for Live Imaging and Quantification of Viral Infection.
Virus Diseases
Generation of recombinant rabies viruses encoding NanoLuc luciferase for antiviral activity assays.
Virus Diseases
Highly sensitive real-time in vivo imaging of an influenza reporter virus reveals dynamics of replication and spread.
Yellow Fever
Using recombination-dependent lethal mutations to stabilize reporter flaviviruses for rapid serodiagnosis and drug discovery.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0013
bis-deoxycoelenterazine
-
pH 7.6, catalytic subunit 19kOLase
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.115
2,8-dibenzyl-6-phenylimidazo[1,2-a]pyrazin-3(7H)-one
Q9GV45; Q9GV46
pH and temperature not specified in the publication
-
0.095
2-[(5-ethylfuran-2-yl)methyl]-8-[(2-fluorophenyl)methyl]-6-phenylimidazo[1,2-a]pyrazin-3(7H)-one
Q9GV45; Q9GV46
pH and temperature not specified in the publication
-
0.06
2-[(5-ethylfuran-2-yl)methyl]-8-[(3-fluorophenyl)methyl]-6-phenylimidazo[1,2-a]pyrazin-3(7H)-one
Q9GV45; Q9GV46
pH and temperature not specified in the publication
-
0.04
2-[(5-methylfuran-2-yl)methyl]-8-[(3-fluorophenyl)methyl]-6-phenylimidazo[1,2-a]pyrazin-3(7H)-one
Q9GV45; Q9GV46
pH and temperature not specified in the publication
-
0.063
6-(2-fluorophenyl)-8-[(4-fluorophenyl)methyl]-2-[(5-methylfuran-2-yl)methyl]imidazo[1,2-a]pyrazin-3(7H)-one
Q9GV45; Q9GV46
pH and temperature not specified in the publication
-
0.058
8-benzyl-2-[(2-fluorophenyl)methyl]-6-phenylimidazo[1,2-a]pyrazin-3(7H)-one
Q9GV45; Q9GV46
pH and temperature not specified in the publication
-
0.167
8-benzyl-2-[(3-methylphenyl)methyl]-6-phenylimidazo[1,2-a]pyrazin-3(7H)-one
Q9GV45; Q9GV46
pH and temperature not specified in the publication
-
0.084
8-benzyl-2-[(furan-2-yl)methyl]-6-(3-hydroxyphenyl)imidazo[1,2-a]pyrazin-3(7H)-one
Q9GV45; Q9GV46
pH and temperature not specified in the publication
-
0.109
8-benzyl-2-[(furan-2-yl)methyl]-6-phenylimidazo[1,2-a]pyrazin-3(7H)-one
Q9GV45; Q9GV46
pH and temperature not specified in the publication
-
0.101
8-benzyl-2-[[3-(furan-2-yl)phenyl]methyl]-6-(4-hydroxyphenyl)imidazo[1,2-a]pyrazin-3(7H)-one
Q9GV45; Q9GV46
pH and temperature not specified in the publication
-
0.035
8-benzyl-6-(3-hydroxyphenyl)-2-[(4-hydroxyphenyl)methyl]imidazo[1,2-a]pyrazin-3(7H)-one
Q9GV45; Q9GV46
pH and temperature not specified in the publication
-
0.121
8-benzyl-6-(4-hydroxyphenyl)-2-[(5-methylfuran-2-yl)methyl]imidazo[1,2-a]pyrazin-3(7H)-one
Q9GV45; Q9GV46
pH and temperature not specified in the publication
-
0.08
8-[(2,3-difluorophenyl)methyl]-2-[(5-methylfuran-2-yl)methyl]-6-phenylimidazo[1,2-a]pyrazin-3(7H)-one
Q9GV45; Q9GV46
pH and temperature not specified in the publication
-
0.06
8-[(2-fluorophenyl)methyl]-2-[(5-methylfuran-2-yl)methyl]-6-phenylimidazo[1,2-a]pyrazin-3(7H)-one
Q9GV45; Q9GV46
pH and temperature not specified in the publication
-
0.064
8-[(3,5-difluorophenyl)methyl]-2-[(5-methylfuran-2-yl)methyl]-6-phenylimidazo[1,2-a]pyrazin-3(7H)-one
Q9GV45; Q9GV46
pH and temperature not specified in the publication
-
0.14
8-[(3,5-difluorophenyl)methyl]-2-[(furan-2-yl)methyl]-6-phenylimidazo[1,2-a]pyrazin-3(7H)-one
Q9GV45; Q9GV46
pH and temperature not specified in the publication
-
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
0.1% luminescence activity expressed in Escherichia coli cells using pCold-ZZ-KAZ vector (with IgG-binding domain of protein A), precipitate
additional information
100% luminescence activity expressed in Escherichia coli cells using pCold-ZZ-KAZ vector (with IgG-binding domain of protein A), supernatant
additional information
2.7% luminescence activity expressed in Escherichia coli cells using pCold-KAZ vector (without IgG-binding domain of protein A), supernatant
additional information
4.7% luminescence activity expressed in Escherichia coli cells using pCold-KAZ vector (without IgG-binding domain of protein A), precipitate
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.6
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
Q9GV45; Q9GV46
the enzyme is a member of the coelenterazine-utilizing luciferases such as Renilla luciferase and Gaussia luciferase
malfunction
Q9GV45; Q9GV46
recombinant 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
physiological function
Q9GV45; Q9GV46
