L6150
Lysine Oxidase from Trichoderma viride
lyophilized powder, ≥20 units/mg protein
Synonym(s):
L-Lysine:oxygen oxidoreductase (deaminating)
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About This Item
CAS Number:
UNSPSC Code:
12352204
NACRES:
NA.54
MDL number:
Product Name
Lysine Oxidase from Trichoderma viride, lyophilized powder, ≥20 units/mg protein
biological source
fungus (Trichoderma viride)
form
lyophilized powder
specific activity
≥20 units/mg protein
mol wt
112 kDa
composition
Protein, 5-20%
storage temp.
2-8°C
Quality Level
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.
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.
Other Notes
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
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
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Reza Karimi Shervedani et al.
Bioelectrochemistry (Amsterdam, Netherlands), 75(2), 124-129 (2009-04-07)
Immobilization of L-lysine alpha-oxidase on gold-mercaptopropionic acid self-assembled monolayer (Au-MPA-LOx SAM) electrode is verified experimentally in the present work. Fabrication steps and electrochemical interaction of Au-MPA-LOx with L-lysine were monitored by general electrochemical methods like cyclic voltammetry (CV) and chronoamperometry
I P Smirnova et al.
Voprosy meditsinskoi khimii, 44(4), 384-387 (1998-12-10)
L-lysin-a-oxidase (LO), a fungal enzyme catalysing oxidative deamination of L-lysin, was used for the inhibition of the reproduction of herpes simplex virus type 1 (HSV-1). Antiviral activity of LO was tested in vitro. The expression of viral antigens and CPE
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.
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
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
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