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Literature summary extracted from

  • Salehi, F.; Emamzadeh, R.; Nazari, M.; Rasa, S.M.
    Probing the emitter site of Renilla luciferase using small organic molecules; an attempt to understand the molecular architecture of the emitter site (2016), Int. J. Biol. Macromol., 93, 1253-1260 .
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.13.12.5 recombinant expression of N-terminally His-tagged enzyme in Escherichia coli strain BL21(DE3) Renilla reniformis

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.13.12.5 dimethyl sulfoxide competitive inhibition at 16.6-66 mM, binding structure analysis by circular dichroism and fluorescence spectroscopy. Seven DMSO molecules interact with amino acids onthe surface of Renilla luciferase. Two of them interact with two catalytic residues (Glu144, His285), the rest of the DMSO molecules have specific interactions with the residues in the substrate binding site including Pro220, Phe180, and Phe261 Renilla reniformis
1.13.12.5 Isopropanol compatitive inhibition at 19.3-76 mM, binding structure analysis by circular dichroism and fluorescence spectroscopy. Four isopropanol molecules interact with amino acids. Most of these molecules move around the amino acidin the binding sites, and only one isopropanol molecule interacts with His285 Renilla reniformis
1.13.12.5 additional information the changes of activity of Renilla luciferase in the presence of low concentrations of small organic molecules is not associated with structural collapse or severe changes in the enzyme conformation. Molecular dynamics simulations indicate that DMSO and isopropanol, as probing molecules, aare both able to bind to the emitter site and remain with the residues of the emitter site Renilla reniformis

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.13.12.5 additional information
-
 additional information enzyme kinetics in presence of inhibitors DMSO and isopropanol, overview Renilla reniformis
1.13.12.5 0.0039
-
 coelenterazine h pH 7.8, 25°C, recombinant His-tagged enzyme Renilla reniformis

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.13.12.5 coelenterazine + O2 Renilla reniformis
-
 coelenteramide + CO2 + hv
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.13.12.5 Renilla reniformis P27652
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.13.12.5 recombinant N-terminally His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and dialysis Renilla reniformis

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.13.12.5 coelenterazine + O2
-
 Renilla reniformis coelenteramide + CO2 + hv
-
 ?
1.13.12.5 coelenterazine h + O2
-
 Renilla reniformis coelenteramide h + CO2 + hv
-
 ?
1.13.12.5 additional information substrate of Renilla luciferase, coelenterazine, is a heterocyclic imidazolo-pyrazinone, which is derivatized with (4-hydroxyphenyl)methyl (R2), 4-hydroxyphenyl (R6), and phenyl-methyl (R8) moieties Renilla reniformis ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.13.12.5 Renilla luciferase
-
 Renilla reniformis
1.13.12.5 RLuc
-
 Renilla reniformis

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.13.12.5 25
-
 assay at Renilla reniformis

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.13.12.5 7.8
-
 assay at Renilla reniformis

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
1.13.12.5 12.4
-
 Isopropanol pH 7.8, 25°C, recombinant His-tagged enzyme Renilla reniformis
1.13.12.5 15.1
-
 dimethyl sulfoxide pH 7.8, 25°C, recombinant His-tagged enzyme Renilla reniformis

General Information

EC Number General Information Comment Organism
1.13.12.5 additional information architecture of the emitter site in a non-binding model, overview Renilla reniformis