QM/MM molecular modelling on mutation effect of chorismate synthase enzyme catalysis

• Published in: Journal of molecular graphics & modelling Vol. 87; pp. 250 - 256
• Main Authors: Lawan, Narin, Chasing, Pongsakorn, Santatiwongchai, Jirapat, Muangpil, Sairoong
• Format: Journal Article
• Language: English
• Published: United States Elsevier Inc 01.03.2019
• Subjects: Binding Sites; Catalysis; Catalytic Domain; Chorismate synthase mechanisms; Enzyme roles; Hydrogen Bonding; Ligands; Models, Molecular; Molecular Structure; Mutation; Phosphorus-Oxygen Lyases - chemistry; Phosphorus-Oxygen Lyases - genetics; Protein Binding; Protein Conformation; Protons; QM/MM molecular modelling and chorismate synthase mutation; Enzyme roles; QM/MM molecular modelling and chorismate synthase mutation; Chorismate synthase mechanisms

Chorismate synthase (CS) catalyzes the conversion of 5-enolpyruvylshikimate-3-phosphate (EPSP) to chorismate which is a key intermediate in the biosynthesis of aromatic amino acids. CS enzyme is a new target for antibacterial drugs. Even though several reaction mechanisms have been proposed, the cat...