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Literature summary for 1.13.12.5 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
Search for more literature for 1.13.12.5

Cloned(Commentary)

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

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information enzyme kinetics in presence and absence of imidazolium-based ionic liquids, overview Renilla reniformis
0.0031
-
 coelenterazine pH 7.8, 25°C, recombinant His-tagged wild-type enzyme Renilla reniformis
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
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)

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 His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography Renilla reniformis

Substrates and Products (Substrate)

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

Subunits

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

General Information

General Information Comment Organism
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