EC Number   |
General Information |
Reference |
|---|
   1.13.12.5 | malfunction |
a collapse of alpha/beta hydrolase fold domain may trigger the irreversible inactivation of the enzyme at higher temperatures. In contrast to wild-type SRLuc8, the alpha-helices in the alpha/beta hydrolase fold domain of engineered C-SRLuc8 have lower perturbations and do not collapse, while some cap domain residues have more perturbations |
744428 |
| 1.13.12.5 | metabolism |
enzyme shows positive cooperativity with coelenterazine, rather due to the kinetic cooperativity conditioned by conformational changes in response to substrate binding than to the presence of two catalytic sites |
765264 |
| 1.13.12.5 | more |
architecture of the emitter site in a non-binding model, overview |
745096 |
| 1.13.12.5 | more |
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 |
745436 |
| 1.13.12.5 | more |
molecular dynamic simulation of the native RLuc based on PDB ID 2PSF, which is the crystal structure of the mutant RLuc luciferase, overview |
744813 |
| 1.13.12.5 | more |
overall structure of the MU-RLuc model involving five mutated residues, F116L, I137V, N178D, N264S and S287P, overview |
746365 |
| 1.13.12.5 | more |
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 |
744253 |
| 1.13.12.5 | physiological function |
Renilla luciferase is an enzyme that is responsible for the bioluminescence of the soft coral Renilla |
710838 |
