Histidine substitution in the most flexible fragments of firefly luciferase modifies its thermal stability

Molecular dynamics (MD) at two temperatures of 300 and 340 K identified two histidine residues, His461 and His489, in the most flexible regions of firefly luciferase, a light emitting enzyme. We therefore designed four protein mutants H461D, H489K, H489D and H489M to investigate their enzyme kinetic...

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Veröffentlicht in:	Archives of biochemistry and biophysics 2017-09, Vol.629, p.8-18
Hauptverfasser:	Rahban, Mahdie, Salehi, Najmeh, Saboury, Ali Akbar, Hosseinkhani, Saman, Karimi-Jafari, Mohammad Hossein, Firouzi, Rohoullah, Rezaei-Ghaleh, Nasrollah, Moosavi-Movahedi, Ali Akbar
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Sequence Amino Acid Substitution Base Sequence Enzyme Stability - genetics Flexibility Histidine Hydrogen Bonding Kinetics Luciferases, Firefly - chemistry Luciferases, Firefly - genetics Luciferases, Firefly - metabolism Molecular Dynamics Simulation Mutation Protein Conformation Protein dynamics Psychrophilic enzyme Rigidity Temperature Thermostability
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