L6150
Lysine Oxidase from Trichoderma viride
lyophilized powder, ≥20 units/mg protein
Synonyma:
L-Lysine:oxygen oxidoreductase (deaminating)
Přihlásitk zobrazení cen stanovených pro organizaci a smluvních cen
About This Item
Číslo CAS:
MDL number:
UNSPSC Code:
12352204
NACRES:
NA.54
Doporučené produkty
biological source
fungus (Trichoderma viride)
Quality Level
form
lyophilized powder
specific activity
≥20 units/mg protein
mol wt
112 kDa
composition
Protein, 5-20%
storage temp.
2-8°C
General description
Lysine Oxidase from Trichoderma viride is a homodimeric flavoenzyme corresponding to molecular mass of 112 kDa. It is stable at 65°C and is highly specific for L-lysine substrate. It comprises FAD-binding, substrate binding and a helical domain with distinct active site funnel.
Application
Lysine Oxidase from Trichoderma viride has been used in the preparation of luminescent biochip preparation.
Biochem/physiol Actions
Lysine Oxidase from Trichoderma viride catalyzes the formation of α-keto- ε-aminocaproate by the oxidative deamination of L-lysine. It displays anti-tumor functionality in cancer leukaemic cells. It is a tumor suppressor for squamous cell, fibroblast, ovarian and gastric tumors. Lysine oxidase also plays key role in connective tissue structural integrity and embryo development.
Unit Definition
One unit will catalyze the formation of 1 μmole of 6-amino-2-oxohexanoic acid from L-lysine per min at 37°C at pH 8.0.
Physical form
Contains phosphate buffer salts and stabilizer
Storage Class
11 - Combustible Solids
wgk_germany
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
Osvědčení o analýze (COA)
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Dokumenty související s produkty, které jste v minulosti zakoupili, byly za účelem usnadnění shromážděny ve vaší Knihovně dokumentů.
J Saurina et al.
Biosensors & bioelectronics, 14(1), 67-75 (1999-02-24)
A new potentiometric method is proposed to determine lysine in pharmaceutical samples. This method is based on a lysine biosensor consisting of a chemically immobilized lysine oxidase membrane attached to an all-solid-state ammonium electrode. Lysine is degraded in the sensor
Patricia Lucas-Elío et al.
Journal of bacteriology, 188(7), 2493-2501 (2006-03-21)
Marinocine is a broad-spectrum antibacterial protein synthesized by the melanogenic marine bacterium Marinomonas mediterranea. This work describes the basis for the antibacterial activity of marinocine and the identification of the gene coding for this protein. The antibacterial activity is inhibited
Vadim S Pokrovsky et al.
Anti-cancer drugs, 24(8), 846-851 (2013-06-20)
L-Lysine α-oxidase (LO) from a novel Trichoderma strain: Trichoderma cf. aureoviride Rifai shows favorable biochemical and kinetic properties (Km for L-lysine of 17.9 µmol/l, optimum pH 8.0, high stability) and significant antiproliferative activity both in vitro and in vivo. The
E E Ferapontova et al.
Biochemistry. Biokhimiia, 66(8), 832-839 (2001-09-22)
Adsorption and bioelectrocatalytic activity of native horseradish peroxidase (HRP) and its recombinant forms on polycrystalline gold electrodes were studied. Recombinant forms of HRP were produced by a genetic engineering approach using an E. coli expression system. According to direct mass
Seiji Okazaki et al.
Journal of biochemistry, 154(3), 233-236 (2013-08-03)
We have determined the x-ray crystal structure of L-lysine ε-oxidase from Marinomonas mediterranea in its native and L-lysine-complex forms at 1.94- and 1.99-Å resolution, respectively. In the native enzyme, electron densities clearly indicate the presence of cysteine tryptophylquinone (CTQ) previously
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