L6150
Lysine Oxidase from Trichoderma viride
lyophilized powder, ≥20 units/mg protein
Sinónimos:
L-Lysine:oxygen oxidoreductase (deaminating)
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About This Item
Número de CAS:
MDL number:
UNSPSC Code:
12352204
NACRES:
NA.54
Productos recomendados
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)
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I P Smirnova et al.
Voprosy meditsinskoi khimii, 46(4), 384-387 (2000-11-15)
The ability of protein isolated from (Trichoderma Rifai) and azydothymidine to inhibit the reproduction of HIV-virus was compared. The obtained experimental data have verified that Trichoderma Rifai protein is a promising human immunodeficiency virus (HIV) inhibitor.
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
E V Lukasheva et al.
Biochemistry. Biokhimiia, 67(10), 1152-1158 (2002-12-04)
This review summarizes data on the properties of L-lysine alpha-oxidase, an enzyme that belongs to the group of oxidases of L-amino acids. This enzyme acts virtually only on L-lysine with a rather low Km yielding alpha-keto-epsilon-aminocaproic acid. The decrease in
O S Zhukova et al.
Voprosy meditsinskoi khimii, 47(6), 588-592 (2002-04-03)
The conjugates of L-lysine alpha-oxidase and monoclonal antibodies ICO-80 towards CD-5 receptor were produced using glutaraldehyde. The cytotoxic effect of conjugates on Yurkat cells line appeared to be lower in comparison with the native enzyme. Negligible decrease of conjugate biological
Jedidah W Danson et al.
Analytical biochemistry, 303(2), 120-130 (2002-04-13)
A new assay for l-lysine alpha-oxidase is described. In this assay, the oxidized product generated from l-lysine is reacted with semicarbazide to form alpha-keto-epsilon-aminocaproate semicarbazone. Formation of the alpha-keto acid semicarbazone is continuously monitored spectrophotometrically at 248 nm (epsilon 10,160
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