Báo cáo khoa học: An important lysine residue in copper⁄quinone-containing amine oxidases

An important lysine residue in copper/quinone-containing amine oxidases

Authors: Anna Mura, Roberto Anedda, Francesca Pintus, Mariano Casu, Alessandra Padiglia, Giovanni Floris, and Rosaria Medda

Field: Biochemistry / Molecular Biology

Document Summary: This study investigates the interaction of xenon with copper/quinone-containing amine oxidases (Cu/TPQ AOs) from various sources, including plant, mammalian, and bacterial enzymes. Utilizing 129Xe NMR spectroscopy and optical spectroscopy, the research explores how xenon influences the activity and structure of these enzymes. The findings suggest that xenon can induce conformational changes, leading to the involvement of a lysine residue in the catalytic mechanism, particularly in plant enzymes. This lysine residue appears to play a role in the reduction of the TPQ cofactor and in modulating substrate specificity, especially for substrates with positively charged amino groups like putrescine. The study also differentiates the effects of xenon on plant versus mammalian AOs, highlighting unique responses in each category and proposing that a specific lysine residue is critical for the function and substrate recognition of plant AOs.

Detailed Table of Contents:

• An important lysine residue in copper/quinone-containing amine oxidases
• Keywords
• Correspondence
• Abstract
• Abbreviations
• Introduction
• Materials and Methods
• Results
• Discussion
• Concluding remarks
• References