Structure-function studies of the non-heme iron active site of isopenicillin N synthase: Some implications for catalysis

Keyphrases

• Structure Function 100%
• Non-heme Iron 100%
• Isopenicillin N Synthase 100%
• Iron Active Site 100%
• Histidine 50%
• Spatial Arrangement 33%
• Active Sites 33%
• Protein-ligand 33%
• Site-directed mutagenesis 16%
• Cysteine 16%
• Asparagine 16%
• Glutamic Acid 16%
• Streptomyces 16%
• Ferrous Iron 16%
• Glutamine 16%
• Structured Support 16%
• Valine 16%
• Modified Proteins 16%
• Aspartic Acid 16%
• Active Species 16%
• Dioxygen 16%
• Spectroscopic Studies 16%
• Mutant Enzyme 16%
• Iron Atom 16%
• Ring Closure 16%
• Oxygenase 16%
• Iron Binding 16%
• Carboxylate Ligands 16%
• Iron Ligands 16%
• Iron Coordination 16%
• Aspartic Acid Residue 16%
• Non-heme 16%
• Molecular Modeling Studies 16%

Biochemistry, Genetics and Molecular Biology

• Synthase 100%
• Active Site 100%
• Histidine 50%
• Wild Type 33%
• Crystal Structure 33%
• Protein Ligand 33%
• Aspartic Acid 33%
• Site-Directed Mutagenesis 16%
• Enzyme 16%
• Crystallography 16%
• Glutamine 16%
• Molecular Model 16%
• Molecular Modeling 16%
• Cysteine 16%
• Spectroscopy 16%
• Valine 16%
• Glutamic Acid 16%
• Oxygenase 16%
• Asparagine 16%
• Streptomyces 16%

Pharmacology, Toxicology and Pharmaceutical Science

• Synthetase 100%
• Heme 100%
• Isopenicillin N 100%
• Histidine 42%
• Aspartic Acid 28%
• Protein Ligand 28%
• Glutamic Acid 14%
• Streptomyces 14%
• Carboxylate 14%
• Glutamine 14%
• Cysteine 14%
• Asparagine 14%
• Oxygenase 14%
• Ferrous Ion 14%
• Site-Directed Mutagenesis 14%
• Oxygen 14%
• Valine 14%