Structural analysis of aliphatic versus aromatic substrate specificity in a copper amine oxidase from hansenula polymorpha

Keyphrases

• Substrate Specificity 100%
• Quinones 100%
• Hansenula Polymorpha 100%
• Copper Amine Oxidase 100%
• Aromatic Substrates 100%
• Primary Amines 75%
• Aldehydes 50%
• Reductive Half-reaction 50%
• Channel Protein 25%
• Active Sites 25%
• Aromatic Amines 25%
• Hydrogen Peroxide 25%
• Specificity Protein 1 25%
• Carbonyl 25%
• Oxidative Deamination 25%
• X-ray Crystal Structure 25%
• Amines 25%
• Amino Acid Side Chains 25%
• Catalytic Mechanism 25%
• Schiff Base 25%
• Benzylamine 25%
• Two-electron 25%
• Aliphatic Amines 25%
• Molecular Oxygen 25%
• Initial Attack 25%
• Schiff Base Chemistry 25%
• Ethylamine 25%
• Substrate Channeling 25%
• Oxidative Half Reaction 25%
• Half Reaction 25%
• Protein-substrate Interaction 25%

Biochemistry, Genetics and Molecular Biology

• Monoamine Oxidase 100%
• Amine Oxidase 100%
• Enzyme Specificity 100%
• Ogataea angusta 100%
• Crystal Structure 50%
• X Ray 50%
• Active Site 50%
• Amino Acids 50%
• Hydrogen Peroxide 50%
• Oxidative Deamination 50%
• Catalytic Mechanism 50%
• Substrate Interaction 50%