Information on EC 1.13.12.13 - Oplophorus-luciferin 2-monooxygenase

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The expected taxonomic range for this enzyme is: Coelomata

EC NUMBER
COMMENTARY
1.13.12.13
-
RECOMMENDED NAME
GeneOntology No.
Oplophorus-luciferin 2-monooxygenase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
Oplophorus luciferin + O2 = oxidized Oplophorus luciferin + CO2 + hnu
show the reaction diagram
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
Oplophorus-luciferin:oxygen 2-oxidoreductase (decarboxylating)
The luciferase from the deep sea shrimp Oplophorus gracilorostris is a complex composed of more than one protein. The enzyme's specificity is quite broad, with both coelenterazine and bisdeoxycoelenterazine being good substrates.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
imidazopyrazinone-type luciferase
Q9GV45
-
Oplophorus luciferase
-
-
-
-
Oplophorus luciferase
Q9GV45
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
deep-sea shrimp
-
-
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
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
show the reaction diagram
-
-
-
-
?
bisdeoxycoelenterazine + O2
oxidized bisdeoxycoelenterazine + CO2 + hn
show the reaction diagram
-
-
-
-
?
bisdeoxycoelenterazine + O2
oxidized bisdeoxycoelenterazine + CO2 + hnu
show the reaction diagram
-
native enzyme, 79%, catalytic subunit 19kOLase, 114% of the activity with coelenterazine, respectively
-
-
?
coelenterazine + O2
oxidized coelenterazine + CO2 + hn
show the reaction diagram
-
-
-
-
?
coelenterazine + O2
oxidized coelenterazine + CO2 + hnu
show the reaction diagram
-
-
-
-
?
f-coelenterazine + O2
oxidized f-coelenterazine + CO2 + hnu
show the reaction diagram
-
native enzyme, 26%, catalytic subunit 19kOLase, 80% of the activity with coelenterazine, respectively
-
-
?
Oplophorus luciferin + O2
oxidized Oplophorus luciferin + CO2 + hv
show the reaction diagram
-
-
-
-
?
h-coelenterazine + O2
oxidized h-coelenterazine + CO2 + hnu
show the reaction diagram
-
native enzyme, 97%, catalytic subunit 19kOLase, 58% of the activity with coelenterazine, respcetively
-
-
?
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
-
-
-
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
Cu2+
-
0.001 mM, 98% inhibition
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
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
4e-05
-
bis-deoxycoelenterazine
-
pH 7.6, native enzymee
0.0013
-
bis-deoxycoelenterazine
-
pH 7.6, catalytic subunit 19kOLase
0.00014
-
coelenterazine
-
pH 7.6, native enzyme
0.0037
-
coelenterazine
-
pH 7.6, catalytic subunit 19kOLase
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
additional information
-
Q9GV45
0.1% luminescence activity expressed in Escherichia coli cells using pCold-ZZ-KAZ vector (with IgG-binding domain of protein A), precipitate; 100% luminescence activity expressed in Escherichia coli cells using pCold-ZZ-KAZ vector (with IgG-binding domain of protein A), supernatant; 2.7% luminescence activity expressed in Escherichia coli cells using pCold-KAZ vector (without IgG-binding domain of protein A), supernatant; 4.7% luminescence activity expressed in Escherichia coli cells using pCold-KAZ vector (without IgG-binding domain of protein A), precipitate
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
7.6
-
Q9GV45
assay at
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
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
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
form inclusion bodies of recombinant Escherichia coli, solubilization with 6 M urea
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
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
Q9GV45
expression of 19 kDa subunit 19kOLase in Escherichia coli
-
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
C164A
-
mutation does not significantly affect catalytic activity of subunit kOLase
C164G
-
mutation does not significantly affect catalytic activity of subunit kOLase
C164S
-
mutation does not significantly affect catalytic activity of subunit kOLase
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
molecular biology
Q9GV45
useful reporter protein in various assay systems including reporter assays and immunoassays