Lysine Oxidase from Trichoderma viride

• Description:

  Lysine Oxidase from Trichoderma viride_x000D_ Catalog number: B2016606_x000D_ Lot number: Batch Dependent_x000D_ Expiration Date: Batch dependent_x000D_ Amount: 10 units_x000D_ Molecular Weight or Concentration: 112 kDa_x000D_ Supplied as: Powder_x000D_ Applications: a molecular tool for various biochemical applications_x000D_ Storage: 2-8°C_x000D_ Keywords: L-Lysine:oxygen oxidoreductase (deaminating)_x000D_ Grade: Biotechnology grade. All products are highly pure. All solutions are made with Type I ultrapure water (resistivity >18 MΩ-cm) and are filtered through 0.22 um._x000D_ _x000D_ References:_x000D_ 1: Kondo H, Kitagawa M, Matsumoto Y, Saito M, Amano M, Sugiyama S, Tamura T, Kusakabe H, Inagaki K, Imada K. Structural basis of strict substrate recognition of l-lysine α-oxidase from Trichoderma viride Protein Sci. 2020 Nov;29(11):2213-2225._x000D_ 2: Kitagawa M, Ito N, Matsumoto Y, Saito M, Tamura T, Kusakabe H, Inagaki K, Imada K. Structural basis of enzyme activity regulation by the propeptide of l-lysine α-oxidase precursor from Trichoderma viride J Struct Biol X. 2021 Jan 13;5:100044._x000D_ 3: 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 α-oxidase from Trichoderma viride J Biochem. 2015 Jun;157(6):549-59._x000D_ 4: Guerrieri A, Ciriello R, Bianco G, De Gennaro F, Frascaro S. Allosteric Enzyme-Based Biosensors-Kinetic Behaviours of Immobilised L-Lysine-α-Oxidase from Trichoderma viride: pH Influence and Allosteric Properties Biosensors (Basel). 2020 Oct 17;10(10):145._x000D_ 5: Kusakabe H, Kodama K, Kuninaka A, Yoshino H, Misono H, Soda K. A new antitumor enzyme, L-lysine alpha-oxidase from Trichoderma_viride. Purification and enzymological properties J Biol Chem. 1980 Feb 10;255(3):976-81._x000D_ 6: Hanson RL, Bembenek KS, Patel RN, Szarka LJ. Transformation of N epsilon-CBZ-L-lysine to CBZ-L-oxylysine using L-amino acid oxidase from Providencia alcalifaciens and L-2-hydroxy-isocaproate dehydrogenase from Lactobacillus confusus Appl Microbiol Biotechnol. 1992 Aug;37(5):599-603._x000D_ 7: Ciriello R, De Gennaro F, Frascaro S, Guerrieri A. A novel approach for the selective analysis of l-lysine in untreated human serum by a co-crosslinked l-lysine-α-oxidase/overoxidized polypyrrole bilayer based amperometric biosensor Bioelectrochemistry. 2018 Dec;124:47-56._x000D_ 8: Khaduev SKh, Lukasheva EV, Vesa VS, OÄ­kava T, Esaki N, Soda K, Adachi O, Iagi K, Berezov TT. [A comparative study of the physico-chemical properties of lysine oxidase from Trichoderma sp. and Trichoderma_viride Y 244-2] Vopr Med Khim. 1992 May-Jun;38(3):46-8._x000D_ 9: Khaduev SKh, Zhukova OS, Dobrynin IaV, Soda K, Berezov TT. [Cytostatic effect of L-lysine-alpha-oxidase from Trichoderma harzianum Rifai and Trichoderma_viride] Biull Eksp Biol Med. 1987 Apr;103(4):458-60._x000D_ 10: Khaduev SKh, Zhukova OS, Dobrynin IaV, Soda K, Berezov TT. [Comparative study of the effect of L-lysine-L-oxidase from Trichoderma harzianum Rifai and Trichoderma viride on nucleic acid synthesis in human tumor cells in vitro] Biull Eksp Biol Med. 1986 May;101(5):603-4._x000D_ _x000D_ Products Related to Lysine Oxidase from Trichoderma viride can be found at Enzymes

• Short Description:

  Catalog Number: B2016606 (10 units)_x000D_ Lysine Oxidase from Trichoderma viride is a high quality enzyme produced by the fungus Trichoderma viride. This enzyme catalyzes the oxidation of lysine, an amino acid, to produce α-aminoadipic acid and ammonia. This product has been used as a molecular tool for various biochemical applications. It has also been used in a wide array of other chemical and immunological applications. Custom bulk amounts of this product are available upon request._x000D_ _x000D_

• Weight:

  0.15

• Length:

  2

• Width:

  0.5

• Height :

  0.5