The tightly bound calcium of MauG is required for tryptophan tryptophylquinone cofactor biosynthesis

Biochemistry, Genetics and Molecular Biology

• Anabolism 100%
• Tryptophan 100%
• Conformational Change 50%
• Precursor 50%
• Dehydrogenase 50%
• Hydrogen Peroxide 50%
• Oxidoreductase 50%
• Conformation 25%
• Posttranslational Modification 25%
• Crystal Structure 25%
• Absorption 25%
• Protein Secondary Structure 25%
• Derived Protein 25%
• Dissociation Constant 25%
• Enzyme 25%
• Circular Dichroism 25%

Keyphrases

• Ca2+ 100%
• MauG 100%
• Tryptophan 100%
• Cofactor Biosynthesis 100%
• Heme 16%
• Hydrogen Peroxide 16%
• Conformational Change 16%
• Methylamine Dehydrogenase 16%
• Equilibrium Studies 8%
• Post-translational Modification 8%
• Fe(IV) 8%
• Spin State 8%
• Resonance Raman Spectra 8%
• Spectral Features 8%
• Secondary Structure 8%
• Kinetic Study 8%
• Change Characteristics 8%
• Circular Dichroism Spectra 8%
• Spectral Properties 8%
• Diheme 8%
• Dehydrogenase Complex 8%
• Equilibrium Dissociation Constant 8%
• Spectral Changes 8%
• Two-step Mechanism 8%
• Domain Movement 8%
• Heme Peroxidase 8%
• Loop Movement 8%
• General Unfolding 8%