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Literature summary extracted from

  • Ghaedizadeh, S.; Emamzadeh, R.; Nazari, M.; Rasa, S.; Zarkesh-Esfahani, S.; Yousefi, M.
    Understanding the molecular behaviour of Renilla luciferase in imidazolium-based ionic liquids, a new model for the alpha/beta fold collapse (2016), Biochem. Eng. J., 105, 505-513 .
No PubMed abstract available

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.13.12.5 recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3) 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 and absence of imidazolium-based ionic liquids, overview Renilla reniformis
1.13.12.5 0.0031
-
 coelenterazine pH 7.8, 25°C, recombinant His-tagged wild-type enzyme Renilla reniformis
1.13.12.5 0.0068 0.0103 coelenterazine pH 7.8, 25°C, recombinant His-tagged wild-type enzyme in presence of 13.3-26.7 mM 1-butyl-3-methylimidazolium tetrafluoroborate Renilla reniformis
1.13.12.5 0.0097 0.0119 coelenterazine pH 7.8, 25°C, recombinant His-tagged wild-type enzyme in presence of 4.8-9.7 mM 1-butyl-3-methylimidazoliumhexafluorophosphate 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 His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography 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
-
 ?

Subunits

EC Number Subunits Comment Organism
1.13.12.5 ? x * 36000, recombinant His-tagged enzyme, SDS-PAGE 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

General Information

EC Number General Information Comment Organism
1.13.12.5 additional information the conformational changes of a main tunnel in the structure of Renilla luciferase are directly related to enzyme activity. The enzyme activity is decreased severely in the presence of ionic liquids 1-butyl-3-methylimidazolium tetrafluoroborate and 1-butyl-3-methylimidazolium hexafluorophosphate, overview. The protein-ionic liquid interactions also have impact on the structure of enzyme, where interactions of Renilla luciferase (with alpha/beta-fold) with fluorine anions causes a conformational collapse in the exposed alpha-helices. The structural distortions in Renilla luciferase in the presence of ionic liquids is started from the outer layer of the enzyme, a model which is called the alpha-shield collapse model. Molecular dynamic simulation studies, overview. The catalytic triad is formed by residues Asp120, Glu144, and His285 Renilla reniformis