3X0V

Structure of L-lysine oxidase

3X0V の概要

• エントリーDOI: 10.2210/pdb3x0v/pdb
• 分子名称: L-lysine oxidase, FLAVIN-ADENINE DINUCLEOTIDE, 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID, ... (4 entities in total)
• 機能のキーワード: oxidative deamination, secreted protein, oxidoreductase
• 由来する生物種: Trichoderma viride
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 124473.81

構造登録者

Sano, T.,Uchida, Y.,Amano, M.,Kawaguchi, T.,Kondo, H.,Inagaki, K.,Imada, K. (登録日: 2014-10-22, 公開日: 2015-04-08, 最終更新日: 2023-11-08)

主引用文献

Amano, M.,Mizuguchi, H.,Sano, T.,Kondo, H.,Shinyashiki, K.,Inagaki, J.,Tamura, T.,Kawaguchi, T.,Kusakabe, H.,Imada, K.,Inagaki, K.
Recombinant expression, molecular characterization and crystal structure of antitumor enzyme, l-lysine alpha-oxidase from Trichoderma viride.
J.Biochem., 157:549-559, 2015

PubMed Abstract: 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. viride. The full-length cDNA consists of 2,119 bp and encodes a possible signal peptide (Met1-Arg77) and the mature protein (Ala78-Ile617). The LysOX gene have been cloned and heterologously expressed in Streptomyces lividans TK24 with the enzyme activity up to 9.8 U/ml. The enzymatic properties of the purified recombinant LysOX, such as substrate specificity and thermal stability, are same as those of native LysOX. The crystal structure of LysOX at 1.9 Å resolution revealed that the overall structure is similar to that of snake venom L-amino acid oxidase (LAAO), and the residues involved in the interaction with the amino or carboxy group of the substrate are structurally conserved. However, the entrance and the inner surface structures of the funnel to the active site, as well as the residues involved in the substrate side-chain recognition, are distinct from LAAOs. These structural differences well explain the unique substrate specificity of LysOX.

PubMed: 25648943
DOI: 10.1093/jb/mvv012

実験手法

X-RAY DIFFRACTION (1.9 Å)