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L6150

Sigma-Aldrich

Lysine Oxidase from Trichoderma viride

lyophilized powder, ≥20 units/mg protein

Synonym(e):

L-Lysine:oxygen oxidoreductase (deaminating)

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About This Item

CAS-Nummer:
70132-14-8
EC-Nummer:
1.4.3.14 (BRENDA, IUBMB)
MDL-Nummer:
MFCD00131554
UNSPSC-Code:
12352204
NACRES:
NA.54

Biologische Quelle

fungus (Trichoderma viride)

Qualitätsniveau

200

Form

lyophilized powder

Spezifische Aktivität

≥20 units/mg protein

Mol-Gew.

112 kDa

Zusammensetzung

Protein, 5-20%

Lagertemp.

2-8°C

Allgemeine Beschreibung

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.

Anwendung

Lysine Oxidase from Trichoderma viride has been used in the preparation of luminescent biochip preparation.

Biochem./physiol. Wirkung

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.

Einheitendefinition

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.

Physikalische Form

Contains phosphate buffer salts and stabilizer

Lagerklassenschlüssel

11 - Combustible Solids

WGK

WGK 3

Flammpunkt (°F)

Not applicable

Flammpunkt (°C)

Not applicable

Persönliche Schutzausrüstung

Eyeshields, Gloves, type N95 (US)

Analysenzertifikate (COA)

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Die Dokumentenbibliothek aufrufen

Raluca-Ioana Stefan-van Staden et al.
Biosensors & bioelectronics, 35(1), 439-442 (2012-03-16)
An amperometric biosensor was proposed for the enantioanalysis of L-lysine. The biosensor is based on the impregnation of L-lysine oxidase in diamond paste. The potential used for the determination of l-lysine was 650 mV. The biosensor exhibited a linear concentration
Studies on Anti-Cancer Activity of Lysyl Oxidase from Trichoderma Viride MTCC 167
Kalra S, et al.
International Journal of Applied Sciences and Biotechnology, 4(1), 57-63 (2016)
Design of luminescent biochips based on enzyme, antibody, or DNA composite layers
Marquette CA, et al.
Analytical and Bioanalytical Chemistry, 377(5), 922-928 (2003)
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
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.
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