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Literature summary for 1.13.12.5 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)

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

Inhibitors

Inhibitors Comment Organism Structure
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
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
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]

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

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Renilla reniformis P27652
-
-

Purification (Commentary)

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

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
coelenterazine + O2
-
Renilla reniformis coelenteramide + CO2 + hv
-
?
coelenterazine h + O2
-
Renilla reniformis coelenteramide h + CO2 + hv
-
?
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

Synonyms Comment Organism
Renilla luciferase
-
Renilla reniformis
RLuc
-
Renilla reniformis

Temperature Optimum [°C]

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

pH Optimum

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

Ki Value [mM]

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

General Information

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