Publications by authors named "Marie Amano"
Article Synopsis
- l-Lysine oxidase (LysOX) is an enzyme that specifically converts l-lysine into α-keto-ε-aminocaproate, producing ammonia and hydrogen peroxide, and exhibits strict substrate specificity compared to other amino acid oxidases.
- Researchers determined the structure of LysOX with l-lysine, revealing that specific hydrogen bonding and a narrow hole in the active site are key to its strict recognition of l-lysine.
- Mutations in key residues essential for l-lysine recognition showed altered substrate specificity, providing insights into the molecular mechanisms behind LysOX's unique selectivity, and indicating potential for designing other amino acid-specific oxidases.
L-Lysine α-oxidase (LysOX) from Trichoderma viride is a homodimeric 112 kDa flavoenzyme that catalyzes the oxidative deamination of L-lysine to form α-keto-ε-aminocaproate. LysOX severely inhibited growth of cancer cells but showed relatively low cytotoxicity for normal cells. We have determined the cDNA nucleotide sequence encoding LysOX from T.
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