Structural Characterisation of the Beta-Ketoacyl-Acyl Carrier Protein Synthases, FabF and FabH, of Yersinia pestis

• Main Authors: Nanson, J.D, Himiari, Z, Swarbrick, C.M.D, Forwood, J.K
• Other Authors: DUKE-NUS MEDICAL SCHOOL
• Format: Article
• Published: Nature Publishing Group 2020
• Subjects: 3 oxoacyl acyl carrier protein synthase; aminophenol derivative; antiinfective agent; enzyme inhibitor; platencin; polycyclic hydrocarbon; protein binding; amino acid sequence; antagonists and inhibitors; chemistry; enzyme active site; enzyme specificity; enzymology; genetics; isolation and purification; molecular docking; molecular genetics; molecular model; protein conformation; sequence alignment; structure activity relation; Yersinia pestis; 3-Oxoacyl-(Acyl-Carrier-Protein) Synthase; Amino Acid Sequence; Aminophenols; Anti-Infective Agents; Catalytic Domain; Enzyme Inhibitors; Models, Molecular; Molecular Docking Simulation; Molecular Sequence Data; Polycyclic Compounds; Protein Binding; Protein Conformation; Sequence Alignment; Structure-Activity Relationship; Substrate Specificity
• Online Access: https://scholarbank.nus.edu.sg/handle/10635/180426
• Institution: National University of Singapore

10.1038/srep14797