L6150
Lysine Oxidase from Trichoderma viride
lyophilized powder, ≥20 units/mg protein
Sinonimo/i:
L-Lysine:oxygen oxidoreductase (deaminating)
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About This Item
Numero CAS:
Numero MDL:
Codice UNSPSC:
12352204
NACRES:
NA.54
Prodotti consigliati
Origine biologica
fungus (Trichoderma viride)
Livello qualitativo
Forma fisica
lyophilized powder
Attività specifica
≥20 units/mg protein
PM
112 kDa
Composizione
Protein, 5-20%
Temperatura di conservazione
2-8°C
Descrizione generale
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.
Applicazioni
Lysine Oxidase from Trichoderma viride has been used in the preparation of luminescent biochip preparation.
Azioni biochim/fisiol
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.
Definizione di unità
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.
Stato fisico
Contains phosphate buffer salts and stabilizer
Codice della classe di stoccaggio
11 - Combustible Solids
Classe di pericolosità dell'acqua (WGK)
WGK 3
Punto d’infiammabilità (°F)
Not applicable
Punto d’infiammabilità (°C)
Not applicable
Dispositivi di protezione individuale
Eyeshields, Gloves, type N95 (US)
Certificati d'analisi (COA)
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I documenti relativi ai prodotti acquistati recentemente sono disponibili nell’Archivio dei documenti.
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)
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
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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