Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 1.13.12.13 extracted from

  • Inouye, S.; Sasaki, S.
    Overexpression, purification and characterization of the catalytic component of Oplophorus luciferase in the deep-sea shrimp, Oplophorus gracilirostris (2007), Protein Expr. Purif., 56, 261-268.
    View publication on PubMed
Search for more literature for 1.13.12.13

Cloned(Commentary)

Cloned (Comment) Organism
expression of 19 kDa subunit 19kOLase in Escherichia coli Oplophorus gracilirostris

Protein Variants

Protein Variants Comment Organism
C164A mutation does not significantly affect catalytic activity of subunit kOLase Oplophorus gracilirostris
C164G mutation does not significantly affect catalytic activity of subunit kOLase Oplophorus gracilirostris
C164S mutation does not significantly affect catalytic activity of subunit kOLase Oplophorus gracilirostris

Inhibitors

Inhibitors Comment Organism Structure
Cu2+ 0.001 mM, 98% inhibition Oplophorus gracilirostris
iodoacetamide 1 mM, catalytic subunit kOLase, 50% residual activity, native enzyme, 80% residual activity Oplophorus gracilirostris
N-ethylmaleimide 0.1 mM, catalytic subunit kOLase, 1% residual activity, native enzyme, 81% residual activity Oplophorus gracilirostris

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.00004
-
 bis-deoxycoelenterazine pH 7.6, native enzymee Oplophorus gracilirostris
0.00014
-
 coelenterazine pH 7.6, native enzyme Oplophorus gracilirostris
0.0013
-
 bis-deoxycoelenterazine pH 7.6, catalytic subunit 19kOLase Oplophorus gracilirostris
0.0037
-
 coelenterazine pH 7.6, catalytic subunit 19kOLase Oplophorus gracilirostris

Localization

Localization Comment Organism GeneOntology No. Textmining
extracellular
-
 Oplophorus gracilirostris
-
-

Organism

Organism UniProt Comment Textmining
Oplophorus gracilirostris
-
-
-

Purification (Commentary)

Purification (Comment) Organism
form inclusion bodies of recombinant Escherichia coli, solubilization with 6 M urea Oplophorus gracilirostris

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
bisdeoxycoelenterazine + O2 native enzyme, 79%, catalytic subunit 19kOLase, 114% of the activity with coelenterazine, respectively Oplophorus gracilirostris oxidized bisdeoxycoelenterazine + CO2 + hnu
-
 ?
coelenterazine + O2
-
 Oplophorus gracilirostris oxidized coelenterazine + CO2 + hnu
-
 ?
f-coelenterazine + O2 native enzyme, 26%, catalytic subunit 19kOLase, 80% of the activity with coelenterazine, respectively Oplophorus gracilirostris oxidized f-coelenterazine + CO2 + hnu
-
 ?
h-coelenterazine + O2 native enzyme, 97%, catalytic subunit 19kOLase, 58% of the activity with coelenterazine, respcetively Oplophorus gracilirostris oxidized h-coelenterazine + CO2 + hnu
-
 ?
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 Oplophorus gracilirostris ?
-
 ?

Subunits

Subunits Comment Organism
More 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 Oplophorus gracilirostris