Using peptide substrate analogs to characterize a radical intermediate in NosN catalysis

Keyphrases

• S-adenosylmethionine 100%
• Radical Intermediates 100%
• Peptide Substrate 100%
• Substrate Analog 100%
• Ring Systems 66%
• Methyl 33%
• Side Chain 33%
• Dimethyl 33%
• Methyl Groups 33%
• In Vitro Activity 33%
• Hydrogen Atom 33%
• Threonine 33%
• Electron Paramagnetic Resonance Spectroscopy 33%
• Lactones 33%
• Synthetic Approaches 33%
• Antibacterial Activity 33%
• Thioether Linkage 33%
• Radical S-adenosylmethionine Enzymes 33%
• Indolic 33%
• Trisubstituted 33%
• Methylene Group 33%
• Radical S-Adenosylmethionine 33%
• Methylase 33%
• Thiopeptide Antibiotics 33%
• Gram-positive Pathogens 33%
• Thiazole Ring 33%
• Nosiheptide 33%

Chemistry

• Cyclic Structure 100%
• EPR Spectroscopy 33%
• Methyl Group 33%
• Hydrogen Atom 33%
• Macrocycle 33%
• Thioester 33%
• Antibacterial 33%
• Methylene Group 33%
• Nosiheptide 33%
• formation 33%
• Thiazole 33%
• Lactone 33%
• Hydroxypyridine 33%
• Serine Residue 33%

Biochemistry, Genetics and Molecular Biology

• S-Adenosyl Methionine 100%
• Substrate Analog 100%
• Infectious Agent 20%
• Enzyme 20%
• Gene Linkage 20%
• Methyltransferase 20%
• Electrophilicity 20%
• Thiazole 20%
• Thioester 20%
• Serine 20%
• Threonine 20%
• Antibacterial Activity 20%