the secreted luciferase of the deep-sea shrimp Oplophorus gracilirostris catalyzes the oxidation of coelenterazine to emit blue light (lambda_max = 460 nm)
additional information
Q9GV45; Q9GV46
the coelenterazine-binding site and the catalytic site for the luminescence reaction might be in a central cavity of the beta-barrel structure of the catalytic subunit KAZ
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). LUCI_OPLGR
196
0
21533
Swiss-Prot
Secretory Pathway (Reliability: 1)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
heterooligomer
Q9GV45; Q9GV46
x * 19000, catalytic subunit, + x * 35000, noncatalytic subunit, SDS-PAGE
additional information
additional information
-
enzyme consists of 19 and 35 kDa proteins. 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
additional information
Q9GV45; Q9GV46
the structure of the mutant catalytic subunit nanoKAZ consists of 11 antiparallel beta-strands forming a beta-barrel that is capped by 4 short alpha-helices. The coelenterazine-binding site and the catalytic site for the luminescence reaction might be in a central cavity of the beta-barrel structure of the catalytic subunit KAZ
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified mutated 19 kDa protein nanoKAZ, X-ray diffraction structure determination and analysis at 1.71-2.3.A resolution and dialysis
Q9GV45; Q9GV46
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
-
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
-
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
-
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
N166R
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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
additional information
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
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
-
enzyme retains activity in culture medium for more than 15 h at 37°C
55
-
enzyme shows high physical stability, retaining activity with incubation up to 55°C
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
form inclusion bodies of recombinant Escherichia coli, solubilization with 6 M urea
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recombinant His-tagged catalytic subunit mutant nanoKAZ from Escherichia coli strain BL21 by nickel affinity chromatography and dialysis, wild-typeKAZ is purified from inclusion bodies using 6 M urea-nickel chelate affinity column chromatography
Q9GV45; Q9GV46
recombinant His-tagged catalytic wild-type and mutant enzymes and catalytic subunits from Escherichia coli by nickel affinity chromatgraphy
Q9GV45; Q9GV46
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
construction of a cold induced expression vector in Escherichia coli cells that consists of a histidine tag sequence for nickel chelate affinity purification, IgG-binding domain of protein A (ZZ-domain) and the multiple cloning sites, the role of ZZ-domain as a solubilizing partner at 15°C is demonstrated by expressing the imidazopyrazinone-type luciferase of Oplophorus
recombinant expression and secretion of 19 kDa catalytic subunit mutant nanoKAZ from CHO-K1 cells. 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. Recombinant expression of His-tagged wild-type and mutant KAZs in Escherichia coli. The secreted proteins form aggregates
Q9GV45; Q9GV46
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
Q9GV45; Q9GV46
recombinant expression of His-tagged 19 kDa catalytic subunit mutant nanoKAZ in Escherichia coli strain BL21. In bacterial cells, wild-type KAZ is mainly expressed as inclusion bodies
Q9GV45; Q9GV46
the catalytic domain of Oplophorus luciferase (19kOLase) is expressed in Escherichia coli cells using the cold-induced vectors of pCold-KAZ. Cold induction for Escherichia coli cells is carried out at 15°C
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the fused proteinof nanoKAZ with IgG-binding domain (ZZ domain) is expressed in the cytoplasm of Escherichia coli cells as a soluble form and purified. A secretory expression of nanoKAZ in CHO-K1 cells is performed using nanoKAZ fused with the signal peptide sequence of Gaussia luciferase
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RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
wild-typeKAZ is purified from inclusion bodies using 6 M urea-nickel chelate affinity column chromatography
Q9GV45; Q9GV46
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