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Literature summary for 1.13.12.5 extracted from

  • Kahrani, Z.F.; Ganjalikhany, M.R.; Rasa, S.M.M.; Emamzadeh, R.
    New Insights into the Molecular characteristics behind the function of Renilla luciferase (2018), J. Cell. Biochem., 119, 1780-1790 .
    View publication on PubMed
Search for more literature for 1.13.12.5

Application

Application Comment Organism
diagnostics Renilla Luciferase (RLuc) is a blue light emitter protein which can be applied as a valuable tool in medical diagnosis Renilla reniformis

Protein Variants

Protein Variants Comment Organism
additional information super RLuc8 is a Renilla luciferase variant in which 16 amino acids are substituted 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
-
 ?
coelenterazine h + O2 Renilla reniformis
-
 excited coelenteramide h monoanion + CO2
-
 ?

Organism

Organism UniProt Comment Textmining
Renilla reniformis P27652
-
-

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 excited coelenteramide h monoanion + CO2
-
 ?
coelenterazine h + O2 an induced-fit mechanism is proposed where ligand-binding induces conformational changes of the active site. Insights regarding the controversial properties and the mechanism of the reaction catalysis of Renilla luciferase and its red-shifted light emittingvariant (Super RLuc 8) Renilla reniformis excited coelenteramide h monoanion + CO2
-
 ?
coelenterazine-h + O2 substrate binding structure Renilla reniformis coelenteramide h + CO2 + hv
-
 ?

Subunits

Subunits Comment Organism
? x * 37000, SDS-PAGE and crystallization Renilla reniformis

Synonyms

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

General Information

General Information Comment Organism
additional information enzyme active site structure and ligand-receptor interactions, molecular docking. Structure analysis using crystal structure of Renilla luciferase 8 (RLuc8), a thermostable variant of RLuc, in apo-form and incomplex with its product-coelenteramide. The enzyme has a deep tunnel made up of mostly hydrophobic residues and the catalytic triad (D120, E144 and H285) is embedded at the bottom of the tunnel. Molecular dynamic simulation and molecular docking, simulation of open conformation for docking study and of of receptor-ligand complex, with ligand/substrate coelenterazine-h (ZINC2569714), after molecular docking, overview. Evaluation of the enzymes' active site in complex with coelenterazine-h. The RMSD value is moderately higher in Super RLuc8 compared with the native variant which represents the higher motion of the ligand in Super RLuc8 Renilla reniformis