3x0v | pdb_00003x0v

Structure of L-lysine oxidase

spinqualitylabelsall models 3x0v, resolution 1.90Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3x0v is a 2 chain structure with sequence from Trichoderma viride. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: EPE, FAD Activity: L-lysine oxidase, with EC number 1.4.3.14 Resources: FirstGlance, OCA, RCSB, PDBsum Publication Abstract from PubMed L-Lysine alpha-oxidase (LysOX) from Trichoderma viride is a homodimeric 112 kDa flavoenzyme that catalyzes the oxidative deamination of L-lysine to form alpha-keto-epsilon-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 A 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. Recombinant expression, molecular characterization and crystal structure of antitumor enzyme, l-lysine alpha-oxidase from Trichoderma viride.,Amano M, Mizuguchi H, Sano T, Kondo H, Shinyashiki K, Inagaki J, Tamura T, Kawaguchi T, Kusakabe H, Imada K, Inagaki K J Biochem. 2015 Feb 3. pii: mvv012. PMID:25648943 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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