Kinetic and structural analysis of substrate specificity in two copper amine oxidases from Hansenula polymorpha

Keyphrases

• Substrate Specificity 100%
• Hansenula Polymorpha 100%
• Copper Amine Oxidase 100%
• Kcat 80%
• Benzylamine 60%
• Methylamine 40%
• Substrate Binding 40%
• Substrate-binding Pocket 40%
• Proton Loss 40%
• Substrate Channeling 40%
• Steady-state Kinetics 20%
• Active Sites 20%
• Kinetic Data 20%
• Amino Acid Variation 20%
• Catalytic Efficiency 20%
• Methyl Groups 20%
• X-ray Crystal Structure 20%
• Binding Residues 20%
• Sequence Identity 20%
• Km Value 20%
• Schiff Base 20%
• Value Differences 20%
• Energy Barrier 20%
• Funnel-shaped 20%
• Catalytic Intermediates 20%
• Substrate Entry 20%
• Side Chamber 20%
• Proton Abstraction 20%
• Substrate Size 20%
• Enzyme Substrate Specificity 20%
• Phenyl Substituent 20%

Biochemistry, Genetics and Molecular Biology

• Catalytic Efficiency 100%
• Enzyme Specificity 100%
• Ogataea angusta 100%
• Enzyme 75%
• Active Site 50%
• Crystal Structure 25%
• X Ray 25%
• Steady State 25%
• Amino Acids 25%
• Monoamine Oxidase 25%
• Amine Oxidase 25%
• Turnover Number 25%