Mutagenesis of tryptophan199 suggests that hopping is required for MauG-dependent tryptophan tryptophylquinone biosynthesis

Biochemistry, Genetics and Molecular Biology

• Mutagenesis 100%
• Anabolism 100%
• Dehydrogenase 100%
• Oxidoreductase 100%
• Tryptophan 100%
• Electron Transport 60%
• Posttranslational Modification 20%
• Wild Type 20%
• Crystal Structure 20%
• Derived Protein 20%
• Enzyme 20%
• Protein Precursor 20%
• Heme Iron 20%

Keyphrases

• MauG 100%
• Mutagenesis 100%
• Tryptophan 100%
• Methylamine Dehydrogenase 41%
• Fe(IV) 33%
• Long-range Electron Transfer 16%
• Complex Structure 8%
• High-valent 8%
• Heme Iron 8%
• Differential Effects 8%
• Heme 8%
• Post-translational Modification 8%
• Midway 8%
• M-value 8%
• Spectroscopic Properties 8%
• Redox Properties 8%
• Electron Transfer Reaction 8%
• Redox State 8%
• Quinol 8%
• Diheme 8%
• Protein-protein Interface 8%
• Precursor Protein 8%
• Total Biosynthesis 8%
• Structured Interfaces 8%
• Biosynthetic Processes 8%
• Two-electron Oxidation 8%