Copper binding by a unique family of metalloproteins is dependent on kynurenine formation

Keyphrases

• Metalloproteins 100%
• Copper Binding 100%
• Kynurenine 100%
• Copper Homeostasis 60%
• Oxidation State 20%
• High Affinity 20%
• Copper Sites 20%
• Histidine 20%
• Methionine 20%
• Genetic Context 20%
• Operon 20%
• Natural Products 20%
• Biochemical Characterization 20%
• Tryptophan 20%
• Copper Ions 20%
• Cytochrome c Peroxidase 20%
• Metabolic Enzymes 20%
• Copper Binding Site 20%
• Context-related 20%
• Diverse Roles 20%
• Diheme 20%
• Ribosomally Synthesized 20%
• Biosynthesized 20%
• Unique Fold 20%
• Neighborhood Analysis 20%
• Methane-oxidizing Bacteria 20%
• Genetic Neighborhood 20%
• Methanotrophs 20%
• Methanobactin 20%
• Methylosinus Trichosporium OB3b 20%
• Particulate Methane Monooxygenase 20%
• MauG 20%

Immunology and Microbiology

• Homeostasis 100%
• Metalloprotein 100%
• Binding Site 33%
• Crystal Structure 33%
• Operon 33%
• Methanotroph 33%
• Methylosinus trichosporium 33%
• Cytochrome 33%
• Peroxidase 33%
• Methionine 33%
• Histidine 33%
• Tryptophan 33%
• Monooxygenase 33%

Biochemistry, Genetics and Molecular Biology

• Metalloprotein 100%
• Kynurenine 100%
• Homeostasis 60%
• Genomics 40%
• Binding Site 20%
• Crystal Structure 20%
• Enzyme 20%
• Operon 20%
• Copper Ion 20%
• Cytochrome C Peroxidase 20%
• Methane Monooxygenase 20%
• Methylosinus trichosporium 20%
• Methanotroph 20%
• Histidine 20%
• Methionine 20%
• Tryptophan 20%